|
Name |
Accession |
Description |
Interval |
E-value |
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
858-1938 |
0e+00 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1486.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 858 TRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 937
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 938 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDR 1017
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1018 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAK 1097
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1098 KEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1177
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1178 LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1257
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1258 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1337
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1338 TRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQR 1417
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1418 LEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALS 1497
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1498 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1577
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1578 NMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1657
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1658 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSAL 1737
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1738 LDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGS 1817
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1818 VKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1897
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 212450 1898 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276952 [Multi-domain] Cd Length: 673 Bit Score: 1443.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14920 231 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14920 311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14920 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKG 658
Cdd:cd14920 471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAFGSAYKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14920 551 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14920 631 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-781 |
0e+00 |
|
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276951 [Multi-domain] Cd Length: 662 Bit Score: 1329.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG---------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQ 337
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK-FQKP 576
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 577 RQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgldqvtgitETAFGSAYKTK 656
Cdd:cd01377 469 KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE-----------SGGGGGKKKKK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 657 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 736
Cdd:cd01377 538 GGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQ 617
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 212450 737 RYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01377 618 RYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276895 [Multi-domain] Cd Length: 676 Bit Score: 1234.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14932 235 TMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14932 315 QKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14932 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGsAYKTKKG 658
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHG-AFKTRKG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14932 554 MFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 633
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14932 634 EILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276883 [Multi-domain] Cd Length: 670 Bit Score: 1203.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14919 228 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14919 308 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14919 388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKG 658
Cdd:cd14919 468 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALPGAFKTRKG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14919 548 MFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14919 628 EILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276885 [Multi-domain] Cd Length: 673 Bit Score: 1194.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14921 231 TLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKG 658
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14921 551 MFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 630
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14921 631 EILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-781 |
0e+00 |
|
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276899 [Multi-domain] Cd Length: 675 Bit Score: 1184.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd15896 235 TMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd15896 315 QKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd15896 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITEtaFGSAYKTKKG 658
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSE--MPGAFKTRKG 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd15896 553 MFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd15896 633 EILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276876 [Multi-domain] Cd Length: 674 Bit Score: 1175.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKpRQ 578
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrIVGLDQVTgITETAFGSayKTKKG 658
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKG 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14911 552 MFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14911 632 ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276893 [Multi-domain] Cd Length: 670 Bit Score: 1138.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQE 338
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSayKTKKG 658
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGG--RPRRG 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14930 548 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14930 628 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-781 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1110.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKN 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------VGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 247 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSN-GYI 325
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 326 PIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:pfam00063 307 LCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:pfam00063 387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 566 EQGTHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGIT 645
Cdd:pfam00063 464 TFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 646 ETafgsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGF 725
Cdd:pfam00063 543 ST----PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGF 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 726 PNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:pfam00063 619 PNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-793 |
0e+00 |
|
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.
Pssm-ID: 214580 [Multi-domain] Cd Length: 677 Bit Score: 1018.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhQGELERQLLQANPILESFG 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------VGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 240 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRF 319
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 320 LSNG-YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGM 397
Cdd:smart00242 225 LNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 398 NVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFE 477
Cdd:smart00242 305 DPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 478 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDK 557
Cdd:smart00242 384 VNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 558 TFVEKLVQEQGTHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivg 637
Cdd:smart00242 461 TFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPS------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 638 ldqvtgitetafGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 717
Cdd:smart00242 534 ------------GVSNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLEN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 718 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERD 793
Cdd:smart00242 602 IRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1358 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 917.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 36 VWIPSERHGFEAASIKEERGDEVLVELA---ENGKKALVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 191 VIQYLAHVASSHkgrkdhniPPESpkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGAN 270
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 271 IETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFS 349
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 350 HDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 429
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 430 AVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 509
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 510 QREGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGTHSKFQKPRQLKDKadFCI 587
Cdd:COG5022 475 VKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 588 IHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVgldqvtgitetafgsayktKKGMFRTVGQLY 667
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------------------SKGRFPTLGSRF 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 668 KESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA-- 745
Cdd:COG5022 612 KESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKsw 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 746 --IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRGYLARKAFAKKQQQL 823
Cdd:COG5022 692 tgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRI 771
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 824 SALKILQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKqtkveaeleemerkhqqlLEEKNILA 903
Cdd:COG5022 772 KKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKT------------------IKREKKLR 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 904 EQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVeeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEK 983
Cdd:COG5022 834 ETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL-------QSAQRVELAERQLQELKIDVKSISSLKLVNLELES 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 984 VTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS--QLAEEEEKAKNLAKLKNKQEmMITDLEERLKKEEKTRQ 1061
Cdd:COG5022 907 EIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESKLKE-TSEEYEDLLKKSTILVR 985
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1062 ELEKAKRKLDG---ETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGDEEavqknnalkviRELQAQIAELQEdle 1138
Cdd:COG5022 986 EGNKANSELKNfkkELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSE-----------STELSILKPLQK--- 1050
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1139 sekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNH--EAQIQEIRQRHATALE 1216
Cdd:COG5022 1051 ----LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLvkPANVLQFIVAQMIKLN 1126
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1217 ELSEQLEQAKRFKANLEKNKQGLESDNKELACevkVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQ 1296
Cdd:COG5022 1127 LLQEISKFLSQLVNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVNDLK 1203
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1297 NELDNVSS----------LLEEAEKKGI------KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1358
Cdd:COG5022 1204 NELIALFSkifsgwprgdKLKKLISEGWvpteysTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-781 |
0e+00 |
|
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276950 [Multi-domain] Cd Length: 633 Bit Score: 867.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSS-----------SSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQD 332
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 333 KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGT 569
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 570 HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkdvdrivgldqvtgitetaf 649
Cdd:cd00124 467 HPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 650 gsayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 729
Cdd:cd00124 519 -----------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRL 581
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 212450 730 VFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd00124 582 PFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276953 [Multi-domain] Cd Length: 676 Bit Score: 787.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESpkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLAT----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14927 236 MATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQK 575
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 576 PR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKD-VDRIVGLDQVTGITETafgs 651
Cdd:cd14927 472 PRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENyVGSDSTEDPKSGVKEK---- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 652 ayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 731
Cdd:cd14927 548 --RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILY 625
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 212450 732 QEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14927 626 ADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276878 [Multi-domain] Cd Length: 668 Bit Score: 771.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKP 576
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitETAFGSAYK 654
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFATADA--------DSGKKKVAK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14913 541 KKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDF 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 735 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14913 621 KQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276874 Cd Length: 666 Bit Score: 750.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippeSPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK----------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKP 576
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 577 RQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitETAFGSAY 653
Cdd:cd14909 467 KPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQSG--------GGEQAKGG 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 KTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14909 539 RGKKGGgFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYP 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 733 EFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14909 619 DFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 738.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKP 576
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 577 RQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivgldqvtgitETAFGSAY 653
Cdd:cd14934 465 KGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKE--------------EEAPAGSK 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 KTKKGM-FRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14934 531 KQKRGSsFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYP 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 733 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14934 611 EFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-781 |
0e+00 |
|
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276831 [Multi-domain] Cd Length: 629 Bit Score: 724.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd01380 306 IVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 497 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK--FQ 574
Cdd:cd01380 386 FNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 KPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSsdkfvaelwkdvdrivgldqvtgitetafgsayK 654
Cdd:cd01380 462 KPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------K 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 TKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd01380 507 NRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEF 583
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 212450 735 RQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01380 584 FSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-781 |
0e+00 |
|
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276892 [Multi-domain] Cd Length: 662 Bit Score: 717.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASShkgrkdhnippesPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM-------------IESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQK 575
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivglDQVTGiTETAFGSAY 653
Cdd:cd14929 462 PKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFEN-------YISTD-SAIQFGEKK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14929 534 RKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYAD 613
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 734 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14929 614 FKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276881 [Multi-domain] Cd Length: 668 Bit Score: 706.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPG----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14917 153 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQK 575
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdriVGLDqvtGITETAFGsay 653
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANY---AGAD---APIEKGKG--- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 KTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14917 539 KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 618
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 212450 733 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14917 619 DFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-781 |
0e+00 |
|
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276882 [Multi-domain] Cd Length: 668 Bit Score: 692.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 181 GAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES--------GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 261 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQET 339
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 340 MEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 500 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPRQ 578
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 LKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgldqVTGITETAFGSAYKTK 656
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY--------ASAEADSGAKKGAKKK 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 657 KGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQ 736
Cdd:cd14918 543 GSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQ 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 212450 737 RYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14918 623 RYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276887 [Multi-domain] Cd Length: 671 Bit Score: 690.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKP 576
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdriVGLDQVTGITETAFGsayK 654
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNY---AGAEAGDSGGSKKGG---K 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14923 544 KKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 735 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14923 624 KQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276877 [Multi-domain] Cd Length: 673 Bit Score: 688.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPR 577
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 578 QLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitETAFGSAYK- 654
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQTAEG--------ASAGGGAKKg 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 -TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14912 544 gKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 212450 733 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14912 624 DFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276875 [Multi-domain] Cd Length: 671 Bit Score: 688.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPR 577
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 578 QLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgldqVTGITETAFGSAYKT 655
Cdd:cd14910 472 PAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGA--------AAAEAEEGGGKKGGK 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 656 KKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14910 544 KKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADF 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 735 RQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14910 624 KQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276880 [Multi-domain] Cd Length: 670 Bit Score: 687.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnippespkPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN--------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDN 335
Cdd:cd14916 154 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14916 232 LLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14916 312 EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 496 LFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQ 574
Cdd:cd14916 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 KPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdriVGLDqvTGitETAFGSA 652
Cdd:cd14916 468 KPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTY---ASAD--TG--DSGKGKG 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 653 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14916 541 GKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYG 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 212450 733 EFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14916 621 DFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-781 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 679.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQ 337
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKP 576
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgldqvTGITETAFGSAYK 654
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQ--------TAEAEGGGGKKGG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14915 543 KKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYAD 622
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 734 FRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14915 623 FKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-781 |
0e+00 |
|
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276849 [Multi-domain] Cd Length: 661 Bit Score: 649.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14883 303 NVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQK 575
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 576 PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgLDQVTGITETAFGSAYKT 655
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD----LLALTGLSISLGGDTTSR 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 656 KKGMFR-TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14883 535 GTSKGKpTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEF 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 212450 735 RQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14883 615 VDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-781 |
0e+00 |
|
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276829 Cd Length: 652 Bit Score: 648.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpVKHqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VKD------MLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQE 338
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---R 415
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd01378 306 SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 496 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGTHSKFQ 574
Cdd:cd01378 386 IFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 KPRQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgldqvtgitetafgsa 652
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 653 yKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd01378 525 -LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 733 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01378 604 KFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-781 |
0e+00 |
|
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276834 Cd Length: 647 Bit Score: 645.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQE 338
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd01383 221 LKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd01383 301 VKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 499 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRq 578
Cdd:cd01383 381 RHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 579 lkDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSayktkkg 658
Cdd:cd01383 457 --GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLFASKMLDASRKALPLTKASGSDS------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 659 MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd01383 526 QKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRY 605
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 739 EILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01383 606 GFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-781 |
0e+00 |
|
class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276832 Cd Length: 648 Bit Score: 610.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01381 222 DIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSK 572
Cdd:cd01381 382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 573 FQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkDVDRIVGLDqvtgitetafgSA 652
Cdd:cd01381 458 YLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLF-NEDISMGSE-----------TR 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 653 YKTKkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd01381 525 KKSP-----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFE 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 733 EFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01381 600 EFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-781 |
0e+00 |
|
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.
Pssm-ID: 276835 Cd Length: 647 Bit Score: 607.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS-----------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDN 335
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIK 412
Cdd:cd01384 225 YRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 413 VGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01384 304 VTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHS 571
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 572 KFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgldqvtgiteTAFGS 651
Cdd:cd01384 460 RFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLPR------------EGTSS 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 652 AYKtkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 731
Cdd:cd01384 526 SSK-----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPF 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 212450 732 QEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd01384 601 EEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-781 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 579.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQ 337
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRA 405
Cdd:cd01382 208 RMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 566 EQGTHSKFQKPRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdvdrivg 637
Cdd:cd01382 440 KHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF-------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 638 ldqvTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 717
Cdd:cd01382 512 ----ESSTNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 718 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd01382 588 LDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-781 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 573.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV- 413
Cdd:cd14872 220 EVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 573
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 574 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgLDQVTgitetafgsay 653
Cdd:cd14872 457 VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSE----GDQKT----------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 ktkkgMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14872 522 -----SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHER 596
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 212450 734 FRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14872 597 FLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-781 |
3.10e-179 |
|
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276855 [Multi-domain] Cd Length: 662 Bit Score: 559.39 E-value: 3.10e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 254 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 334 DNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 412 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQEQG 568
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASFG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 569 T-------------HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdkfvaelwkdvdri 635
Cdd:cd14890 477 RksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 636 vgldqvTGITETafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 715
Cdd:cd14890 542 ------RSIREV--------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMM 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 716 EGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14890 602 EAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-781 |
4.27e-174 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 545.50 E-value: 4.27e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnipPESPKPVkhqgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN------------QRRNNLV------TEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01387 143 FFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQ 574
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 KPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgLDQVTGITETAFGSAYK 654
Cdd:cd01387 458 KPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSH-----RAQTDKAPPRLGKGRFV 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 TKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd01387 531 TMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVF 610
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 735 RQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 781
Cdd:cd01387 611 IDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-781 |
2.21e-169 |
|
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276868 [Multi-domain] Cd Length: 658 Bit Score: 532.43 E-value: 2.21e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkpvkhqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNF 336
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGTHSKFQ 574
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 K----PRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrIVGLDQVTGITETAFG 650
Cdd:cd14903 453 DviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE---KVESPAAASTSLARGA 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 651 SAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 730
Cdd:cd14903 528 RRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLL 607
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 212450 731 FQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 781
Cdd:cd14903 608 HEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-781 |
2.26e-169 |
|
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276836 [Multi-domain] Cd Length: 690 Bit Score: 533.88 E-value: 2.26e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLahVASSHKGrkdhnippespkpvkHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---------------YGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHS 571
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 572 KFQKPrQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdriVGLDQVT----GITET 647
Cdd:cd01385 460 YYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVREL-------IGIDPVAvfrwAVLRA 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 648 AFGSAY--------------------------------KTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEK 695
Cdd:cd01385 531 FFRAMAafreagrrraqrtaghsltlhdrttksllhlhKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEK 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 696 RAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQ 775
Cdd:cd01385 609 KPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGK 684
|
....*.
gi 212450 776 SKIFFR 781
Cdd:cd01385 685 TKVFLK 690
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-779 |
5.97e-167 |
|
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276866 [Multi-domain] Cd Length: 655 Bit Score: 525.89 E-value: 5.97e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 171 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkpvkhqgeLERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------VRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYIP 326
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 327 IPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQL 484
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 485 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFV 560
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 561 EKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdvdrivgldq 640
Cdd:cd14901 464 NKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 641 vtgitetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRI 720
Cdd:cd14901 531 ---------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 721 CRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrIGQSKIF 779
Cdd:cd14901 590 SRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-743 |
3.80e-165 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 521.56 E-value: 3.80e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVT---------GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIP-- 326
Cdd:cd14888 145 LQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 327 ----------------------IPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPE 384
Cdd:cd14888 225 idmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 385 NTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG 461
Cdd:cd14888 305 ASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 462 ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGV 541
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 542 LALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS 621
Cdd:cd14888 462 FCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 622 DKFVAELWKD-VDRIVGLdqvtgitetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKL 700
Cdd:cd14888 540 NPFISNLFSAyLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLF 604
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 701 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 743
Cdd:cd14888 605 DRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-781 |
6.43e-164 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 517.43 E-value: 6.43e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSL----------KEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR- 415
Cdd:cd14873 231 REVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14873 307 EEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQ 574
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 KPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVtgitetafGSAYK 654
Cdd:cd14873 460 KPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFEHVSSRNNQDTL--------KCGSK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 655 TKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEF 734
Cdd:cd14873 530 HRR---PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDF 606
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 212450 735 RQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14873 607 YKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-781 |
2.01e-163 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 515.29 E-value: 2.01e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNippespkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN------------RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD 332
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 333 --KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAi 406
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd01379 299 LTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd01379 379 LCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 563 LvqEQGTHSKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdvdrivgldqvt 642
Cdd:cd01379 455 F--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 643 gitetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 722
Cdd:cd01379 517 -------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRR 577
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 723 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd01379 578 QGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-781 |
4.01e-159 |
|
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276862 [Multi-domain] Cd Length: 635 Bit Score: 503.84 E-value: 4.01e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD----- 332
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 333 --KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14897 223 yyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 567 QGTHSKFQKPrqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdvdrivgldqvtgite 646
Cdd:cd14897 460 CGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 647 tafgsayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 726
Cdd:cd14897 522 ------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYP 583
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 212450 727 NRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd14897 584 IRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-781 |
5.54e-158 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 501.60 E-value: 5.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQ 330
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 331 QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAI 406
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 407 LTPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIF 476
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 477 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 555
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 556 DKTFVEKLVQEQ-GTHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkdvdr 634
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 635 ivgldqvtgitetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 714
Cdd:cd14892 536 -------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGV 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 715 LEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELDPNLYRIGQSKIFFR 781
Cdd:cd14892 584 LEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-741 |
3.92e-148 |
|
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276865 Cd Length: 627 Bit Score: 473.25 E-value: 3.92e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkDHNIPPESPKPVKHQGeLERQLLQANPILESFGNAKT 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSG-IAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 244 VKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEhlksdlllegfnnyrflsng 323
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 324 yipipGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLG 396
Cdd:cd14900 214 -----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAG 472
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 473 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 552
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 553 KATDKTFVEKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSSdkfvaelwkdV 632
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------V 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 633 DrivgldqvtgitetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 712
Cdd:cd14900 508 D-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCN 561
|
650 660
....*....|....*....|....*....
gi 212450 713 GVLEGIRICRQGFPNRIVFQEFRQRYEIL 741
Cdd:cd14900 562 GVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-744 |
9.23e-146 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 467.97 E-value: 9.23e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKHQ-GELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKStKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 249 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLE----GFNNYRFLSNG 323
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 324 YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 401
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 402 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 474
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 552
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 553 KATDKTFVEKLVQEQGTHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdv 632
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF--- 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 633 drivglDQVTGITETAFGSAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 712
Cdd:cd14907 554 ------SGEDGSQQQNQSKQKKSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYL 626
|
650 660 670
....*....|....*....|....*....|..
gi 212450 713 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 744
Cdd:cd14907 627 GVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-781 |
1.34e-144 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 464.77 E-value: 1.34e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 177 TGESGAGKTENTKKVIQYLAHVAsshkgrkdhnippespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 257 RINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-- 332
Cdd:cd14889 144 QLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRev 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 333 ---KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAi 406
Cdd:cd14889 217 qywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd14889 294 LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKL 563
Cdd:cd14889 374 ACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 564 VQEQGTHSKFQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELW----KDVDRIVGLD 639
Cdd:cd14889 451 NIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFtatrSRTGTLMPRA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 640 QVTGITETAFGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIR 719
Cdd:cd14889 529 KLPQAGSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIR 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 720 ICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFFR 781
Cdd:cd14889 603 IRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-781 |
8.71e-144 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 461.82 E-value: 8.71e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 252 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 329
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 330 QQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 404
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 405 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 482
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 483 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 563 LVQEQGTHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqSSDKFvaelwkdvdrivgLDQV 641
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF-------------SDQM 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 642 TGITEtafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIC 721
Cdd:cd14891 535 QELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVL 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 722 RQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14891 585 KVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-781 |
8.58e-138 |
|
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276869 Cd Length: 653 Bit Score: 445.54 E-value: 8.58e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkpvkhqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDN 335
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14904 302 ESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGTHSK 572
Cdd:cd14904 382 KFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNES 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 573 FQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgldqvtGITETAFGSA 652
Cdd:cd14904 458 IDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE---------APSETKEGKS 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 653 YKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14904 527 GKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPK 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 212450 733 EFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 781
Cdd:cd14904 606 ELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-781 |
1.71e-137 |
|
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276861 [Multi-domain] Cd Length: 644 Bit Score: 444.22 E-value: 1.71e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkpvkhqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------RQPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQ 337
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-G 414
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14896 301 YGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 494 QQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 573
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 574 QKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDrivgldqvtgitetafgSAY 653
Cdd:cd14896 458 AKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------------PQY 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 KTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14896 519 GLGQGK-PTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQA 597
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 734 FRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14896 598 FLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-781 |
1.48e-134 |
|
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276873 [Multi-domain] Cd Length: 682 Bit Score: 437.42 E-value: 1.48e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPEspkpvkhQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-------KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGE--------HLKSDLLLEGFNNYRFL 320
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 321 SNGYIPIPGQ-QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLG 396
Cdd:cd14908 234 GQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFE 474
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 553
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 554 ATDKTFVEKLV--------QEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNMDPLNdnvatllhqssdkf 624
Cdd:cd14908 470 GSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 625 vaelwkdvdrivgldqvtgitetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 704
Cdd:cd14908 536 -----------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKR 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 705 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK-----------------GFMDGKQACERMIRALELD 767
Cdd:cd14908 586 VTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqklcvKKMCKDLVKGVLSPAMVSM 664
|
730
....*....|....*...
gi 212450 768 PNL----YRIGQSKIFFR 781
Cdd:cd14908 665 KNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-743 |
4.53e-134 |
|
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276867 [Multi-domain] Cd Length: 716 Bit Score: 437.40 E-value: 4.53e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQS---------STEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLsNGYIP-- 326
Cdd:cd14902 152 SSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPsf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 327 --IPGQQDKDN--FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNV 399
Cdd:cd14902 231 arKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 400 MEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIA 471
Cdd:cd14902 311 DKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 472 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWF 551
Cdd:cd14902 391 GFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 552 PKATDKTFVEKLVQEQGTHSKfqkprqlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkD 631
Cdd:cd14902 468 PKGSNQALSTKFYRYHGGLGQ------------FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN--------E 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 632 VDRIVGLDQVTGITETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 709
Cdd:cd14902 528 VVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQM 607
|
650 660 670
....*....|....*....|....*....|....
gi 212450 710 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 743
Cdd:cd14902 608 RSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-834 |
1.57e-131 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 433.69 E-value: 1.57e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvkhqgelERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI--------------QNAIMAANPVLEAFGNAKTIRNNNSSRFGRF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 256 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:PTZ00014 251 MQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:PTZ00014 331 FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTN 490
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITN 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 491 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTH 570
Cdd:PTZ00014 490 EMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNN 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 571 SKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGldqvtgitetafg 650
Cdd:PTZ00014 567 PKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEKG------------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 651 sayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 730
Cdd:PTZ00014 633 ---KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRT 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 731 FQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLAHLEEERDLKITDIIIFFQAVC 807
Cdd:PTZ00014 708 FAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALI 787
|
730 740
....*....|....*....|....*..
gi 212450 808 RGYLARKAFAKKqqqlsaLKILQRNCA 834
Cdd:PTZ00014 788 LKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-742 |
2.53e-131 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 428.99 E-value: 2.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 168 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvKHQGELERQLLQANPILESFGNAKTVK 245
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSK---------RRRAISGSELLSANPILESFGNARTLR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 246 NDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--NYR 318
Cdd:cd14895 146 NDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 319 FLSNG--YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD---------------QAS 381
Cdd:cd14895 226 YISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 382 MPENTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK 458
Cdd:cd14895 306 PSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 459 ----------RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPC 528
Cdd:cd14895 386 falnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 529 IDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNM 606
Cdd:cd14895 465 LEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 607 DPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITETAFGSAYKTKKGmfrtVGQLYKESLTKLMATLRNTNPNFV 686
Cdd:cd14895 541 DQPNAELFSVLGKTSDAHLRELFEFFKASESAELSLGQPKLRRRSSVLSSVG----IGSQFKQQLASLLDVVQQTQTHYI 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 687 RCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 742
Cdd:cd14895 617 RCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-779 |
1.29e-126 |
|
class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276843 Cd Length: 649 Bit Score: 413.61 E-value: 1.29e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvkhqgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI--------------QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIK 412
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 413 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTHS 571
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 572 KFqKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVdrivgldqvtgITETAfgs 651
Cdd:cd14876 459 KF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGV-----------VVEKG--- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 652 ayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVF 731
Cdd:cd14876 524 --KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPF 599
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 732 QEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 779
Cdd:cd14876 600 EEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-781 |
4.40e-125 |
|
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276837 [Multi-domain] Cd Length: 689 Bit Score: 410.93 E-value: 4.40e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPESpkpvkhqgelerqlLQA-NPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVEK--------------LNAaLTVLEAFGNVRTALNGNATRFSQLFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:cd01386 143 LDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI--------- 406
Cdd:cd01386 223 FSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 407 ---LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN---- 479
Cdd:cd01386 303 qqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 480 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALL 545
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 546 DEECWFPKATDKTFVEKLVQEQG--THSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQ 619
Cdd:cd01386 462 DEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 620 SSDKFVAelwkdvdrivgldqvtgitetafgsayKTKKGMFRTVgqlyKESLTKLMATLRNTNPNFVRCIIPNH--EKRA 697
Cdd:cd01386 542 SQKETAA---------------------------VKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDE 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 698 GK----------LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGF-----MDGKQACERMIR 762
Cdd:cd01386 591 RStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLE 670
|
730
....*....|....*....
gi 212450 763 ALELDPNLYRIGQSKIFFR 781
Cdd:cd01386 671 ELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-743 |
2.12e-118 |
|
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276846 [Multi-domain] Cd Length: 658 Bit Score: 390.75 E-value: 2.12e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 175 LCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGK 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 255 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKD 334
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 335 NFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 412 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGT 569
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 570 HSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGitetaf 649
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 650 gsaykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 729
Cdd:cd14880 538 -----QSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRV 612
|
650
....*....|....
gi 212450 730 VFQEFRQRYEILTP 743
Cdd:cd14880 613 SHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-744 |
1.25e-117 |
|
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276871 [Multi-domain] Cd Length: 715 Bit Score: 390.49 E-value: 1.25e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 177 TGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNN--------NNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 257 RINFDVTGYIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLAGAGehlKSDLLLEGFNN----YRFL---------- 320
Cdd:cd14906 153 KIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 321 ----SNGYIPIPGQQDKD-NFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---C 392
Cdd:cd14906 230 ksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 393 HLLGMNVMEFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQ 460
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 461 GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppG 540
Cdd:cd14906 390 NNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--G 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 541 VLALLDEECWFPKATDKTFVEKLVQE-QGTHSKFQkpRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQ 619
Cdd:cd14906 467 ILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 620 SSDKFVAELWKdvdrivglDQVTGITETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGK 699
Cdd:cd14906 544 SSNFLKKSLFQ--------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNN 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 212450 700 LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 744
Cdd:cd14906 610 FNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-781 |
6.48e-113 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 374.61 E-value: 6.48e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 253 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQ 331
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 332 DKDNFQETMEAMHIMgFSHDEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILT 408
Cdd:cd14886 223 DQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIIT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 409 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd14886 302 KVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVeklvq 565
Cdd:cd14886 378 INYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT----- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 566 eQGTHSKFQKPRQLKDKA---DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLdqvt 642
Cdd:cd14886 450 -SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGN---- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 643 gitetafgsayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 722
Cdd:cd14886 525 -------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIH 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 723 QGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14886 590 RGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-781 |
4.90e-112 |
|
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276842 [Multi-domain] Cd Length: 664 Bit Score: 372.61 E-value: 4.90e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnippESPKPVKHQgeLERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN-------TSQRSIADK--IDENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 256 IRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPG 329
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 330 Q--QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAIL 407
Cdd:cd14875 232 KtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 408 tprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 567 QGTHSK-FQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdrivgldqvtgit 645
Cdd:cd14875 465 WANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTL----------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 646 etafgsaYKTKKGMFR---TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 722
Cdd:cd14875 527 -------LSTEKGLARrkqTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKR 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 723 QGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSKIFFR 781
Cdd:cd14875 600 QGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-738 |
3.45e-109 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 366.34 E-value: 3.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 168 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKND 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 248 NSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-----AGEHLKSDLLLEGFNNYRFLS 321
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 322 NGYIPI--PGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ-------- 389
Cdd:cd14899 240 QSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 390 --KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT---------- 457
Cdd:cd14899 320 ftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 458 ----KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE 533
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 534 RpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLN 610
Cdd:cd14899 479 H--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 611 DNVATLLHQSSDKFVAEL-----WKDVDRIVGLDQVTGITETAFGSAYKTKkgmfrTVGQLYKESLTKLMATLRNTNPNF 685
Cdd:cd14899 557 ESAAQLLAGSSNPLIQALaagsnDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKIQLNELLSTVRATTPRY 631
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 212450 686 VRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 738
Cdd:cd14899 632 VRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-780 |
2.23e-97 |
|
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276845 [Multi-domain] Cd Length: 647 Bit Score: 329.51 E-value: 2.23e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKPVKhqgeLERQLLQANPILESFGNAKTVK 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTK----LSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 246 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNG 323
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 324 Y--IPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMN 398
Cdd:cd14879 223 HplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 399 VMEFtRAILTPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGF 473
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 474 EIF---ELNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALL 545
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGIL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 546 DEEC-WFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSS 621
Cdd:cd14879 449 DDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SP 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 622 DkFVAelwkdvdrivgldqvtgitetafgsayktkkgMFRTVGQLyKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLD 701
Cdd:cd14879 519 D-FVN--------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFD 564
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 702 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERMIRALELDPNLYRIGQSKIFF 780
Cdd:cd14879 565 KRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-781 |
2.40e-97 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 332.00 E-value: 2.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 251 RFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFlsngyipipgq 330
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 331 qDKDNFQETMEAMHIMGFSHDEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL------- 395
Cdd:cd14887 216 -DLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclss 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 396 GMNVMEFTRAILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 455
Cdd:cd14887 292 GLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 456 RTKR-------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 519
Cdd:cd14887 372 RSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 520 --DFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGTH 570
Cdd:cd14887 452 csAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 571 SKFQK--PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDKFVaelwkdvdRIVGLDQVTGIteta 648
Cdd:cd14887 532 AKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT--------RLVGSKKNSGV---- 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 649 fgSAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNR 728
Cdd:cd14887 599 --RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCR 673
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|...
gi 212450 729 IVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 781
Cdd:cd14887 674 LPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-745 |
4.45e-96 |
|
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276863 Cd Length: 578 Bit Score: 323.39 E-value: 4.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDvtGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQET 339
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 340 MEAMHIMGFSHdeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14898 210 CSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 500 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgthSKFQKPRqL 579
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 580 KDKADFCII--HYAGKVDYKADEWLMKNMDplndnvatllhqssdkfvaelwkdvdrivgldqvtGITETAFGSAYKTKK 657
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNRE-----------------------------------KGQLLIFKNLLINDE 474
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 658 GMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQR 737
Cdd:cd14898 475 GSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEER 554
|
....*...
gi 212450 738 YEILTPNA 745
Cdd:cd14898 555 YRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-781 |
1.32e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 315.99 E-value: 1.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvKHqgelerqllqANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRF--------KH----------VNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 256 IRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQ 330
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 331 QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 487
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 488 YTNEKLQQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATD 556
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 557 KTFVEKL---VQEQGTHSKFQKPRQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVA 626
Cdd:cd14878 450 PNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 627 ELwkdvdrivgldqvtgitetafgsaYKTKkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVL 706
Cdd:cd14878 530 HL------------------------FQSK---LVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVS 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 707 DQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALELDPNL--YRIGQSKIFFR 781
Cdd:cd14878 583 AQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVLQQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-781 |
3.29e-91 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 311.18 E-value: 3.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAhvasshkgrkdhnippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL-------------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 339 TMEAMHIMGFsHDEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14937 218 LMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 494 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 573
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 574 QKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRIVGLDQVTGITetafgsaY 653
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVSESLGRKNLIT-------F 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 654 KtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRIcRQGFPNRIVFQE 733
Cdd:cd14937 524 K------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDV 590
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 212450 734 FRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 781
Cdd:cd14937 591 FLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-733 |
1.92e-80 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 281.02 E-value: 1.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT-------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 251 RFGKFIRINFD---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-AGEHLKSDLLLEGFNNYRFL 320
Cdd:cd14884 144 RCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 321 --------------------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKkerntdqa 380
Cdd:cd14884 224 npdeshqkrsvkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 381 smpentvaqKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ 460
Cdd:cd14884 296 ---------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 461 GA-----------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCI 529
Cdd:cd14884 367 DEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 530 DLIERpanppgVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGTHSK-FQKPR--------QLKDKADFCIIHY 590
Cdd:cd14884 446 IFIAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 591 AGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdvdrivgldqvtgitetafgSAYKTKKGMFRTVGQLYKES 670
Cdd:cd14884 520 AGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE-----------------------ANNGGNKGNFLSVSKKYIKE 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 671 LTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQE 733
Cdd:cd14884 577 LDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-768 |
2.39e-78 |
|
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276847 [Multi-domain] Cd Length: 633 Bit Score: 273.53 E-value: 2.39e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpKPVKHqgelerqLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET-DAFKH-------LAAAFTVLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 253 GKFIRINFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQ 330
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 331 QDKDNFQETMEAMHIMGFshdEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiL 407
Cdd:cd14881 212 EDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 408 TPRIK-VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFEL 478
Cdd:cd14881 284 TTRTHnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 479 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDK 557
Cdd:cd14881 360 SQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 558 TFVEKLVQEQGTHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdkfvaelwkdvdrivg 637
Cdd:cd14881 436 SYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 638 ldqvtgiteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 717
Cdd:cd14881 499 ---------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLET 560
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 212450 718 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 768
Cdd:cd14881 561 VNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-746 |
2.56e-73 |
|
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276841 [Multi-domain] Cd Length: 628 Bit Score: 258.65 E-value: 2.56e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 178 GESGAGKTENTKKVIQYLAHvasshkgrkdhniPPESPKPVKHQGELERqllqanpILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------QPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDvTGYIVGANIE-TYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14874 131 LLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14874 210 KHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 414 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 494 QQLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK 572
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 573 FQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdvdrivgldqvtgitetaFGSA 652
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLL--------------------FESY 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 653 YKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 732
Cdd:cd14874 500 SSNTSDMIVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKT 579
|
650
....*....|....
gi 212450 733 EFRQRYEILTPNAI 746
Cdd:cd14874 580 TFARQYRCLLPGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-781 |
3.23e-69 |
|
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276870 Cd Length: 673 Bit Score: 247.70 E-value: 3.23e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnippespkpvkhqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNF 336
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 417 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 497 FNHTMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF-Q 574
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 575 KPRQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKF-------------VAELWKDVD-------- 633
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYlfsrdgvfninatVAELNQMFDakntakks 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 634 --RIVGL---------DQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAGKL 700
Cdd:cd14905 514 plSIVKVllscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTF 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 701 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSKIF 779
Cdd:cd14905 594 DVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTKIF 671
|
..
gi 212450 780 FR 781
Cdd:cd14905 672 LR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-780 |
7.75e-69 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 248.35 E-value: 7.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDhnipPESPKPVKHqgELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD----SEGASGVLH--PIGQQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgEH---LKSDLLL-EGFNNYRFLSNGyIPI 327
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 328 PGQ--QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------L 395
Cdd:cd14893 236 ATNfaLDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 396 GMNVMEFTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG- 461
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 462 ---ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCI 529
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 530 DLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD------------FCIIHYAGKVDYK 597
Cdd:cd14893 476 QLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 598 ADEWLMKNMDPLNDNVATLLHQSSDKfvaelwkdVDRIVGLDQVT--------------GITETAFG----SAYKTKKGM 659
Cdd:cd14893 554 GKGLSSKNMLSISSTCAAIMQSSKNA--------VLHAVGAAQMAaassekaakqteerGSTSSKFRksasSARESKNIT 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 660 FRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYe 739
Cdd:cd14893 626 DSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY- 703
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 212450 740 iltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 780
Cdd:cd14893 704 --------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-741 |
1.17e-62 |
|
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276848 Cd Length: 642 Bit Score: 227.32 E-value: 1.17e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG-------------------ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG------ 329
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 330 ----QQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14882 219 rddpEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNS 480
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 481 FEQLCINYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDK 557
Cdd:cd14882 374 LEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 558 TFVEKLVQEQgtHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDvdrivg 637
Cdd:cd14882 446 NYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN------ 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 638 lDQVTGItetafgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 714
Cdd:cd14882 515 -SQVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDLEYKPRGFHSEVVRQQMRALAV 578
|
650 660
....*....|....*....|....*..
gi 212450 715 LEGIRICRQGFPNRIVFQEFRQRYEIL 741
Cdd:cd14882 579 LDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-779 |
1.48e-60 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 222.79 E-value: 1.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 179 ESGAGKTENTKKVIQYLAHVA--SSHKGRKDHNIPPESPKPV---KHQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgSRRLPTNLNDQEEDNIHNEentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 254 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 334 DNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 387
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 388 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 464
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 465 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 544
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 545 LDEECWFPKATDKTFVEKL-VQEQGTHSKF-QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 622
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSiIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 623 KFVAELWKDVDrivgLDQVTGITET----AFGSAYKTKKGMFRTVGQ----LYKESLTKLMATLRNTNPNFVRCIIPNHE 694
Cdd:cd14938 558 EYMRQFCMFYN----YDNSGNIVEEkrrySIQSALKLFKRRYDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNES 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 695 KRA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERMIRALELDPNLYRI 773
Cdd:cd14938 634 KRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNYEWMI 705
|
....*.
gi 212450 774 GQSKIF 779
Cdd:cd14938 706 GNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-265 |
6.46e-60 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 203.35 E-value: 6.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 200 SSHKGRKDHNIppeSPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 265
Cdd:cd01363 81 FNGINKGETEG---WVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1026-1871 |
3.31e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 147.51 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1026 AEEEEKAKNL-AKLKNKQ-EMMITDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQ 1103
Cdd:TIGR02168 209 AEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1104 AALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKRE 1183
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1184 QEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDNkelacevkvlqqvkaeSEHK 1263
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI----------------EELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1264 RKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEetrqKLN 1343
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1344 LSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVdddlgtiegLEENKKKLLKDMESLSQRLEEKAM 1423
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV---------VVENLNAAKKAIAFLKQNELGRVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1424 AYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAeekNISARYAEERDRAEAEAREKETKAL------- 1496
Cdd:TIGR02168 575 FLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNALELAKKLRPGyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1497 --------SLARALEEALEAKEEFERQNKQLRADMEdlmsskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQAT 1568
Cdd:TIGR02168 652 gdlvrpggVITGGSAKTNSSILERRREIEELEEKIE--------------ELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1569 EDAKLRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANK 1648
Cdd:TIGR02168 718 RKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1649 ARDEAIKQLRKLQAQ--------------MKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR 1714
Cdd:TIGR02168 797 ELKALREALDELRAEltllneeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1715 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSA----- 1789
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleea 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1790 ---AQKSENARQQLERQNKELKAKLQELeGSVK----SKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLK 1862
Cdd:TIGR02168 957 ealENKIEDDEEEARRRLKRLENKIKEL-GPVNlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
....*....
gi 212450 1863 EVFMQVEDE 1871
Cdd:TIGR02168 1036 DTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1130-1845 |
5.03e-34 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 143.66 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1130 IAELQEDLESEKASRNKAEKQKrDLSEELEALKTELEdTLDTTAAQQELRTKREQEvaelkkaieeetknheAQIQEIRQ 1209
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1210 RHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELA 1289
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1290 EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR 1369
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1370 KNLEKQMLALQAQLAEAKKK-VDDDLGTIEGLEENKKKLLKDM----ESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMV 1444
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLeealEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1445 DLDHQRQI---VSNLEKKQKKF--------DQMLAEEKNISARYAEERDRAEAEAREKETKAL----SLARALEEALEAK 1509
Cdd:TIGR02168 497 LQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaiaFLKQNELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1510 EEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKL---------------- 1573
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1574 --------RLEVNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE 1644
Cdd:TIGR02168 657 pggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1645 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1724
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1725 DEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGE--------------RSAA 1790
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerasleealallRSEL 896
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1791 QKSENARQQLERQNKELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAK 1845
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
987-1868 |
1.36e-32 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 139.05 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 987 EAKIKKMEEEIllleDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEmmitDLEERLKKEEKtrQELEKA 1066
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1067 KRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV-IRELQAQIAELQEDLESEKASRN 1145
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1146 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtknhEAQIQEIRQRHATALEELS---EQL 1222
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1223 EQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNV 1302
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1303 SSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLQEQQEEEEEARKN---L 1372
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNRLNnvvV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1373 EKQMLALQA-QLAEAKKkvdddLGTIEGLEENKkklLKDMESLSQRLEEKA---MAYDKLE---KTKNRLQQELDDLMV- 1444
Cdd:TIGR02169 555 EDDAVAKEAiELLKRRK-----AGRATFLPLNK---MRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVv 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1445 -DLDHQRQIVSN----------LEKKQKKFDQMLAEEKNISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFE 1513
Cdd:TIGR02169 627 eDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1514 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQAR 1593
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1594 DEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1673
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1674 ARASRDEIFAQSKESEKKLKGLEAEILQLQEEfaaserarrhaeqeRDELADEIansasgkSALLDEKRRLEARIAQLEE 1753
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKE--------------RDELEAQL-------RELERKIEELEAQIEKKRK 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1754 ELEEEQSNMELLNERfrkttlqvdtlNSELAGERSAAQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATISTLEA 1831
Cdd:TIGR02169 918 RLSELKAKLEALEEE-----------LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLK 986
|
890 900 910
....*....|....*....|....*....|....*..
gi 212450 1832 KIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQV 1868
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1195-1944 |
1.67e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 132.10 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1195 EETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LESDNKELACEVKVLQQVKAESEHKRKKLDAQ 1270
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1271 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1350
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1351 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEkamaydkLEK 1430
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1431 TKNRLQQElddlmvdldhQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKE 1510
Cdd:TIGR02168 415 RRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1511 EFERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRTLEQQV----------EEMRTQLEE-LEDELQA-----TEDAKLR 1574
Cdd:TIGR02168 485 AQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAaLGGRLQAvvvenLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1575 LE---------VNMQAMKAQFERDLQARDEQNEEKKRM-------LVKQVRELEAELED--------ERKQRALAVAAKK 1630
Cdd:TIGR02168 562 IAflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGflgvakdLVKFDPKLRKALSYllggvlvvDDLDNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1631 KMEMDLKDLEGQ-------------------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1685
Cdd:TIGR02168 642 RPGYRIVTLDGDlvrpggvitggsaktnssilerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1686 KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1765
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1766 NERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkFKATISTLEAKIAQLEEQLEQEAK 1845
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1846 ERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA---- 1920
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAeale 960
|
810 820
....*....|....*....|....*..
gi 212450 1921 ---TEANEGLSREVSTLKNRLRRGGPI 1944
Cdd:TIGR02168 961 nkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1064-1750 |
7.98e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 7.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1064 EKAKRKLDGETTDL---QDQIAELQAQIEELKIQ--LAKKEEELQAALARGDEEAvqknnALKVIRELQAQIAELQEDLE 1138
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPLERQaeKAERYRELKEELKELEAEL-----LLLKLRELEAELEELEAELE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1139 SEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEvAELKKAIEEETKNHEAQIQEIRQRhATALEEL 1218
Cdd:COG1196 250 ELEAELEELEAELAELEAELEELRLELE------ELELELEEAQAEE-YELLAELARLEQDIARLEERRREL-EERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1219 SEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1298
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1299 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1378
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1379 LQAQLAEAKKKvdddlgtieglEENKKKLLKDMESLSQRLEEKamaydKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEk 1458
Cdd:COG1196 482 LLEELAEAAAR-----------LLLLLEAEADYEGFLEGVKAA-----LLLAGLRGLAGAVAVLIGVEAAYEAALEAAL- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1459 kqkkfdqMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRA-DMEDLMSSKDDVGKNV 1537
Cdd:COG1196 545 -------AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAvDLVASDLREADARYYV 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1538 HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1617
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1618 ERKQRALAVAAKKkmEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSkESEKKLKGLEA 1697
Cdd:COG1196 698 ALLAEEEEERELA--EAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE-ELERELERLER 774
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1698 EILQLQ-------EEFAAserarrhAEQERDELADEIANsasgksaLLDEKRRLEARIAQ 1750
Cdd:COG1196 775 EIEALGpvnllaiEEYEE-------LEERYDFLSEQRED-------LEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1633 |
2.77e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 128.25 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 859 RQEEELQakdeeLMKVKEKQTKVEAELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKK-QELEEILHDL 937
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLRlEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 938 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDR 1017
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1018 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAK 1097
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1098 KEEELQAALARGDE-----EAVQKNNALKVIRELQAQIAELQ---EDLESEKASRNKAEKQKRDLSEELEALKTELEDTL 1169
Cdd:TIGR02168 405 LEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEeelEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1170 DTTAAQQELRTKREQEVAELKKAIEEETKNHE---------AQIQEIRQRHATALEE---------LSEQLEQAKRFKAN 1231
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1232 LEKNKQG--------------LESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKV------TEGERLRVELAE- 1290
Cdd:TIGR02168 565 LKQNELGrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddlDNALELAKKLRPg 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1291 -------------------KANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1351
Cdd:TIGR02168 645 yrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1352 EEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKT 1431
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1432 KNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEE 1511
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1512 FERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVNMQAMKAQF 1586
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEEAEALENKIE 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1587 ERDLQARDEQNEEKKR---------MLVKQVRELEAELEDERKQRALAVAAKKKME 1633
Cdd:TIGR02168 965 DDEEEARRRLKRLENKikelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
854-1729 |
3.69e-28 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 124.40 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 854 LLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFaeaeemrarlaakkQELEEI 933
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL--------------YALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 934 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQldeeegaRQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKL 1013
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESK-------LDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1014 MEDRIAECtsqlaeeeekaknlaklknkqemmitdleerlkkeektRQELEKAKRKLDgettDLQDQIAELQAQIEELKI 1093
Cdd:TIGR02168 370 LESRLEEL--------------------------------------EEQLETLRSKVA----QLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1094 QLakkeEELQAALARGDEEAVQKNNALKvirelQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttA 1173
Cdd:TIGR02168 408 RL----ERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELREELE------E 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1174 AQQELRTKREQevaelkkaiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNK-ELACE--- 1249
Cdd:TIGR02168 473 AEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaal 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1250 --------VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK--KGIKFAKD 1319
Cdd:TIGR02168 544 ggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1320 AASLESQLQDTQELlqeetRQKLNLSSRIRQLEEEK-----------NNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1388
Cdd:TIGR02168 624 GVLVVDDLDNALEL-----AKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1389 KVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQML 1467
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1468 AEEKNIsaryaeERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadMEDLMSSKDDVGKNVHELEKSKRTL 1547
Cdd:TIGR02168 779 EAEAEI------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--LESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1548 EQQVEEMRTQLEELEDELQATEDAklrLEVNMQAMKAQFERDLQARDEQNEekkrmLVKQVRELEAELEDERKQRALAVA 1627
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESE---LEALLNERASLEEALALLRSELEE-----LSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1628 AKKKMEMDLKDLEGQIEaankardeaikqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQL----- 1702
Cdd:TIGR02168 923 KLAQLELRLEGLEVRID-------------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnl 989
|
890 900
....*....|....*....|....*....
gi 212450 1703 --QEEFAASERARRHAEQERDELADEIAN 1729
Cdd:TIGR02168 990 aaIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
817-1459 |
3.20e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.20 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 817 AKKQQQLSA-LKILQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQL 895
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 896 LEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdlesrveeeeeRNQILQNEKKKMQGHIQDLEEQLDEEEGA 975
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------------RLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 976 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK 1055
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1056 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE 1135
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1136 DLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATAL 1215
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1216 EELSEQLEQAKRFKANLeknkqGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKL 1295
Cdd:COG1196 586 AALAAALARGAIGAAVD-----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1296 QNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQ 1375
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1376 MLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLS---QR-LEEkamaYDKLEKTKNRLQQELDDLMVDLDHQRQ 1451
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGpvnLLaIEE----YEELEERYDFLSEQREDLEEARETLEE 816
|
....*...
gi 212450 1452 IVSNLEKK 1459
Cdd:COG1196 817 AIEEIDRE 824
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
856-1554 |
3.89e-27 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 120.93 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 935
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 936 DLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ-----LEKVTAEAKIKKMEEEILLLEDQNSKFLKE 1010
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1011 KKLMEDRIAECTSQLAEEEEK----AKNLAKLKNKQEMMiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI---AE 1083
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQAldaaERELAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1084 LQAQIEelkiqlAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE----DLESEKASRNKAEKQKRDLSEELE 1159
Cdd:TIGR02168 535 YEAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLV 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1160 ALKTELEDTLD------------TTAAQQELRTKREQEVAELKK-------AIEEETKNHEAQIQEIRQRhataLEELSE 1220
Cdd:TIGR02168 609 KFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGdlvrpggVITGGSAKTNSSILERRRE----IEELEE 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1221 QLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELD 1300
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1301 NVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQ 1380
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1381 AQLAEAKKKVDDDLGTIEGLEENK-------KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIV 1453
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIeeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1454 SNLEKKQKKFDQMLAE-EKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDD 1532
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDF 1004
|
730 740
....*....|....*....|..
gi 212450 1533 VGKNVHELEKSKRTLEQQVEEM 1554
Cdd:TIGR02168 1005 LTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
869-1750 |
9.96e-27 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 119.79 E-value: 9.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 869 EELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 948
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 949 QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIllledqnskflkeKKLMEDRIAECTSQLAEE 1028
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI-------------KDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1029 EEKAKNLaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALAR 1108
Cdd:TIGR02169 300 EAEIASL-------ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1109 GDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1188
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1189 LKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLqqvkaesEHKRKKLD 1268
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEE-YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1269 AQVQELtAKVTEGERLRVELAekankLQNELDNVSSLLEEAEKKGIKFAKdaaslESQLQDTQELLQEETRQKLNLSSRI 1348
Cdd:TIGR02169 525 GTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1349 R------------QLEEEKNNLQEQQEEEEEARKNLEK--------QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLL 1408
Cdd:TIGR02169 594 SedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAarrlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1409 KDMESLSQRLEEkamaydkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNISARYAEERDRA 1484
Cdd:TIGR02169 674 AELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1485 EAEAREKETKALSLARaleeALEAKEEFERQNKQLRADMEDLMSSKDDVGknVHELEKSKRTLEQQVEEMRTQLEELEDE 1564
Cdd:TIGR02169 747 SSLEQEIENVKSELKE----LEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1565 LQATEDAKLRLEVNMQAMKAQfERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE 1644
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1645 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKGLEAEILQLQEEFAASERARRHAEQ 1718
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
890 900 910
....*....|....*....|....*....|..
gi 212450 1719 ERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
228-722 |
2.43e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 117.92 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 228 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHIFYQ 296
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 297 LLAGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHDEILSMLKVVS 361
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 362 SVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVEALA 435
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 436 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQlfnh 499
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYA---- 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 500 tmfileqEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATD----------KTFVEKLVQEQGt 569
Cdd:cd14894 565 -------REEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNS- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 570 hSKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDVDRivgL 638
Cdd:cd14894 637 -SRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ---L 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 639 DQVTGITETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGI 718
Cdd:cd14894 713 GWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQM 791
|
....
gi 212450 719 RICR 722
Cdd:cd14894 792 EICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1107-1927 |
7.30e-26 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 117.09 E-value: 7.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1107 ARGDEEAVQKNnalkvIRELQAQIAELQEDLESEKASRNKAEKQKrDLSEELEalktELEDTLdTTAAQQELRTKREQEV 1186
Cdd:TIGR02169 175 ALEELEEVEEN-----IERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKR----EYEGYE-LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1187 AELKkAIEEETKNHEAQIQEIRQRHATALEELSEQleqAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKK 1266
Cdd:TIGR02169 244 RQLA-SLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1267 LDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSS 1346
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1347 RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYD 1426
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1427 KLEKTKNRLQQELDdlmvDLDHQRQIVSNLEKKQKKFDQMLaeEKNISARYAEERDRAEAEarEKETKALSLAraleeal 1506
Cdd:TIGR02169 480 RVEKELSKLQRELA----EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA------- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1507 eakeeferqnkqLRADMEDLMSSKDDVGKNVHELEKSK---RTLEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMK 1583
Cdd:TIGR02169 545 ------------AGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1584 AQFERDLQ--ARDE---QNEEKKRMLVKQVR--ELEAELEDE--------RKQRALAVAAKKKMEmDLKDLEGQIEAANK 1648
Cdd:TIGR02169 610 PKYEPAFKyvFGDTlvvEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1649 ARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIA 1728
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1729 NSASGKSALLDEKRRLEARIAQLEEELEEEQsnMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELK 1808
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1809 AKLQELEGSV------KSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQM 1882
Cdd:TIGR02169 847 EQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 212450 1883 EKANARMKQLKRqLEEAEEEATRANASRRKLQRELDDATEANEGL 1927
Cdd:TIGR02169 927 EALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
854-1716 |
1.44e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 115.94 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 854 LLQVTRQEEELQAKDEElmkVKEKQTKVEAELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 931
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 932 EILHDLESRVEEEEERNQILQNEKKKMqghiqdleEQLDEEEGARQKLQLEKVTAEakIKKMEEEILLLEDQNSKFLKEK 1011
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI--------KDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1012 KLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEEL 1091
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1092 KIQLAKKEEELQaalaRGDEEAVQKNNALKVIRE-----------LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1160
Cdd:TIGR02169 405 KRELDRLQEELQ----RLSEELADLNAAIAGIEAkineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1161 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE------AQIQEIRQRHATALEELS--------------- 1219
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvAQLGSVGERYATAIEVAAgnrlnnvvveddava 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1220 -EQLEQAKRFKAN----LEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELtakvteGERLRVELAEKANK 1294
Cdd:TIGR02169 561 kEAIELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1295 LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNNLQEQqeeeeeaRKNLEK 1374
Cdd:TIGR02169 635 LMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1375 QMLALQAQLAEAKKKvdddlgtIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1454
Cdd:TIGR02169 703 RLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1455 NLEKKQKKFDQMLAEEKNISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1534
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1535 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQARDEQNEEKKRMLVKQVRELEAE 1614
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1615 LEDERKQRALAVAAKKKMEMDLKDLEGQIeAANKARDEAIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKE 1687
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDE 990
|
890 900
....*....|....*....|....*....
gi 212450 1688 SEKKLKGLEAEILQLQEEFAASERARRHA 1716
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
921-1622 |
3.01e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.65 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 921 ARLAAKKQELEEILHDLESrveeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLL 1000
Cdd:COG1196 209 AEKAERYRELKEELKELEA---------ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1001 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRkldgettDLQDQ 1080
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE-------EAEEE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1160
Cdd:COG1196 353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1161 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQrhataLEELSEQLEQAKRFKANLEKNKQGLE 1240
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE-----LLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1241 SDNKELacevkvlqqvkaeseHKRKKLDAQVQELTAKVTEGERLRVELAEkanKLQNELDNVSSLLEEAEKKGIKFAKDA 1320
Cdd:COG1196 508 EGVKAA---------------LLLAGLRGLAGAVAVLIGVEAAYEAALEA---ALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1321 ASLEsqlqDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKkkvDDDLGTIEGL 1400
Cdd:COG1196 570 KAGR----ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARL---EAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1401 EENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRqivsnlekkqkkfdqmLAEEKNISARYAEE 1480
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEE----------------LELEEALLAEEEEE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1481 RDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelEKSKRTLEQQVEEMRTQLEE 1560
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE--------PPDLEELERELERLEREIEA 778
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1561 LEDelqatedaklrleVNMQAMkAQFERdLQARDEQNEEKKRMLVKQVRELE---AELEDERKQR 1622
Cdd:COG1196 779 LGP-------------VNLLAI-EEYEE-LEERYDFLSEQREDLEEARETLEeaiEEIDRETRER 828
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1331-1896 |
6.93e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.49 E-value: 6.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1331 QELLQEETRQKLNLSS-RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLK 1409
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1410 DMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAR 1489
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1490 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1569
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1570 DAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRAlAVAAKKKMEMDLKDLEGQIEAANKA 1649
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG-VKAALLLAGLRGLAGAVAVLIGVEA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1650 RDEAIKQLRkLQAQMKDYQRELEEARasrdeifAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN 1729
Cdd:COG1196 535 AYEAALEAA-LAAALQNIVVEDDEVA-------AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1730 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKA 1809
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1810 KLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQM---EKAN 1886
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdlEELE 766
|
570
....*....|
gi 212450 1887 ARMKQLKRQL 1896
Cdd:COG1196 767 RELERLEREI 776
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1116-1949 |
1.96e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 112.13 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1116 KNNALKVIRELQAQIAELQEDLESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1195
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1196 ETKNHEAQiqeiRQRHATALEELSEQLEQAKRFKANLEKNKQGLESD--NKELACEVKVLQQVKAESEHKR--------- 1264
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTMHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1265 -KKLDAQVQELTAKVTEGE-RLRVELAEKANK----LQNELDNVSSLLEEAEKKGIKFAKDAASLESQ---LQDTQELLQ 1335
Cdd:pfam15921 226 lRELDTEISYLKGRIFPVEdQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1336 EETRQKLnlSSRIRQLEEeknnlqeqqeeeeearknLEKQMLALQAQLAEAKKKVDDDLgtieglEENKKKLLKDMESLS 1415
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYEDKI------EELEKQLVLANSELT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1416 QRLEEKamayDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKNISARYAEERDR-AEAEAREKE 1492
Cdd:pfam15921 360 EARTER----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1493 TKALSlARALEEALEAKEEFERQNKQLR---ADMEDLMSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQ 1566
Cdd:pfam15921 435 LKAMK-SECQGQMERQMAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1567 AT--EDAKLRLEVNMQAMKAQFERdlqardeqNEEKkrmlvkQVRELEAELEDERKQRAlavAAKKKMEMDLKDLEGQIE 1644
Cdd:pfam15921 514 ATnaEITKLRSRVDLKLQELQHLK--------NEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1645 -AANKARDEAIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERD 1721
Cdd:pfam15921 577 lVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1722 ELADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNERFRKTTLQVDTLNSELAGERSAAQ----KSENAR 1797
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETTTNKLKMQLKSAQseleQTRNTL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1798 QQLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERaaanKLVRRTEKKLKEVFMQVEDERrhaDQ 1877
Cdd:pfam15921 716 KSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEK---NK 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1878 YKEQMEKANARMKQLKRQLEEAEEEATRAN----------------ASRRKLQRELDDATEANEGLSREvSTLKNRLRRG 1941
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASlqfaecqdiiqrqeqeSVRLKLQHTLDVKELQGPGYTSN-SSMKPRLLQP 866
|
....*...
gi 212450 1942 GPITFSSS 1949
Cdd:pfam15921 867 ASFTRTHS 874
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
976-1565 |
8.60e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 106.69 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 976 RQKLQLEKV-TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLK 1054
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1055 KEEKTRQELEKAKR---KLDGETTDLQDQIAELQAQIEELKiqlaKKEEELQAALARgdeeavqknnaLKVIRELQAQIA 1131
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1132 ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ---EVAELKKAIE--EETKNHEAQIQE 1206
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1207 IRQRHA-TALEELSEQLEQAKRFKANLEKN-------KQGLESDNKELACEVKVLQQVKAE--------SEHKRKKLdaq 1270
Cdd:PRK03918 377 LKKRLTgLTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKEL--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1271 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK--KGIKFAKDAASLESQLQD-TQELLQEETRQKLNLSSR 1347
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1348 IRQLEEEKNNLQEQQEEEeearKNLEKQMLALQAQLAEAKKKVDDDLGTiegLEENKKKLLKDMESLSQRLEEKAMAYDK 1427
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELEPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1428 LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEErdraeaEAREKETKALSLARALEEALE 1507
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRA 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1508 AKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1565
Cdd:PRK03918 681 ELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1324-1940 |
4.58e-21 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 101.02 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1324 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEeeeeARKNLEKQMLALQAQLAEAKKKVDDDLGTIE----- 1398
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILHELEsrlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1399 ------GLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEekn 1472
Cdd:pfam01576 87 eeersqQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1473 isaryaeerdrAEAEAREKETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRTLEQQVE 1552
Cdd:pfam01576 164 -----------FTSNLAEEEEKAKSLSKLKN-----------KHEAMISDLEERLKKEE---KGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1553 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKM 1632
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1633 EMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASER 1711
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1712 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQ 1791
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1792 KSENARQQLERQNKELKAKLQElEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDE 1871
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1872 RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
857-1744 |
1.07e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 100.05 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 857 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 936
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 937 LESRVEEEEERNQILQNEKKKMQGHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1016
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1017 RIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKrkldgetTDLQDQIAELQAQIEELKIQLA 1096
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE-------EELEKLQEKLEQLEEELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1097 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqQ 1176
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1177 ELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQV 1256
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1257 KAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQE 1336
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1337 ETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQ 1416
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1417 RLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKnisaryaeerdrAEAEAREKETKAL 1496
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1497 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE 1576
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1577 VNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1655
Cdd:pfam02463 845 EQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1656 QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERD-----ELADEIANS 1730
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYnkdelEKERLEEEK 1004
|
890
....*....|....
gi 212450 1731 ASGKSALLDEKRRL 1744
Cdd:pfam02463 1005 KKLIRAIIEETCQR 1018
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1730 |
4.04e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 98.29 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 859 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMR----ARLAAKKQELEEIL 934
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKkaeaARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 935 HDLESRVEEEEERnqiLQNEKKkmqghiqdleeqLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1014
Cdd:PTZ00121 1195 KAEDARKAEAARK---AEEERK------------AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 EDRIAECTSQLAEEEEKAKNLAKLKNKQEmmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK-- 1092
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkk 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1093 IQLAKKEEELQAALARGDEEAVQKNnalkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1172
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAA-------EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1173 AAQQELRTKREqevaELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKelACEVKV 1252
Cdd:PTZ00121 1411 KKAAAAKKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKK 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1253 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNEldnvssllEEAEKKGIKFAKDAASLESQLQDTQE 1332
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEE 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1333 LLQEETRQKLNLSSRirqlEEEKNNLQEQQEEEEearKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDME 1412
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKK----AEEDKNMALRKAEEA---KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1413 SLSQRLEEKAMAYDKLEKTKNRLQQElddlmvdlDHQRQIVSNLEKKQKKFDQMLAEEknisARYAEERDRAEAEAREKE 1492
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKA--------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1493 TKAlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1572
Cdd:PTZ00121 1698 AEE---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1573 LRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmdlkdlegqieaankarDE 1652
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DS 1830
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1653 AIKQLRKLQAQMKDYQRELEEARASRDEIfaqSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANS 1730
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
860-1436 |
8.75e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.67 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 860 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 939
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 940 RVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEILLLEDQNSkflkEKKLMEDRIA 1019
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1020 ECTSQLAEEEEKAKNLAKLKNKQEMM-----------ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQI 1088
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1089 EELKiqLAKKEEELQAALARGDEEAvqknnalKVIRELQAQIAELQEDLEsekasrnKAEKQKRDLSEELEALKTELEdt 1168
Cdd:PRK03918 429 EELK--KAKGKCPVCGRELTEEHRK-------ELLEEYTAELKRIEKELK-------EIEEKERKLRKELRELEKVLK-- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1169 ldttaaqQELRTKREQEVAELKKAIEEETKNHEAQiqeirqrhatALEELSEQLEQAKRFKANLEKNKQGLESD---NKE 1245
Cdd:PRK03918 491 -------KESELIKLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1246 LACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLES 1325
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE-------LKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1326 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARknLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKK 1405
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590
....*....|....*....|....*....|.
gi 212450 1406 KllkdmeslsqrLEEKAMAYDKLEKTKNRLQ 1436
Cdd:PRK03918 705 E-----------REKAKKELEKLEKALERVE 724
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1030-1411 |
1.02e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 96.66 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1030 EKAKNLAKLKNKQEMM---ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1106
Cdd:TIGR02168 674 ERRREIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1107 ARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEV 1186
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1187 AELKKAIEEETKNHEaQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKK 1266
Cdd:TIGR02168 834 AATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1267 LDAQVQELTAKV----TEGERLRVELAEKANKLQNEldnVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKL 1342
Cdd:TIGR02168 913 LRRELEELREKLaqleLRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1343 NLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQaqlAEAKKKVDDdlgTIEGLEENKKKLLKDM 1411
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID---REARERFKD---TFDQVNENFQRVFPKL 1052
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
874-1491 |
1.24e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 96.29 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 874 VKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLESRVEEEEERNQI 950
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 951 LQNEKKKMQGHIQDLEeqldeeegarqKLQLEKVTAEAKIKKMEEEIllledqnskflkekKLMEDRIAECTSQLAEEEE 1030
Cdd:PRK03918 226 LEKEVKELEELKEEIE-----------ELEKELESLEGSKRKLEEKI--------------RELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1031 KAKNLAKLKNKQEMMITdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGD 1110
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1111 EEAvqknNALKVIRELQAQIaelqEDLESEKASRNKaEKQKRDLsEELEALKTELEDTLDTTAAQqelRTKREQEVAELK 1190
Cdd:PRK03918 359 ERH----ELYEEAKAKKEEL----ERLKKRLTGLTP-EKLEKEL-EELEKAKEEIEEEISKITAR---IGELKKEIKELK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1191 KAIEEETKNH-----------EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLE---SDNKELACEVKVLQQV 1256
Cdd:PRK03918 426 KAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESELIKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1257 KaESEHKRKKLDaqVQELTAKVTEGERLRvelaEKANKLQNELDNVSSLLEEAEkkgiKFAKDAASLESQLQDTQELLQE 1336
Cdd:PRK03918 506 K-ELEEKLKKYN--LEELEKKAEEYEKLK----EKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1337 ETRQKLN--------LSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLaLQAQLAEAKKKVDDDLGTIEGLEENKKKLL 1408
Cdd:PRK03918 575 LLKELEElgfesveeLEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELDKAFEELAETEKRLEELRKELEELE 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1409 K-----DMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK---KFDQMLAEEKNISARYAEE 1480
Cdd:PRK03918 654 KkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKY 733
|
650
....*....|.
gi 212450 1481 RDRAEAEAREK 1491
Cdd:PRK03918 734 KALLKERALSK 744
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
990-1808 |
1.33e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.75 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 990 IKKMEEeiLLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAK-- 1067
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEea 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1068 RKLDGETTDLQDQIAELQAQIEEL-KIQLAKKEEEL-QAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1145
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDArKAEEARKAEDArKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1146 KAEKQKRDlseelEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQA 1225
Cdd:PTZ00121 1184 AEEVRKAE-----ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1226 KRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRvELAEKANKLQNELDNVSSL 1305
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1306 LEEAEKKGIKFAKDAASLESQLQDTQEllqEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAE 1385
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEE---KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1386 AKKKVDDDLgtiegleENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEldDLMVDLDHQRQIVSNLEKKQKKFDQ 1465
Cdd:PTZ00121 1415 AAKKKADEA-------KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKA 1485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1466 MLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlmSSKDDVGKNVHELEKSKR 1545
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE---KKKADELKKAEELKKAEE 1562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1546 TleQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQ--NEEKKRMLVKQVRELEAELEDERKQRA 1623
Cdd:PTZ00121 1563 K--KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1624 LAVAAKKKMEMDLKDlegqiEAANKARDEAIKQlrklqaQMKDYQRELEEARASRDEifaqSKESEKKLKGLEAEILQLQ 1703
Cdd:PTZ00121 1641 KEAEEKKKAEELKKA-----EEENKIKAAEEAK------KAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAE 1705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1704 EEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSEL 1783
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
810 820
....*....|....*....|....*
gi 212450 1784 agersaAQKSENARQQLERQNKELK 1808
Cdd:PTZ00121 1786 ------DEEDEKRRMEVDKKIKDIF 1804
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1181-1938 |
1.58e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.29 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1181 KREQEVAELKkAIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKAnLEKNKQGLESdnKELACEVKVLqqvkaes 1260
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQ----LERLRREREKAERYQA-LLKEKREYEG--YELLKEKEAL------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1261 EHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEE-AEKKGIKFAKDAASLESQLQDTQELLQEETR 1339
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1340 QKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLE 1419
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1420 EKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqmlaeeknisaryaEERDRAEAEAREKETKALSLA 1499
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1500 raleealEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT----------- 1568
Cdd:TIGR02169 462 -------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvg 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1569 EDAKLRLEV----NMQAMKAQFERDLQARDEQNEEKK--RMLVKQVRELEAEledERKQRALAVAAKKKMEMDLKDLEGQ 1642
Cdd:TIGR02169 535 ERYATAIEVaagnRLNNVVVEDDAVAKEAIELLKRRKagRATFLPLNKMRDE---RRDLSILSEDGVIGFAVDLVEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1643 IEAANKA--RD----EAIKQLRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKGLEAEILQLQEEF 1706
Cdd:TIGR02169 612 YEPAFKYvfGDtlvvEDIEAARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1707 AASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGE 1786
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1787 RSAAQKSENARQQLER-----QNKELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKL 1861
Cdd:TIGR02169 771 EEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEV-SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1862 KEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1606-1944 |
2.18e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.39 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1606 KQVRELEAELEdeRKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1685
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1686 KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELL 1765
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA-------ELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1766 NERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgsvkskfkATISTLEAKIAQLEEQLEQEAK 1845
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE--------EAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1846 ERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRAnASRRKLQRELDDATEANE 1925
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA-AARLLLLLEAEADYEGFL 507
|
330
....*....|....*....
gi 212450 1926 GLSREVSTLKNRLRRGGPI 1944
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAV 526
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1494 |
3.23e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 95.59 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 855 LQVTRQEEELQaKDEELMKVKEKQTKVEAELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 933
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 934 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-----ARQKLQLEKVTAEAK----IKKMEEEILLLEDQN 1004
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaeeKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1005 SKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1082
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1083 ELQAQIEEL--KIQLAKKEEEL--QAALARGDEEAVQKNNALKVIREL--QAQIAELQEDLESEKASRNKAEKQKRDlSE 1156
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAkkKAEEAKKADEAKKKAEEAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1157 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhataleelSEQLEQAKRFKANLEKNK 1236
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1237 qgleSDNKELACEVKVLQQVKAESEHKRKKldAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSllEEAEKKGIKF 1316
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1317 AKDAAslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNlekqmlalqaqlAEAKKKVDDDLGT 1396
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA------------AEALKKEAEEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1397 IEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISAR 1476
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 212450 1477 YAEERDRAEAEAREKETK 1494
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
855-1666 |
6.90e-19 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 93.88 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 855 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIL 934
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 935 HDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1014
Cdd:pfam02463 268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKtRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1094
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK-LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1095 LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT--- 1171
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkar 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1172 ------TAAQQELRTKREQEVAELKKAIEEETKNHEAQI--QEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESD- 1242
Cdd:pfam02463 507 sglkvlLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIstAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPk 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1243 -------------NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA 1309
Cdd:pfam02463 587 lklplksiavleiDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1310 EKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKK 1389
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1390 VDDDlgtiEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1469
Cdd:pfam02463 747 EEEE----EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1470 EKNISArYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQ 1549
Cdd:pfam02463 823 LIEQEE-KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1550 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQN--EEKKRMLVKQVRELEAELEDERKQRALAVA 1627
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
810 820 830
....*....|....*....|....*....|....*....
gi 212450 1628 AKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKD 1666
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1146-1727 |
1.34e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.82 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1146 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR--QRHATALEELSEQLE 1223
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEklEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1224 QAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDaQVQELTAKVTEGERLRVELAEKANKLQNELDNVS 1303
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1304 SLLEEAEKKGIKFAKDAASLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLQEQQ------------EEEEEAR 1369
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekelEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1370 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGL---------------EENKKKLLKD-MESLSQRLEEKAMAYDKLEKTKN 1433
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEyTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1434 RLqqelddlmVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFE 1513
Cdd:PRK03918 481 EL--------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1514 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQAR 1593
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1594 DEQNEEKKR--MLVKQVRELEAELEDERKQRAlaVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQ---MKDYQ 1668
Cdd:PRK03918 633 EELAETEKRleELRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEleeREKAK 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1669 RELEEARASRDEIfaqsKESEKKLKGLEAEilqlqeefaaserARRHAEQERDELADEI 1727
Cdd:PRK03918 711 KELEKLEKALERV----EELREKVKKYKAL-------------LKERALSKVGEIASEI 752
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
952-1771 |
2.58e-18 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 92.34 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 952 QNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLA-EEEE 1030
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRdEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1031 KAKNLAKLKNKQEMMITDLEER------LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQA 1104
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENkeeekeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1105 ALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLdTTAAQQELRTKREQ 1184
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL-ELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1185 EVAELKKAIEEETKNHEAQIQEIRQRHATALEE-LSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHK 1263
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1264 RKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAE-----KKGIKFAKDAASLESQLQDTQELLQEET 1338
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVenykvAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1339 RQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLAlqAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL 1418
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA--TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1419 EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSL 1498
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1499 AraleEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR-LEV 1577
Cdd:pfam02463 730 A----QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEeLRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1578 NMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1657
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1658 RKLQaQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASErarrhaEQERDELADEIANSASGKSAL 1737
Cdd:pfam02463 886 DELE-SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP------EELLLEEADEKEKEENNKEEE 958
|
810 820 830
....*....|....*....|....*....|....
gi 212450 1738 LDEKRRLEARIAQLEEELEEEQSNMELLNERFRK 1771
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1083-1704 |
4.01e-18 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 91.24 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1083 ELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKasrNKAEKQKRDLSEELEALK 1162
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1163 TEledtldttaaqQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHaTALEELSEQLEQAKRFKANLEKNKQGLESD 1242
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1243 NKELACEVKVLQQVKAESEHKRKKLDAQVQ---ELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKD 1319
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1320 AASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR-----KNLEKQMLALQAQLAEAKKKVDDDL 1394
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1395 GTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDdlmvdldhqrqivsNLEKKQKKFDQMLAEEKNIS 1474
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--------------NLESQINDLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1475 ARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1554
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1555 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELE--DERKQRALAVAAKKKM 1632
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNkdDFELKKENLEKEIDEK 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212450 1633 EMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQE 1704
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
860-1439 |
4.16e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.25 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 860 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 939
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 940 RveeeeernqilqnekkkmqghiqdleeqldeEEGARQKLQLEKVTAEAkikkmeeeillLEDQNSKFLKEKKLMEDRIA 1019
Cdd:PRK02224 294 E-------------------------------RDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1020 ECTSQLAEEEEKAKNLAKlknkqemMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1099
Cdd:PRK02224 332 ECRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1100 EELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLES-----------------EKASRNKAEKQKRDLSEELEALK 1162
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1163 TELEDTLDTTAAqqelRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQakrfkanLEKNKQGLEsd 1242
Cdd:PRK02224 485 EDLEEEVEEVEE----RLERAEDLVEAEDRIERLEERREDLEELIAERRET-IEEKRERAEE-------LRERAAELE-- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1243 nkelacevkvlqqvkAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNeLDNVSSLLEEAEKKGikfaKDAAS 1322
Cdd:PRK02224 551 ---------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE----DEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1323 LESQLQDTQElLQEETRQKL-NLSSRIRQLEEE--KNNLQEQQEEEEEARKNLEKQMLALQaQLAEAKKKVDDDLGTIEG 1399
Cdd:PRK02224 611 LREKREALAE-LNDERRERLaEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLD-ELREERDDLQAEIGAVEN 688
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 212450 1400 LEENKKKLLKDMESLSQRLEEKAMAYDK---LEKTKNRLQQEL 1439
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYDEaeeLESMYGDLRAEL 731
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1124-1731 |
5.63e-18 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 91.13 E-value: 5.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1124 RELQAQIAELQEDLESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtknHE 1201
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA---EL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1202 AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKE-LACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTE 1280
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1281 GERlrvELAEKANKLQNELDNVSSLLEEAEKkgikfakDAASLESQLQDTQEllqeetrqklnlssRIRQLEEEKNNLQE 1360
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRDLRR--------------ELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1361 QqeeeeeaRKNLEKQMLALQAQLAEAKKKVDDDL-----------------GTIEGL----------------------E 1401
Cdd:COG4913 434 R-------KSNIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvppehyaaalrwvN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1402 ENKKKLLKDMESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMV------------DLDHQR-------QIVSN 1455
Cdd:COG4913 507 RLHLRGRLVYERVRTGLPDPERPrldpdslAGKLDFKPHPFRAWLEAELGrrfdyvcvdspeELRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1456 LEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1535
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1536 NVHELEKSKRTLEQ------QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVR 1609
Cdd:COG4913 666 AEREIAELEAELERldassdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1610 ELEAELEDERKQRALAVAAKKKMEmdlkDLEGQIEAANKARDEAIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESE 1689
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYL 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 212450 1690 KKLKGLEAEIL-QLQEEFAasERARRHAEQERDELADEIANSA 1731
Cdd:COG4913 819 ALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRAI 859
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1373-1940 |
6.26e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 90.48 E-value: 6.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1373 EKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAmaydklEKtknrlQQELDDLMVDLDHQRQI 1452
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1453 VSNLEKKQKKFDQMLAEEKNISARYAEERD--RAEAEAREKETKALSLARALEEaleakeefeRQNKQLRADMEDLMSSK 1530
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARREELE---------DRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1531 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAklrlevnmqamkaqferdlqaRDEQNEEkkrmlvkqVRE 1610
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA---------------------VEDRREE--------IEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1611 LEAELEDERKQRALAvaakkkmEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDE---------- 1680
Cdd:PRK02224 389 LEEEIEELRERFGDA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpv 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1681 ----IFAQSKESEKKLKGLEAEILQLQEEFAASErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELE 1756
Cdd:PRK02224 462 egspHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1757 EEQSNMELLNERfrkttlqVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkfKATISTLEAKIAQL 1836
Cdd:PRK02224 534 EKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--LERIRTLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1837 EEQLEqeakeraaanklvRRTEKklKEVFMQVEDERRhadqykEQMEKANARMKQLKRQLEEAEEEATRANASR-----R 1911
Cdd:PRK02224 605 EDEIE-------------RLREK--REALAELNDERR------ERLAEKRERKRELEAEFDEARIEEAREDKERaeeylE 663
|
570 580
....*....|....*....|....*....
gi 212450 1912 KLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
838-1492 |
8.69e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.59 E-value: 8.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 838 KLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAElEEMERKHQQLLEEKNILAEQLQAETELFAEAE 917
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 918 EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAK-----IKK 992
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaeeDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 993 MEEEILLLEDQNSKFLKEKKLMED-RIAECTSQLAEEEEKAKnlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLD 1071
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1072 GETTDLQDQIAELQAQIEELKiqlAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1151
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1152 RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATAleelsEQLEQAKRFKAN 1231
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-----EELKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1232 LEKNKQGLESDNKElACEVKVLQQ---VKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEE 1308
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1309 AEKKGIKFAKDAASLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALqaqlaeAKK 1388
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV------IEE 1783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1389 KVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYdkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1468
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENG 1861
|
650 660
....*....|....*....|....
gi 212450 1469 EEKNISARYAEERDRAEAEAREKE 1492
Cdd:PTZ00121 1862 EDGNKEADFNKEKDLKEDDEEEIE 1885
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1000-1812 |
9.53e-18 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 90.18 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1000 LEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLkkeEKTRQELEKAKrkldgetTDLQD 1079
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQL---QNTVHELEAAK-------CLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1080 QIAELQAQIEELKIQLAKKE---EELQAALARGDEEAVQK---NNALKVI--RELQAQIAELQEDLESEKASrnkAEKQK 1151
Cdd:pfam15921 164 MLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyeHDSMSTMhfRSLGSAISKILRELDTEISY---LKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1152 RDLSEELEALKTELEDTLDTTAAQQELRtkreqevaelkkaIEEETKNHEAQIQEIRQRHATALEE---LSEQL----EQ 1224
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQDR-------------IEQLISEHEVEITGLTEKASSARSQansIQSQLeiiqEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1225 AKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSS 1304
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSE---LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1305 LLEEAEKKgikfakdaASLESqlQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARK----NLEKQMLALQ 1380
Cdd:pfam15921 385 DLHKREKE--------LSLEK--EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1381 AQlAEAKKKVDDDLGTIEGLEENKKKLLKDmeslsqrLEEKAMAYDKLEKTknrlqqeLDDLMVDLDHQRQIV----SNL 1456
Cdd:pfam15921 455 GK-NESLEKVSSLTAQLESTKEMLRKVVEE-------LTAKKMTLESSERT-------VSDLTASLQEKERAIeatnAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1457 EKKQKKFDQMLAEEKNISaryaEERDRAEAEAREKETKALSLARALEEALEakeeferqnkqLRADMEDLMSSKDDVGKN 1536
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLK----NEGDHLRNVQTECEALKLQMAEKDKVIEI-----------LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1537 VHELEKSKRTLEQQVEEMRTQLEELEdELQATEDAKLrlevnmqamkaqfeRDLQARDEQNEEKKRMLVKQVRELEAELE 1616
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDAKI--------------RELEARVSDLELEKVKLVNAGSERLRAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1617 DERKQRALAVAAKKKMEMDLKDLEGQIEAANK----ARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1692
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1693 KGLEAEIlqlqeefaASERARRHAEQERDELADE-IANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRK 1771
Cdd:pfam15921 730 MGMQKQI--------TAKRGQIDALQSKIQFLEEaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 212450 1772 ttLQVDTLNSELAGERSAAQKSEnARQQLERQNKE-LKAKLQ 1812
Cdd:pfam15921 802 --LKEKVANMEVALDKASLQFAE-CQDIIQRQEQEsVRLKLQ 840
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
909-1747 |
1.42e-17 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 89.90 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 909 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKkmqghiQDLEEQLDEEEGARQKLQLEKVTAEA 988
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 989 KIKKMEEEILLLEDQNSKFLKEkklmedriaectsqlaeeeekakNLAKLKNKQEMmitdleerlkkEEKTRQELEKAKR 1068
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1069 KLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKviRELQAQIAELQEDLESEKASRNKAE 1148
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1149 KQkrdLSEELEALKTEledtLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQ--IQEIRQRHATALEELSEQLEQAK 1226
Cdd:pfam12128 440 YR---LKSRLGELKLR----LNQATATPELLLQLENFDERIERAREEQEAANAEVerLQSELRQARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1227 RFkanLEKNKQGLEsdnkelacEVKVLQQVKAESEHKRKKLDAQV-QELTAKVTEGERL-RVELAEKANKlqneldnvSS 1304
Cdd:pfam12128 513 RR---LEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDwEQSIGKVISPELLhRTDLDPEVWD--------GS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1305 LLEEAEKKGIKFAKDAASLESQLQDTQELlqeetRQKLNLSSRIRQLEEEKnnlqeqqeeeeeaRKNLEKQMLALQAQLA 1384
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEEL-----RERLDKAEEALQSAREK-------------QAAAEEQLVQANGELE 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1385 EAKKKVDDDLGTIEGLEENKKKLLKDMESLSqrleekamayDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKFD 1464
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWL 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1465 QMLAEEKnISARYAEERDRAEAEarekETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1544
Cdd:pfam12128 703 EEQKEQK-REARTEKQAYWQVVE----GALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1545 RTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFERDLQardEQNEEKKRMLVKQVRELEAELEDERKQRAL 1624
Cdd:pfam12128 778 RTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQLAR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1625 AVAAKKkmeMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARASRDEIFAQSKESEKKLKGLEAEI 1699
Cdd:pfam12128 833 LIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 212450 1700 LQLQEEFAASERARRHAEQER--DELADEIANSASGKSALLDEKRRLEAR 1747
Cdd:pfam12128 910 KKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1123-1748 |
4.31e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1123 IRELQAQIAELQEDLESEKAsrnkaEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEVAELKKAieeetknhea 1202
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIE-----EKEEKDLHERLNGLESELAEL---DEEIERYEEQREQARETRDEA---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1203 qiQEIRQRHATALEELSEqleqakrfkanleknkqglesdnkeLACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1282
Cdd:PRK02224 240 --DEVLEEHEERREELET-------------------------LEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1283 RLRVELAEKANKLQNELDNVSSLLEEaekkgikFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqq 1362
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1363 eeeeearKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEEnkkkllkDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1442
Cdd:PRK02224 359 -------EELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1443 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS-ARYAEERDRAEAEAREKETKAlslaraleealeakeeferqnkQLRA 1521
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKCPEcGQPVEGSPHVETIEEDRERVE----------------------ELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1522 DMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELqatedaklrlevnmqamkAQFERDLQARDEQNEEKK 1601
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELI------------------AERRETIEEKRERAEELR 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1602 rmlvKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1681
Cdd:PRK02224 544 ----ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1682 FAQSKESEKKLKGLEAEILQLQEEFaasERARRHAEQERDELADEIANSASGKSALLDEKR-RLEARI 1748
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEI 683
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
987-1576 |
7.77e-17 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 87.00 E-value: 7.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 987 EAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKA 1066
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1067 KRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEEL---QAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKAS 1143
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1144 RNKAEKQKRDLSEELEALKTELEDTldttaAQQELRTKREQEvaELKKAIEEETKnheaqiqeirqrhataleelseQLE 1223
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNT-----QTQLNQLKDEQN--KIKKQLSEKQK----------------------ELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1224 QAKRFKANLEKNKQGLESdnkelacEVKVLQQVKAESEHKR-----KKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1298
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1299 LDNVSSlleEAEKKGIKFAKDAASLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1378
Cdd:TIGR04523 351 LTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1379 LQAQLAEAKKKVDDDLGTIEGLEENK-------KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQ 1451
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDsvkeliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1452 IVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSS 1529
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieELKQTQKSLKKK 583
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 212450 1530 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE 1576
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1213-1932 |
8.03e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 87.28 E-value: 8.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1213 TALEELSEQLEQAKRFKANLEKNKQglesdnkelacEVKVLQQVKAESEhkrkKLDAQVQELTAKVTEGERLRVELAE-K 1291
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAE----RYAAARERLAELEYLRAALRLWFAQrR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1292 ANKLQNELDNVSSLLEEAEKKgikfakdAASLESQLQDTQELLQEETRQKLNLS-SRIRQLEEEKNNLQEQQEEEEEARK 1370
Cdd:COG4913 290 LELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1371 NLEKQMLALQAQLAEakkkvdddlgTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQR 1450
Cdd:COG4913 363 RLEALLAALGLPLPA----------SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1451 QIVSNLEKKQKKFDQMLAEEKNISA---RYA------EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQL 1519
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelPFVgelievRPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1520 RADMEDLMSSkddvGKNVHELEKSKRTLEQQVE----EMRTQLEEL------------EDELQATEDAkLRLEVNMQAMK 1583
Cdd:COG4913 513 RLVYERVRTG----LPDPERPRLDPDSLAGKLDfkphPFRAWLEAElgrrfdyvcvdsPEELRRHPRA-ITRAGQVKGNG 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1584 AQFERDLQARDEQ-------NEEKKRMLVKQVRELEAELEDerkqralAVAAKKKMEMDLKDLEGQIEAANKARD--EAI 1654
Cdd:COG4913 588 TRHEKDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAE-------AEERLEALEAELDALQERREALQRLAEysWDE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1655 KQLRKLQAQMKDYQRELEEARASRDEifaqskesekkLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgk 1734
Cdd:COG4913 661 IDVASAEREIAELEAELERLDASSDD-----------LAALEEQLEELEAELEELEEELDELKGEIGRLEKELE------ 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1735 sALLDEKRRLEARIAQLEEELEEEQSnmELLNERFRkttlqvdtlnsELAGERSAAQKSENARQQLERQNKELKAKLQEL 1814
Cdd:COG4913 724 -QAEEELDELQDRLEAAEDLARLELR--ALLEERFA-----------AALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1815 EGSV---KSKFKATISTLEAKIAQLEE------QLEQE---AKERAAANKLVRRTEKKLKEVFMQVEDERRHAdqyKEQM 1882
Cdd:COG4913 790 ERAMrafNREWPAETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERI 866
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 212450 1883 EKANARMKQLK----RQLeeAEEEATRANASRRKLQRELDDATEANEGLSREVS 1932
Cdd:COG4913 867 DPLNDSLKRIPfgpgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1636-1920 |
1.96e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1636 LKDLEGQIEAANKAR----DEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASER 1711
Cdd:COG1196 202 LEPLERQAEKAERYRelkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1712 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeLEEEQsnmELLNERFRKTTLQVDTLNSELAGERSAAQ 1791
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE----LEEEL---AELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1792 KSENARQQLERQNKELKAKLQELEGSVKSKFKA------TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVF 1865
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEEllealrAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1866 MQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDA 1920
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1009-1604 |
3.86e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 84.71 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1009 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL-----------------EKAKRKLD 1071
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELetleaeiedlretiaetEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1072 GETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1151
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1152 RDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKAIEEETKnheaqiqeirqrhatALEELSEQLEQAKRFKAN 1231
Cdd:PRK02224 359 EELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRE---------------RFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1232 LEKNKQGLESDNKELACEVKVLQQVKAESEhkrKKLDA-QVQELTAKVTEGERLRV--ELAEKANKLQNELDNVSSLLEE 1308
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAE---ALLEAgKCPECGQPVEGSPHVETieEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1309 AEKKgIKFAKDAASLESQLQDTQEllqeetrQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1388
Cdd:PRK02224 494 VEER-LERAEDLVEAEDRIERLEE-------RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1389 KVDDDLGTIEGLEenkkkllkdmeslsQRLEEKAMAYDKLEKtknrlqqeLDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1468
Cdd:PRK02224 566 EAEEAREEVAELN--------------SKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1469 EEKNisaRYAEERDRAEAEAREKETKALSlaraleealeakeeferqnkQLRADMEDLMSSKDDVGKNVHELEKSKRTLE 1548
Cdd:PRK02224 624 ERRE---RLAEKRERKRELEAEFDEARIE--------------------EAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1549 QQ---VEEMRTQLEELEDELQATEDAKLRLEV------NMQAMKAQFERDLQARDEqnEEKKRML 1604
Cdd:PRK02224 681 AEigaVENELEELEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQRNV--ETLERML 743
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
862-1577 |
5.08e-16 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 84.78 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 862 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfAEAEEMRARLAAKK---QELEEILHDLE 938
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSN--TQIEQLRKMMLSHEgvlQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 939 srveeeeernqilQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEkvtAEAKIKKMEEEILLLEDQNSKFLKEKK------ 1012
Cdd:pfam15921 198 -------------EASGKKIYEHDSMSTMHFRSLGSAISKILRE---LDTEISYLKGRIFPVEDQLEALKSESQnkiell 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1013 --LMEDRIAECTSQ-------LAEEEEKAKNLA------------KLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLD 1071
Cdd:pfam15921 262 lqQHQDRIEQLISEheveitgLTEKASSARSQAnsiqsqleiiqeQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1072 GettdlqdqiaelqaQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1151
Cdd:pfam15921 342 D--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRD 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1152 RDLSEELEALKTELED------TLDT--TAAQQELRTKREQEVAELKKAIE--EETKNHEAQIQEIRQRHATALEELSEQ 1221
Cdd:pfam15921 408 TGNSITIDHLRRELDDrnmevqRLEAllKAMKSECQGQMERQMAAIQGKNEslEKVSSLTAQLESTKEMLRKVVEELTAK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1222 ---LEQAKR----FKANLEKNKQGLESDNKELA-------CEVKVLQQVKAESEHKRkkldaQVQeltakvTEGERLRVE 1287
Cdd:pfam15921 488 kmtLESSERtvsdLTASLQEKERAIEATNAEITklrsrvdLKLQELQHLKNEGDHLR-----NVQ------TECEALKLQ 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1288 LAEKANK---LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEE 1364
Cdd:pfam15921 557 MAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVK 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1365 EEEARknlEKQMLALQaqlaEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAmayDKLEKTKNRLQQELDDLMV 1444
Cdd:pfam15921 637 LVNAG---SERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQS 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1445 DLDHQRQIVSNLEKKQ-KKFDQMLAEEKNISARyaeerdRAEAEAREKETKALSLAraLEEALEAKEEFERQNKQLRADM 1523
Cdd:pfam15921 707 ELEQTRNTLKSMEGSDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLEEA--MTNANKEKHFLKEEKNKLSQEL 778
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 1524 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLEV 1577
Cdd:pfam15921 779 STVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLKL 839
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
995-1726 |
5.14e-16 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 84.64 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 995 EEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEeeKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKaKRKLDGET 1074
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1075 TDLQDQIAELQAQIEELKIQLAKkEEELQAALARGDEEAVQKNNAlKVIRELQAQIAELQEDLESEKASRNKAEKQKRDL 1154
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAV-LEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAH 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1155 SEEleALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEE---LSEQLEQAKRFKAN 1231
Cdd:TIGR00618 334 VKQ--QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQREQAT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1232 LEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNeLDNVSSLLEEAEK 1311
Cdd:TIGR00618 412 IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQETRKKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1312 KGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVD 1391
Cdd:TIGR00618 491 VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQ 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1392 DDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQrQIVSNLEKKQKKFDQMLAEEK 1471
Cdd:TIGR00618 567 EIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE-QDLQDVRLHLQQCSQELALKL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1472 NISARYAEERdraeaeAREKETKALSLARALEEaleakeeferQNKQLRADMEDLMSSKddvgknVHELEKSKRTLEQQV 1551
Cdd:TIGR00618 646 TALHALQLTL------TQERVREHALSIRVLPK----------ELLASRQLALQKMQSE------KEQLTYWKEMLAQCQ 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1552 EEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfeRDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKK 1631
Cdd:TIGR00618 704 TLLRELETHIE------EYDREFNEIENASSSLG--SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQ 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1632 MEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKGLEAEILQLQEEFA 1707
Cdd:TIGR00618 776 TGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLKYE 855
|
730
....*....|....*....
gi 212450 1708 ASERARRHAEQERDELADE 1726
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQL 874
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
869-1525 |
1.38e-15 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 82.85 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 869 EELMKVKEKQTKVEAELEEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD----------LE 938
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 939 SRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLE----KVTAEAKIKKMEEEILLLEDQNSKFLKEKklm 1014
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQaenaRLEMHFKLKEDHEKIQHLEEEYKKEINDK--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQIEE 1090
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1091 LKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1171 TTAAQ----QELRT-----------------------KREQEVAELKKAIEEETKNHEAQIQEIR---QRHATALEELSE 1220
Cdd:pfam05483 399 FKNNKevelEELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1221 QLEQAKRFKANLEKNKQGLESDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerLRVELAEKAN 1293
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1294 KLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1373
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1374 KQMLALQAQLAEAKKKVDDDLGTIEGLEENKK----KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQ 1449
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1450 rqivsnLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1525
Cdd:pfam05483 716 ------YDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1066-1441 |
2.39e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 82.42 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1066 AKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1145
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1146 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIE----EETKNHEAQIQEIRQRHATALEELSEQ 1221
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1222 LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDN 1301
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1302 VSSLLEEAEKKgikfAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK----QML 1377
Cdd:TIGR02169 901 LERKIEELEAQ----IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNML 976
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1378 ALQaQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAM-AYDKLEKTKNRLQQELDD 1441
Cdd:TIGR02169 977 AIQ-EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMeAFEAINENFNEIFAELSG 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1287 |
2.72e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.03 E-value: 2.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 857 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQELEE 932
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 933 ILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEILLLEDQNSKFLKEKK 1012
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE--LKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1013 LMEDRIAEcTSQLAEEEEKAKNLAKLKNK-QEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQdQIAELQAQIEEL 1091
Cdd:PRK03918 484 ELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAEL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1092 KIQLAKKEEELQAALARGDEEavqknnALKVIRELQAQIAELqEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT 1171
Cdd:PRK03918 562 EKKLDELEEELAELLKELEEL------GFESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1172 TA-AQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLEsDNKELACEV 1250
Cdd:PRK03918 635 LAeTEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKEL 713
|
410 420 430
....*....|....*....|....*....|....*..
gi 212450 1251 KVLQQVKAESEHKRKKldaqVQELTAKVTEGERLRVE 1287
Cdd:PRK03918 714 EKLEKALERVEELREK----VKKYKALLKERALSKVG 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
861-1447 |
3.80e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 81.22 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKnilaEQLQAETELFaeaeemrarlaakKQELEEILHDLESR 940
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK----EELENELNLL-------------EKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 941 VEEEEERNQILQNEKKKMQGH------IQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEkklm 1014
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNkslesqISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 edrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEErlKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1094
Cdd:TIGR04523 269 ---LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1095 LAKKEEELQAALARG---DEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN----KAEKQKRDLSEELEALKTELED 1167
Cdd:TIGR04523 344 ISQLKKELTNSESENsekQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqNQEKLNQQKDEQIKKLQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1168 TLDTTAAQQELRTKREQEVAELKKAI---EEETKNHEAQIQEIRQrhataleELSEQLEQAKRFKANLEKNKQGLESDNK 1244
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDsvkELIIKNLDNTRESLET-------QLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1245 ELacevKVLQQVKAESEHKRKKLDAQVQELTAKVtegERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLE 1324
Cdd:TIGR04523 497 EL----KKLNEEKKELEEKVKDLTKKISSLKEKI---EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1325 -SQLQDTQELLQEETRQKLNLssrIRQLEEEKNNLQEQQEeeeearkNLEKQMLALQAQLAEAKKKVdddlgtiEGLEEN 1403
Cdd:TIGR04523 570 iEELKQTQKSLKKKQEEKQEL---IDQKEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEN-------EKLSSI 632
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 212450 1404 KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLD 1447
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1253-1939 |
4.32e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.65 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1253 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVEL--AEKANKLQNELDNV-----SSLLEEAEKKGIKFAKDAASLES 1325
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1326 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR-KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENK 1404
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1405 KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqrqiVSNLEKKQKKFDQMLAEEKnisaryaEERDRA 1484
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----------RAELEEVDKEFAETRDELK-------DYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1485 EAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1564
Cdd:TIGR02169 395 EKLKREIN----ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1565 LQATEDAKLRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELEAELE------------DERKQRALAVAAKKKM 1632
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1633 EMDLKDLEGQIEaankardEAIKQLRKLQA---------QMKDYQRELEEAR------------------------ASRD 1679
Cdd:TIGR02169 550 NNVVVEDDAVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyVFGD 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1680 EIFAQSKESEKKLKG------LEAEILQ---------LQEEFAASERARRHAEQERdeLADEIANSASGKSALLDEKRRL 1744
Cdd:TIGR02169 623 TLVVEDIEAARRLMGkyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQR--LRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1745 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgSVKSKFKA 1824
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1825 TISTLEAKIA-----QLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEA 1899
Cdd:TIGR02169 780 ALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 212450 1900 EEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1939
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1290-1864 |
1.22e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.11 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1290 EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR 1369
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1370 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKL--LKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLD 1447
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1448 HQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAeaREKETKALSLARALEEaleakeeferQNKQLRADMEDLm 1527
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKE----------ELERLKKRLTGL- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1528 sSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQARDEQNEEKKRMLvkq 1607
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL--- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1608 vRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARASRDEIFAQ 1684
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1685 SKESEKKLKGLEAEILQLQE---EFAASERARRHAEQERDELADEIANSASGKSALLDEK-------------------- 1741
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaeke 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1742 -RRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGErsaaqKSENARQQLERQNKELKAKLQELEGsVKS 1820
Cdd:PRK03918 614 lEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-----EYEELREEYLELSRELAGLRAELEE-LEK 687
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 212450 1821 KFKATISTLeakiaqleEQLEQEAKERAAANKLVRRTEKKLKEV 1864
Cdd:PRK03918 688 RREEIKKTL--------EKLKEELEEREKAKKELEKLEKALERV 723
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1140-1885 |
1.45e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 80.02 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1140 EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1219
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1220 EQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKAN-KLQNE 1298
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKkKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1299 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDtQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1378
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1379 LQAQLAEAKKKVDDDLGTIEglEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1458
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEE--LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1459 KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEferqnKQLRADMEDLMSSKDDVGKNVH 1538
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE-----NYKVAISTAVIVEVSATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1539 ELEKSKRTLEQQVEEMRTQLEELEDELqateDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1618
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLK----LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1619 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFA---QSKESEKKLKGL 1695
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKkkeQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1696 EAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTL- 1774
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLk 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1775 -QVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAAnKL 1853
Cdd:pfam02463 798 aQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL-KE 876
|
730 740 750
....*....|....*....|....*....|..
gi 212450 1854 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKA 1885
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
813-1459 |
3.45e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 813 RKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEaeleemERKH 892
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 893 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqghiqdleeqldee 972
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 973 egARQKLQLEKVTAEAkiKKMEEEILLLEDQNSKFLKEKKLMEDRIAEcTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1052
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQIEELKIQ----LAKKEEELQAALARGDEEAVQKNNALKVIRELQA 1128
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1129 QIAELQEDLESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKAIEEETKNHEAQIQEir 1208
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1209 qrhatalEELSEQLEQAKRFKAnlEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKvtEGERLRVEL 1288
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--KIAHLKKEE 1766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1289 AEKANKLQNELDNV--SSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKN---NLQ 1359
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNmqlEEA 1846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1360 EQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESlsqRLEEKAMAYDKLEKTKNRLQQEl 1439
Cdd:PTZ00121 1847 DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER---EIPNNNMAGKNNDIIDDKLDKD- 1922
|
650 660
....*....|....*....|
gi 212450 1440 DDLMVDLDHQRQIVSNLEKK 1459
Cdd:PTZ00121 1923 EYIKRDAEETREEIIKISKK 1942
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
927-1703 |
4.02e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 78.24 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 927 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQGHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEILL 999
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1000 LEDQNS--KFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL------------EK 1065
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1066 AKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlargdeeavQKNNALKVIRELQAQIAELqedleSEKASrn 1145
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1146 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQA 1225
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1226 KRF---KANLEKNKQGLESD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1298
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1299 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQqeeeeearknlEKQMLA 1378
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1379 LQAQLAEAKKKVDDDLGTIEGLeENKKKLLKDMESLSQRLEEKAMAYDKLEKTknrLQQELDDLMVDLDHQRQIVSNLEK 1458
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHL-KNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1459 KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKDDVG 1534
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELN 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1535 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVK--QVRELE 1612
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgQIDALQ 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1613 AELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1692
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDII 827
|
810
....*....|.
gi 212450 1693 KGLEAEILQLQ 1703
Cdd:pfam15921 828 QRQEQESVRLK 838
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
989-1815 |
4.36e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.55 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 989 KIKKMEEEILLLEDQNSKFLKEKKLMEDRiaecTSQLAEEEEKA-----KNLAKLKNKQEMMITDLEERLKKEEKTRQEL 1063
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKD----NSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1064 EKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQA--------ALARGDEEAVQKNNALKVIRELQAQIAELQE 1135
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1136 DLESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKAIEEETKNHEAQIQEIRQR 1210
Cdd:TIGR00606 412 QLCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1211 HATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESehkRKKLDAQVQELTAKVTEGERLRVELAE 1290
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGY 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1291 KANK--LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRI------RQLEEEKNNLQEQQ 1362
Cdd:TIGR00606 569 FPNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEI 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1363 EEEEEARKNLEKQMLALQAQLAEAKKK-------VDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRL 1435
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1436 QQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQ 1515
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1516 NKQL-RADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQARd 1594
Cdd:TIGR00606 809 AQQAaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL----KSEKLQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1595 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKardeaikqlrKLQAQMKDYQRELEEA 1674
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1675 RASRDEIFAQSKES-EKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1753
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212450 1754 ELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELE 1815
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
850-1311 |
5.09e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 77.80 E-value: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 850 KVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 929
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 930 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEdqnsKFLK 1009
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1010 EKKLMEDRIAECTSQLAEEEEKaknlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIA--ELQAQ 1087
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1088 IEELKIQLAKKEEELQAALARGDEEAVQKnnalkvIRELQAQIAELQEDLESEKASRNKA---EKQKRDLSEELEALKTE 1164
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKAEEYEKLKEK------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1165 LEDTLDTTAAQQELRTKreqevaELKKAIEE--ETKNHEAQIQEIRQRhataLEELSEQLEQAkrfkanlEKNKQGLESD 1242
Cdd:PRK03918 579 LEELGFESVEELEERLK------ELEPFYNEylELKDAEKELEREEKE----LKKLEEELDKA-------FEELAETEKR 641
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1243 NKELACEVKVLQQVKAESEHKRK-----KLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1311
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
860-1703 |
5.24e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.16 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 860 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 939
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 940 RVEEEEERN-QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK---KLME 1015
Cdd:TIGR00606 277 RKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1016 DRIAE-------------CTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIA 1082
Cdd:TIGR00606 357 DRHQEhirardsliqslaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1083 ELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELqedlesEKASRNKAEKQKRDLSEELEALK 1162
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1163 TELEDTLDTTAAQQElRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA---NLEKNKQGL 1239
Cdd:TIGR00606 511 ADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQT 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1240 ESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerlrvelAEKANKLQNELDNVSSLLEEAEKKGIKFAKD 1319
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1320 AASLESQLQDTQE-------LLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1392
Cdd:TIGR00606 662 TAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1393 DLGTIEGLEENKKKLLKDMESLSQRLEEKamayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKN 1472
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1473 ISARYAEERDRAEAEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRTLEQQVE 1552
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLV 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1553 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQN---EEKKRMLVKQVRELEAELED-ERKQRALAVAA 1628
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDY 971
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1629 KKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQ 1703
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1111-1929 |
5.35e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1111 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK 1190
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1191 KaIEEETKNHEA--QIQEIRQRHATALEELSEQLEQAKRfkanleknkqglESDNKELACEVKVLQQVKAESehKRKKLD 1268
Cdd:PTZ00121 1110 K-AEEARKAEEAkkKAEDARKAEEARKAEDARKAEEARK------------AEDAKRVEIARKAEDARKAEE--ARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1269 AQVQELTAKVTEGER-LRVELAEKANKLQ--NELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqKLNLS 1345
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKaEELRKAEDARKAEaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE---EERNN 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1346 SRIRQLEEEKNNLQEQQEEEEEArknlEKQMLALQAQLAEAKKKVDddlgtieglEENKKKLLKDMESLSQRLEEKAMAy 1425
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKA----EEARKADELKKAEEKKKAD---------EAKKAEEKKKADEAKKKAEEAKKA- 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1426 DKLEKTKNRLQQELDDLMvdldhqrqivSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETkalslARALEEA 1505
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAK----------KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-----AKKKADA 1382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1506 LEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRT--QLEELEDELQATEDAKLRLEvnmqamk 1583
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKadEAKKKAEEAKKADEAKKKAE------- 1454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1584 aqferdlQARDEQNEEKKRMLVKQVRELEAELEDERKqralAVAAKKKMEMDLKDLEgQIEAANKARDEAIKQLRKLQAQ 1663
Cdd:PTZ00121 1455 -------EAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAK 1522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1664 MKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAASERARRhAEQERDELADEIANSASGKSALLDEKRR 1743
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELK--KAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1744 LEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQlERQNKELKAKLQELEGSVKSKFK 1823
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAE 1678
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1824 ATISTLEAKiAQLEEQLEQEAKERAAANKLVRRTEKKLK----------EVFMQVEDERRHADQYKEQMEKANARMKQLK 1893
Cdd:PTZ00121 1679 EAKKAEEDE-KKAAEALKKEAEEAKKAEELKKKEAEEKKkaeelkkaeeENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
810 820 830
....*....|....*....|....*....|....*.
gi 212450 1894 RQLEEAEEEATRANASRRKLQRELDDATEANEGLSR 1929
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
854-1602 |
7.79e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.32 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 854 LLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 929
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 930 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFL 1008
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1009 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQI 1088
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1089 EELKIQLAKKEEELQAALARGDE-EAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED 1167
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVEnYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1168 TLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1247
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1248 CEVKVLQQVKAESEHKRKKLDAQVQELTA--KVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLES 1325
Cdd:pfam02463 677 EIQELQEKAESELAKEEILRRQLEIKKKEqrEKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1326 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKK 1405
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1406 KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAE 1485
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1486 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDEL 1565
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 212450 1566 QATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR 1602
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1215-1869 |
8.84e-14 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 76.98 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1215 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1294
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1295 LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK 1374
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1375 QMLALQAQLAEAKKKVDDdlgtIEGLEENKKKLLKDMESLSQRLEEKAmayDKLEKTKNRLQQELDDlmvdldhQRQIVS 1454
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1455 NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKE---TKAL-SLARALEEALEAKEEFERQNKQLRADMEDLMSsk 1530
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwNKELkSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1531 dDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlqardeQNEEKKRMLVKQVRE 1610
Cdd:TIGR04523 346 -QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1611 LEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1690
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1691 KLKGLEAEILQLqeefaaserarrhaEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR 1770
Cdd:TIGR04523 497 ELKKLNEEKKEL--------------EEKVKDLTKKI-------SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1771 KTTL--QVDTLNSELagersaaQKSENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERA 1848
Cdd:TIGR04523 556 KENLekEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660
....*....|....*....|.
gi 212450 1849 AANKLVRRTEKKLKEVFMQVE 1869
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVK 648
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
986-1496 |
5.07e-13 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 74.47 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 986 AEAKIKKMEeeiLLLEDQNSKFLKEKKLMEDRiaectSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEktrQELEK 1065
Cdd:pfam10174 190 AEMQLGHLE---VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1066 AKRKLDGETTDLQDQIAELQA----------QIEELKIQLAKKEEELQAALARGDEEAVQKNNA---LKVIRE------- 1125
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETLTNQNSDCkqhIEVLKEsltakeq 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1126 ----LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKAIE---EETK 1198
Cdd:pfam10174 339 raaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1199 NHEAQIQEIRQRHA----------TALEELSEQLEQAKRFKANLEKNKqglESDNKELACEVKVLQQvkaesehKRKKLD 1268
Cdd:pfam10174 412 DKDKQLAGLKERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1269 AQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELlQEETRQKLNLSSRI 1348
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRI 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1349 RQLEEEknnLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvDDDLGTIEGL------EENKKKL-LKDMESLSQR---- 1417
Cdd:pfam10174 561 RLLEQE---VARYKEESGKAQAEVERLLGILREVENEKNDK-DKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKkgaq 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1418 -LEEKAMAYDklEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKAL 1496
Cdd:pfam10174 637 lLEEARRRED--NLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
817-1442 |
5.26e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.62 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 817 AKKQQQLSALKILqRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELmkvkekqTKVEAELEEMERKHQQLL 896
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-------RAQEAVLEETQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 897 EEKNILAEQlQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGAR 976
Cdd:TIGR00618 291 KAAPLAAHI-KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 977 QKLQleKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE 1056
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1057 EKTRQ-------ELEKAKRKLDGETTDLQDQ-----------------IAELQAQIEELKIQLAKKEEELQAA------- 1105
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1106 --LARGDEEAVQKNNALKVIR----ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1179
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1180 TKREQEVAELKKAIEEETKN-----HEAQIQEIRQRHATALEELSEQLEQAKRFKANL---EKNKQGLESDNKELACEVK 1251
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLTQERVREHALsirVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1252 VLQQVKAESEHKRKKLDAqVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDA--ASLESQLQD 1329
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTL-LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1330 TQELL------QEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLgtiegleEN 1403
Cdd:TIGR00618 767 NEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL-------EE 839
|
650 660 670
....*....|....*....|....*....|....*....
gi 212450 1404 KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1442
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1009-1231 |
5.77e-13 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.87 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1009 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQI 1088
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1089 EELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDT 1168
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1169 LdttAAQQELRTKREQEVAELKKAIEEEtknhEAQIQEIRQRhATALEELSEQLEQAKRFKAN 1231
Cdd:COG4942 187 R---AALEALKAERQKLLARLEKELAEL----AAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1396-1939 |
8.37e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1396 TIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNI-- 1473
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLeg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1474 SARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQV-- 1551
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIke 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1552 -EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKqralavaAKK 1630
Cdd:PRK03918 333 lEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1631 KMEMDLKDLE---GQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASR--DEIFAQSKESEKKLKGLEAEILQLQEE 1705
Cdd:PRK03918 402 EIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1706 FAASERARRHAEQER--DELADEIANSASGKSALLDEKRRLEARiaqleeeleeeqsNMELLNERFRKTTLQVDTLNSEL 1783
Cdd:PRK03918 482 LRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAE-------------EYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1784 agerSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEqLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:PRK03918 549 ----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKK 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1864 VFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1939
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
893-1485 |
2.11e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 893 QQLLEEKNIL--AEQLQaetELFAEAEEMRARLA-AKKQE--LEEILhDLESRVEEEEERNQILQNEKKKMQghiqdlee 967
Cdd:COG4913 215 EYMLEEPDTFeaADALV---EHFDDLERAHEALEdAREQIelLEPIR-ELAERYAAARERLAELEYLRAALR-------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 968 qldeEEGARQKLQLekvtAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEeeKAKNLAKLKNKqemmIT 1047
Cdd:COG4913 283 ----LWFAQRRLEL----LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN--GGDRLEQLERE----IE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1048 DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeavqknnALKVIRELQ 1127
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE----------AEAALRDLR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1128 AQIAELQEDLESEKASRN----KAEKQKRDLSEELEALKTEL-----------EDTLDTTAAQQELRTKR------EQEV 1186
Cdd:COG4913 419 RELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEAELpfvgelievrpEEERWRGAIERVLGGFAltllvpPEHY 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1187 AELKKAIEE---------------------------------ETKNHEAQ---IQEIRQRHATALEELSEQLEQAKRF-- 1228
Cdd:COG4913 499 AAALRWVNRlhlrgrlvyervrtglpdperprldpdslagklDFKPHPFRawlEAELGRRFDYVCVDSPEELRRHPRAit 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1229 KANLEKNKQGL-ESDNKELACEVKVLQQvkaESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLE 1307
Cdd:COG4913 579 RAGQVKGNGTRhEKDDRRRIRSRYVLGF---DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1308 EAEKKgikfaKDAASLESQLQDTQELLQ--EETRQKL-NLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLA 1384
Cdd:COG4913 656 YSWDE-----IDVASAEREIAELEAELErlDASSDDLaALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1385 EAKKKVDD-----DLGTIEGLEENKKKLLKD--MESLSQRLEEKamaYDKLEKTKNRLQQELDDLM-----------VDL 1446
Cdd:COG4913 731 ELQDRLEAaedlaRLELRALLEERFAAALGDavERELRENLEER---IDALRARLNRAEEELERAMrafnrewpaetADL 807
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1447 D------------HQRQIVSNLEKKQKKFDQMLAEE-----KNISARYAEERDRAE 1485
Cdd:COG4913 808 DadleslpeylalLDRLEEDGLPEYEERFKELLNENsiefvADLLSKLRRAIREIK 863
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
858-1472 |
4.33e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 858 TRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 937
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 938 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ-----------------LEKVTAEAKIKKMEEEILLL 1000
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQknidkiknkllklelllSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1001 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNlakLKNKQEMMITDLEERlkkeektRQELEKAKRKLDgettDLQDQ 1080
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ---LKDEQNKIKKQLSEK-------QKELEQNNKKIK----ELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQlakKEEELqaalargdeeavqknnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1160
Cdd:TIGR04523 290 LNQLKSEISDLNNQ---KEQDW--------------------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1161 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIE---EETKNHEAQIQEIRQrhataleelseQLEQAKRFKANLEKNKQ 1237
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1238 GLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFA 1317
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1318 KDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQeeeeearKNLEKQMLALQAQL--AEAKKKVDDDLG 1395
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNK 568
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1396 TIEGLEENKKKLLKDMESLSQRLeekamayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKN 1472
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1048-1222 |
5.18e-12 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 67.64 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1048 DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKViRELQ 1127
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1128 AqiaeLQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKAIEEETKNHEAQIQEI 1207
Cdd:COG1579 93 A----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170
....*....|....*
gi 212450 1208 RQRHATALEELSEQL 1222
Cdd:COG1579 162 EAEREELAAKIPPEL 176
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
870-1442 |
5.84e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.41 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 870 ELMKVKEKQTKVEAELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAA---KKQELEEILHDLESRVE 942
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKAltgKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 943 EEEERNQILQNEKKKMQghiqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEI-LLLEDQNSKFLKEKKLMEDRIAEC 1021
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI----------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1022 TSQLAE---EEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQIEELKIQL 1095
Cdd:pfam12128 450 KLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1096 AKKEEELQAALA------------------------------------------RGDEEAVQKNNALKVIRELQAQIAEL 1133
Cdd:pfam12128 530 FPQAGTLLHFLRkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELRERLDKA 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1134 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKAIEEETKNHEA 1202
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1203 QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGlESDNKelacevkvLQQVKAESEHKRKKLDAQVQEL-TAKVTEG 1281
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG-ALDAQ--------LALLKAAIAARRSGAKAELKALeTWYKRDL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1282 ERLRVElAEKANKLQNELDNVSSLLEEAEKKGikfaKDAASLESQLQDTqeLLQEETRQKLNLSSRIRQLEEEKNNLQEQ 1361
Cdd:pfam12128 761 ASLGVD-PDVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLATQLSNIERAISELQQQLARL 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1362 QEEEEEARKNLEKQMLALQAQLAEAK---KKVDDDLGTIEGLEENKKKLLKDMeSLSQRLEEKAMAYDKLEKTKNRLQQE 1438
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSenlRGLRCEMSKLATLKEDANSEQAQG-SIGERLAQLEDLKLKRDYLSESVKKY 912
|
....
gi 212450 1439 LDDL 1442
Cdd:pfam12128 913 VEHF 916
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1019-1750 |
6.02e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.52 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1019 AECTSQLAEEEEK----AKNLAKLKNKQEMMITDLE---ERL----------KKEEKTRQELEKAKRKLD---GETTDLQ 1078
Cdd:COG3096 295 FGARRQLAEEQYRlvemARELEELSARESDLEQDYQaasDHLnlvqtalrqqEKIERYQEDLEELTERLEeqeEVVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1079 DQIAELQAQ-------IEELKIQLAkkeeELQAALARGDEEAVQKNNALKVIRELQAQ--------------IAELQEDL 1137
Cdd:COG3096 375 EQLAEAEARleaaeeeVDSLKSQLA----DYQQALDVQQTRAIQYQQAVQALEKARALcglpdltpenaedyLAAFRAKE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1138 ESEKASRNKAEkQKRDLSEE-----------LEALKTELEDTLDTTAAQQELRTKREQEvAELKKAIEEETKNHEAQIQE 1206
Cdd:COG3096 451 QQATEEVLELE-QKLSVADAarrqfekayelVCKIAGEVERSQAWQTARELLRRYRSQQ-ALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1207 IRQRHATAL-EELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKvtegERLR 1285
Cdd:COG3096 529 RQQQNAERLlEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAAR----APAW 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1286 VELAEKANKLQNELdnvsslleeaekkGIKFAkDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEqqeee 1365
Cdd:COG3096 605 LAAQDALERLREQS-------------GEALA-DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ----- 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1366 eeARKNLEKQMLALQAQ------------------------------------LAEAKKKVD------DDLGTIEGLEEN 1403
Cdd:COG3096 666 --PGGAEDPRLLALAERlggvllseiyddvtledapyfsalygparhaivvpdLSAVKEQLAgledcpEDLYLIEGDPDS 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1404 KKKLLKDMESLSQ----RLEEKAMAYDKL-----------EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1468
Cdd:COG3096 744 FDDSVFDAEELEDavvvKLSDRQWRYSRFpevplfgraarEKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1469 EEKNIsaryAEERDrAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEK-SKRTL 1547
Cdd:COG3096 824 GHLAV----AFAPD-PEAELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLlADETL 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1548 EQQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFERdLQARDEQNEEKKRMLVKQVRELEaeledERKQ 1621
Cdd:COG3096 892 ADRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLKQQIFALS-----EVVQ 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1622 RALAVAAKKKMEM-----DLKD-LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGL 1695
Cdd:COG3096 966 RRPHFSYEDAVGLlgensDLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1696 EAEILQLQEEFAASERARRHAeqerdeladEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:COG3096 1046 GVQADAEAEERARIRRDELHE---------ELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1050-1880 |
6.23e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.52 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1050 EERLKKEEKT---RQELEKAKRKLDGEttdlQDQIAELQAQIEELKIQLAKKEEELQAA---LARGdEEAVQKNNAlkvI 1123
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAAsdhLNLV-QTALRQQEK---I 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1124 RELQAQIAELQEDLESEKASRNKAEKQKrdlsEELEALKTELEDTLDTTAAQqelrtkreqeVAELKKAIEEEtknheaQ 1203
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEEAAEQL----AEAEARLEAAEEEVDSLKSQ----------LADYQQALDVQ------Q 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1204 IQEIRQRHA-TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1282
Cdd:COG3096 410 TRAIQYQQAvQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1283 RLR-----VELAEKANKLQNELDNVSSL---LEEAEKkgikfakdaasLESQLQDTQELLQE-ETRQKLNLSSRIR---- 1349
Cdd:COG3096 490 RSQawqtaRELLRRYRSQQALAQRLQQLraqLAELEQ-----------RLRQQQNAERLLEEfCQRIGQQLDAAEEleel 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1350 --QLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLE----------ENKKKLLKDMESLSQR 1417
Cdd:COG3096 559 laELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1418 LEEKAMAYDKLEKTKNRLQQElddlmvdldhqrqiVSNLEKKQKKFD---QMLAEEKN------------------ISAR 1476
Cdd:COG3096 639 EREATVERDELAARKQALESQ--------------IERLSQPGGAEDprlLALAERLGgvllseiyddvtledapyFSAL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1477 YAEER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK-- 1542
Cdd:COG3096 705 YGPARhaivvpD-------------LSAVK-------------EQLAGLEDCPEDLYliegdpDSFDDSVFDAEELEDav 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1543 ----SKRTL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDL-----QARDEQ 1596
Cdd:COG3096 759 vvklSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVgghlaVAFAPD 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1597 NEEKKRMLVKQVRELEAELED----ERKQRALAVAAKKKMEMdlkdLEGQIEAANKARDEAikqlrkLQAQMKDYQRELE 1672
Cdd:COG3096 834 PEAELAALRQRRSELERELAQhraqEQQLRQQLDQLKEQLQL----LNKLLPQANLLADET------LADRLEELREELD 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1673 EARASRDEIFAQSK---ESEKKLKGLEAEILQ---LQEEFAASERARRHAEQERDELADEIANSA----SGKSALLDEKR 1742
Cdd:COG3096 904 AAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGLLGENS 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1743 RLEARIAQLEEELEEEQSNmelLNERFRKTTLQVDTLNSELAGERSAAQkseNARQQLerqnKELKAKLQELEGSV---- 1818
Cdd:COG3096 984 DLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSRD---AKQQTL----QELEQELEELGVQAdaea 1053
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1819 -------KSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKevfmqveDERRHADQYKE 1880
Cdd:COG3096 1054 eerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
774-1161 |
8.14e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 774 GQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRgylARKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKP 853
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 854 LLQ-VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfaeaeemrarlaaKKQELEE 932
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--------------ALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 933 ILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEeqldeeegarqklqlekvtaeAKIKKMEEEILLLEDQnskflkekk 1012
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLE---------------------EQIEELSEDIESLAAE--------- 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1013 lmedrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK 1092
Cdd:TIGR02168 861 -----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1093 IQLAKKEEELQAALARGDEEAVQKNNALKV--------IRELQAQIAEL-------QEDLESEKASRNKAEKQKRDLSEE 1157
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDdeeearrrLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEA 1015
|
....
gi 212450 1158 LEAL 1161
Cdd:TIGR02168 1016 KETL 1019
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1645-1863 |
8.79e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.02 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1645 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1724
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1725 DEIANSASGKSALLDE----KRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQL 1800
Cdd:COG4942 97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1801 ERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:COG4942 177 EALLAELEEERAALE-ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
857-1459 |
1.58e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 69.82 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 857 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILHD 936
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNRL---QQELDDLLVD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 937 LESrveeeeeRNQILQNEKKKMQG-----------HIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------- 994
Cdd:pfam01576 589 LDH-------QRQLVSNLEKKQKKfdqmlaeekaiSARYAEERDRAEAEAREKetraLSLARALEEALEAKEElertnkq 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 995 -----EEILLLEDQNSKFLKE----KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEK 1065
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1066 AKRKLdgettdLQDQIAELQAQIEELKIQLA-------KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLE 1138
Cdd:pfam01576 742 EKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1139 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQ---RHATAL 1215
Cdd:pfam01576 816 EARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRleaRIAQLE 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1216 EELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELTAKVTEgerlrvelaekankl 1295
Cdd:pfam01576 896 EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE--------------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1296 qneldnvsslLEEAEKKgiKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnlqeqqeeeeearknlekq 1375
Cdd:pfam01576 957 ----------MEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK---------------------- 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1376 mlalqaQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSN 1455
Cdd:pfam01576 1003 ------KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVST 1076
|
....
gi 212450 1456 LEKK 1459
Cdd:pfam01576 1077 LKSK 1080
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
2.51e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 60.14 E-value: 2.51e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 212450 31 TAKKLVWIPSERHGFEAASIKEERGDEVLVELaENGKKALVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
904-1277 |
2.69e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 69.00 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 904 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQGHIQDLEEQLDEEEG 974
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQLEKVTAEAKIKKmeEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAE--EEEKAKNLAKLKNKQEMMItdleER 1052
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQIEELK--------IQLAKKEEELQAALARGDEEAVQKNNALKVIR 1124
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1125 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQI 1204
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1205 QEIRQRHATALEELSEQLEQAKRFKANLEKNKQglesdnkelacEVKVLQQVKaESEHKRKKLDAQVQELTAK 1277
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----------EREMMRQIV-ESEKARAEYEATTPITTIK 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1078-1322 |
2.77e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1078 QDQIAELQAQIEELKIQLAKKEEELQAALArgdeeavQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEE 1157
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKK-------EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1158 LEALKTELEdtldttaaqqelrtKREQEVAELKKAIEEETKNHEAQI---QEIRQRHATALEELSEQLEQAKRFKANLEK 1234
Cdd:COG4942 92 IAELRAELE--------------AQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1235 NKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGI 1314
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
....*...
gi 212450 1315 KFAKDAAS 1322
Cdd:COG4942 238 AAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1263-1720 |
3.00e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.64 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1263 KRKKLDAQVQELTAKVTEGERLRVELAEkankLQNELDNVSSLLEEAEKKGIKFAKDAASLEsQLQDTQELLQEETRQKL 1342
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1343 NLSSRIRQLEEEKNNLQeqqeeeeeARKNLEKQMLALQAQLAEAKKKVDddlgtiEGLEENKKKLLKDMESLSQRLEEKA 1422
Cdd:COG4717 140 ELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELE------ELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1423 MAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM------------LAEEKNISARYAEERDRAEAEARE 1490
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1491 KETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ--AT 1568
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1569 EDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELEDERK--QRALAVAAKKKMEMDLKDLEGQIEAA 1646
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQE-LKEELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1647 NKARDEAIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKGLEAEILQLQEEFAASERARRHAEQER 1720
Cdd:COG4717 445 EEELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
862-1280 |
3.31e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.51 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 862 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 936
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 937 LESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1016
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1017 RIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA 1096
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1097 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTAA 1174
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1175 QQELRTKREQEVAELKKAIEEETKnheaqiqeirqrhatALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ 1254
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
410 420
....*....|....*....|....*.
gi 212450 1255 QVKAESEHKRKKLDAQVQELTAKVTE 1280
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1042-1294 |
3.31e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 67.48 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1042 QEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeavqknnalk 1121
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1122 vIRELQAQIAELQEDLesekasrnkaEKQKRDLSEELEAL-KTELEDTLDTTAAQQELrtKREQEVAELKKAIEEETKNH 1200
Cdd:COG4942 85 -LAELEKEIAELRAEL----------EAQKEELAELLRALyRLGRQPPLALLLSPEDF--LDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1201 EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVte 1280
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI-- 229
|
250
....*....|....
gi 212450 1281 gERLRVELAEKANK 1294
Cdd:COG4942 230 -ARLEAEAAAAAER 242
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
856-1241 |
3.55e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 935
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 936 DLESRVEEEEERNQILQNEKKKMQGHIQDLE--EQLDEEEGARQKLQLEKvtAEAKIKKMEEEILLLEDQNSKFLKEKKL 1013
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKcpECGQPVEGSPHVETIEE--DRERVEELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1014 MEDrIAECTSQLAEEEEKAKNLAKLknkqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKI 1093
Cdd:PRK02224 501 AED-LVEAEDRIERLEERREDLEEL-------IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1094 QLAKKEEELQAALARGDeeavqknnALKVIRELQAQIAELQEDLES---EKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:PRK02224 573 EVAELNSKLAELKERIE--------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 1171 tTAAQQELRTKREQEVAELKKaIEEETKNHEAQIQEIRQRHATALEELsEQLEQAKRFKANLEKNKQGLES 1241
Cdd:PRK02224 645 -EARIEEAREDKERAEEYLEQ-VEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALENRVEALEA 712
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1214-1937 |
3.95e-11 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 68.53 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1214 ALEELSEQLEQAKRFKANLEKNKQGLESDNKELA---CEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAE 1290
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQehqMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1291 KANKLQNELDNVSSLLEeaekkgikfakdaaslesqLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLQEQQEEEEEARK 1370
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMK-------------------LDNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNDLYH 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1371 NLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLS---QRLEEKAMAYDkLEKTKNRLQQELDDLMVDLD 1447
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlqaDRHQEHIRARD-SLIQSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1448 HQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1527
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1528 SSKDDVGKNVHELEKSKRTLEQQveemrtqleeledELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR----- 1602
Cdd:TIGR00606 468 GSSDRILELDQELRKAERELSKA-------------EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttr 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1603 ----MLVKQVRELEAELEDERKQRALAVAA---------------------KKKMEMDLKDLEGQIEAANKARDEAIKQL 1657
Cdd:TIGR00606 535 tqmeMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkqledwlhskskeINQTRDRLAKLNKELASLEQNKNHINNEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1658 RKLQAQMKDYQRELEEARASRDE------IFAQSKESEKKLKGLEAE-------ILQLQEEFAASERARRHAEQERDELA 1724
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCGSQDEesdlerLKEEIEKSSKQRAMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAELQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1725 DEIANSASGKSALLDEKRRLEARIAQLEEELEE-------EQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSEnar 1797
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE--- 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1798 QQLERQNKELK-AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAA--NKLVRRTEKKLKEVFMQVEDERRH 1874
Cdd:TIGR00606 772 TLLGTIMPEEEsAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKL 851
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1875 ADQYKEQMEKANARMKQLKRQleeaEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1937
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSE----KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
862-1280 |
9.77e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.05 E-value: 9.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 862 EELQAKDEELMKVKEKQTKVEAE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 930
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 931 EEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLK- 1009
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1010 ----EKKLMEDR--IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1083
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1084 LQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKT 1163
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1164 ELEDTLDTTAAQQELRTKREQ--------------EVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK 1229
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY 730
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1230 ANLEKN----KQGLESDNKELACE-VKVLQQVKAESEHKrKKLDAQVQELTAKVTE 1280
Cdd:pfam05483 731 KNKEQEqssaKAALEIELSNIKAElLSLKKQLEIEKEEK-EKLKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1019-1748 |
1.52e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 66.90 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1019 AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERL-----------------KKEEKTRQELEKAKRKL----------D 1071
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtalrqqEKIERYQADLEELEERLeeqnevveeaD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1072 GETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1151
Cdd:PRK04863 376 EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTR----AIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1152 RDLSEELEALKTELEDTLDT----TAAQQELRT-------KREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSE 1220
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAhsqfEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1221 Q------LEQA-KRFKANLEKNKQgLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerlrveLAEKAN 1293
Cdd:PRK04863 532 QqraerlLAEFcKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR-------LAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1294 KLQNELDNVSSLLEEAekkGIKFAkDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1373
Cdd:PRK04863 604 AWLAAQDALARLREQS---GEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALA 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1374 KQM--------------------LALQAQLAEAkkKVDDDLGTIEGLEENKKKLLKDM---------------------E 1412
Cdd:PRK04863 680 ERFggvllseiyddvsledapyfSALYGPARHA--IVVPDLSDAAEQLAGLEDCPEDLyliegdpdsfddsvfsveeleK 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1413 SLSQRLEEKAMAYDKL-----------EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEER 1481
Cdd:PRK04863 758 AVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEA 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1482 DRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRTLEQQVEEMRTQLEE 1560
Cdd:PRK04863 838 ELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQLDE 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1561 LEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELeaeleDERKQRALAVAAKKKMEM 1634
Cdd:PRK04863 906 AEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAAEM 979
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1635 DLKD------LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLkgleaEILQLQEEFAA 1708
Cdd:PRK04863 980 LAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL-----QDLGVPADSGA 1054
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 212450 1709 SERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1748
Cdd:PRK04863 1055 EERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1518-1940 |
2.70e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1518 QLRADMEDLMSSKDDVGKnvheLEKSKRTLEQqVEEMRTQLEELEDELQATEDAKLRLEVnmqAMKAQFERDLQARDEQN 1597
Cdd:COG4913 229 ALVEHFDDLERAHEALED----AREQIELLEP-IRELAERYAAARERLAELEYLRAALRL---WFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 EEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMD-LKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQrelEEARA 1676
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAALG---LPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1677 SRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELe 1756
Cdd:COG4913 378 SAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD- 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1757 eeQSNM----ELL-----NERFR----------KTTLQVDT------------------LNSELAGERSAAQKSENA--- 1796
Cdd:COG4913 457 --EAELpfvgELIevrpeEERWRgaiervlggfALTLLVPPehyaaalrwvnrlhlrgrLVYERVRTGLPDPERPRLdpd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1797 -----------------RQQLERQNKELK-AKLQEL---------EGSVKSKF---------------------KATIST 1828
Cdd:COG4913 535 slagkldfkphpfrawlEAELGRRFDYVCvDSPEELrrhpraitrAGQVKGNGtrhekddrrrirsryvlgfdnRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1829 LEAKIAQLEEQLEQEAKERAAANKLVRRTEK------KLKEVF------MQVEDERRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQErrealqRLAEYSwdeidvASAEREIAELEAELERLDASSDDLAALEEQL 694
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 212450 1897 EEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
977-1722 |
4.10e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.13 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 977 QKLQLEKVTAEAKIK----KMEEEILLLEDQNsKFLKEKKLMEDRIaecTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1052
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALaRGDEEAVQKnnalkVIRELQAQIAE 1132
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKL-KEDHEKIQH-----LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1133 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEetknheaqIQEIRQRHA 1212
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1213 TALEELSEQLEQAKRFKANLEKNKQG-LESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEK 1291
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1292 anklqneldnvSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLQEQQEEEEEARKN 1371
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1372 LEKQMLALQAQLAEAKKKVDDDLGTIEGLE-ENKKKLLKDMESLSQRleekamayDKLEKTKNRLQQELDDLMVDLDHQR 1450
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1451 QIVSNLEKKQKKfdqMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSK 1530
Cdd:pfam05483 520 EDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1531 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRE 1610
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1611 LEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRdeifaqskesEK 1690
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EI 746
|
730 740 750
....*....|....*....|....*....|..
gi 212450 1691 KLKGLEAEILQLQEEFAASERARRHAEQERDE 1722
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1538-1940 |
5.57e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1538 HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnmqamkAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1617
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL------YQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1618 ERKQRALAVAAKKKMEMDLKDL----EGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLK 1693
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1694 GLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTT 1773
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1774 LQVDTLNSELAGE--RSAAQKSENARQQLERQNK-ELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAA 1850
Cdd:COG4717 325 LAALGLPPDLSPEelLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1851 NKLVRRTEKKLKEVFMQVEDERRhadqykeqmEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLS 1928
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDE---------EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELL 475
|
410
....*....|..
gi 212450 1929 REVSTLKNRLRR 1940
Cdd:COG4717 476 QELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1192-1422 |
6.28e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1192 AIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQV 1271
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1272 QELTAKVtegERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1351
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 1352 EEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKA 1422
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1049-1226 |
6.79e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1049 LEERLkkeEKTRQELEKAKRKL------------DGETTDLQDQIAELQAQIEELKIQLAKKE---EELQAALARGDEEA 1113
Cdd:COG3206 180 LEEQL---PELRKELEEAEAALeefrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEarlAALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1114 VQKNNAlKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR-EQEVAELKKA 1192
Cdd:COG3206 257 PELLQS-PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAlQAREASLQAQ 335
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 212450 1193 IEEETK------NHEAQIQEIRQRHATA---LEELSEQLEQAK 1226
Cdd:COG3206 336 LAQLEArlaelpELEAELRRLEREVEVArelYESLLQRLEEAR 378
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
976-1224 |
8.37e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 976 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRI--AECTSQLAEEEEKAKNLAKLKNKqemmITDLEERL 1053
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDD----LAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1054 KKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAEL 1133
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEER 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1134 QEDLESEKA-SRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQE-----VAELKKAIEEETKNH------- 1200
Cdd:COG4913 775 IDALRARLNrAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDglpeyEERFKELLNENSIEFvadllsk 854
|
250 260
....*....|....*....|....*
gi 212450 1201 -EAQIQEIRQRhataLEELSEQLEQ 1224
Cdd:COG4913 855 lRRAIREIKER----IDPLNDSLKR 875
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1147-1896 |
9.60e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 64.22 E-value: 9.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1147 AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKREQEVAELKKAIEEEtknheaqiQEIRQRHATALEELSEQLEQA 1225
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQlLTLCTPCMPDTYHERKQVLEKELKHLREAL--------QQTQQSHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1226 KRFKANleknkqglesdnKELACEVKVLQQVKAESEHKRKKLDAQVQelTAKVTEGERLRVELAEKANKLQNELDNVSSL 1305
Cdd:TIGR00618 257 KKQQLL------------KQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1306 LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQklnlssrirqleEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAE 1385
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI------------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1386 AKKKVDDDLGTIEGLEENKKKLlkDMESLSQRLEEKAMAydKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1465
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLA--HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1466 MLAEEKNisaryaEERDRAEAEAREKETKALSLARALEEALEAKEEFER-----QNKQLRADMEDLMSSKDDVGKNVHEL 1540
Cdd:TIGR00618 467 SLKEREQ------QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpnPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1541 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkrmlvkqvreLEAELEDERK 1620
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-----------TEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1621 QRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES-EKKLKGLEAEI 1699
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEK 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1700 LQL---QEEFAASERARRHAEQ---ERDELADEIANSASGKSALLDekrrleariAQLEEELEEEQSNMELLNERFRKTT 1773
Cdd:TIGR00618 690 EQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLA---------AREDALNQSLKELMHQARTVLKART 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1774 LQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELegsvkskfkatistleakiAQLEEQLEQEAKEraaankl 1853
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL-------------------KTLEAEIGQEIPS------- 814
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 212450 1854 vrrtekKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:TIGR00618 815 ------DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
861-1227 |
1.08e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEAELEEMER--KHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 938
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 939 SrveEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRI 1018
Cdd:COG4717 174 E---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1019 -------------------------------------------AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLK- 1054
Cdd:COG4717 251 llliaaallallglggsllsliltiagvlflvlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGl 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1055 KEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEE--LQAALARGDEEAVQKNNALKVIRELQAQIAE 1132
Cdd:COG4717 331 PPDLSPEELLELLDRIE----ELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1133 LQEDLESEKASRNKAEKQkrdlsEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEaqIQEIRQRHA 1212
Cdd:COG4717 407 LEEQLEELLGELEELLEA-----LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELE 479
|
410
....*....|....*
gi 212450 1213 TALEELSEQLEQAKR 1227
Cdd:COG4717 480 ELKAELRELAEEWAA 494
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1125-1916 |
1.32e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 63.53 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1125 ELQAQIAELQEDLESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE 1201
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1202 AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELTAkvte 1280
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1281 geRLRVELAEKANKLQNELDNVSSLLEEAEKKGikfAKDAASLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEKnn 1357
Cdd:TIGR00606 376 --RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI-- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1358 lqeqqeeeeearknLEKQmlalQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSqRLEEKAMAYDKLEKTKNRLQQ 1437
Cdd:TIGR00606 449 --------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1438 ELDdlmvdldhqrqivsnLEKKQKKFDQMLAEEKnisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQNK 1517
Cdd:TIGR00606 510 KAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1518 QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQARDEQn 1597
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ- 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 eekkrmlvkqvrelEAELEDerkqRALAVAAKKKMEMDLKDLEGQIEAANKardeaikQLRKLQAQMKDYQRELEEARAS 1677
Cdd:TIGR00606 621 --------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1678 R-------DEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:TIGR00606 676 NqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1751 LEEELEEEQSNMELlNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVK----SKFKATI 1826
Cdd:TIGR00606 756 VNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEK 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1827 STLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRA 1906
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914
|
810
....*....|
gi 212450 1907 NASRRKLQRE 1916
Cdd:TIGR00606 915 ETFLEKDQQE 924
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
988-1358 |
1.76e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.86 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 988 AKIKKMEEEILLLEDQNSKF---LKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMM---------ITDLEERLKK 1055
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYaelQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYqelealeaeLAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1056 EEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQL-AKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQ 1134
Cdd:COG4717 151 LEERLEELRELEEELE----ELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1135 EDLESEKASRNKAEKQKRDLSEE----LEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQR 1210
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARllllIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1211 HATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELT-------AKVTEGER 1283
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiaallaeAGVEDEEE 386
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1284 LR--VELAEKANKLQNELDNVSSLLEEAEKKGIKFAK--DAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1358
Cdd:COG4717 387 LRaaLEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1638-1940 |
1.80e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1638 DLEGQIEAANKARDEAIKQLrklqAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1717
Cdd:TIGR02169 143 DVTDFISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1718 QERDELADEIANSasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERfrkttlqvdtlnselagersaaqkSENAR 1797
Cdd:TIGR02169 219 EKREYEGYELLKE---KEALERQKEAIERQLASLEEELEKLTEEISELEKR------------------------LEEIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1798 QQLERQNKELKAKLQELEGSVKSK---FKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRH 1874
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1875 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1518-1850 |
2.47e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 61.62 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1518 QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQARDEQN 1597
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 EEKK---RMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1674
Cdd:pfam19220 107 EELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1675 RASRDEIFAQSKESEKKLKGLEAEILQLQ----EEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1751 LEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQ-----------NKELKAKLQELEGSVK 1819
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraeleeraemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 212450 1820 S-------------KFKATISTLEAKIAQLEEQLEQEAKERAAA 1850
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1484-1709 |
2.47e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1484 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELED 1563
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1564 ELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLV----------KQVRELEAELEDERKQRALAVAAKKKME 1633
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1634 MDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKGLEAEILQLQEEFAAS 1709
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL-------EALIARLEAEAAAAAERTPAA 246
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1695-1937 |
3.02e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1695 LEAEILQLQEEFAASERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTtl 1774
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1775 QVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLV 1854
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1855 RRTEkklkevfMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVSTL 1934
Cdd:COG4913 369 AALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIASL 431
|
...
gi 212450 1935 KNR 1937
Cdd:COG4913 432 ERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1514-1735 |
4.49e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1514 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQAR 1593
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1594 DEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1673
Cdd:COG4942 114 YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212450 1674 ARASRDEIFAQskeSEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKS 1735
Cdd:COG4942 193 LKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
856-1387 |
5.06e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 931
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 932 EILHDLESRVEEEEernQILQNEKKKMQGHIQDLEEQLDEEEgaRQKLQLEKVTAEAKIKKME-EEILLLEDQNSKFLKE 1010
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1011 KKLMEdRIAEctsqlaEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEE 1090
Cdd:pfam05483 424 KKQFE-KIAE------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1091 LKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQedlESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1170
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1171 TTAAQQELRTKREQEVAELKKA---IEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1247
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1248 CEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKlqneldNVSSLLEEAEKKGIKFAKDAASLESQL 1327
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH------KIAEMVALMEKHKHQYDKIIEERDSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1328 QDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAK 1387
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1035-1478 |
5.48e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.32 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1035 LAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTD---LQDQIAELQAQIEELKIQLAKKEEELQAAlargdE 1111
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKL-----E 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1112 EAVQKNNALKVIRELQAQIAELQEDLESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQEVAELKK 1191
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEELLEQLSL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1192 AIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKE--------------LACEVKVLQQVK 1257
Cdd:COG4717 189 ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaALLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1258 AESEHKRKKLDAQVQELTA----------KVTEGERLRVELAEKANKLQNEldNVSSLLEEAEKKGIKFAKDAASLESQL 1327
Cdd:COG4717 269 LSLILTIAGVLFLVLGLLAllflllarekASLGKEAEELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1328 QDTQELLQEetRQKLNLSSRIRQLEEEKNNLQEQ-----------QEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGT 1396
Cdd:COG4717 347 EELQELLRE--AEELEEELQLEELEQEIAALLAEagvedeeelraALEQAEEYQELKEELEELEEQLEELLGELEELLEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1397 iegleENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDldhqrqivSNLEKKQKKFDQMLAEEKNISAR 1476
Cdd:COG4717 425 -----LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED--------GELAELLQELEELKAELRELAEE 491
|
..
gi 212450 1477 YA 1478
Cdd:COG4717 492 WA 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1492 |
5.48e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.60 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 850 KVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERK---HQQLLEEKNILAEQLQAETELFAEAEEMRAR---- 922
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhht 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 923 --------LAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME 994
Cdd:TIGR00606 532 ttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 995 EEILLLEDQNSKFlkekklmEDRIAECTSQLAEE----------EEKAKNLAKLKNKQEMMITDLEERLKKEEK---TRQ 1061
Cdd:TIGR00606 612 NELESKEEQLSSY-------EDKLFDVCGSQDEEsdlerlkeeiEKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQ 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1062 ELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEK 1141
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1142 ASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR---TKREQEVAELKKAIEEETKNheaQIQEIRQRHATALEEL 1218
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKdveRKIAQQAAKLQGSDLDRTVQ---QVNQEKQEKQHELDTV 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1219 SEQLEQAKRFKANLEKNKQGLESDNKELACE---VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKL 1295
Cdd:TIGR00606 842 VSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1296 QNELDNVSSLLEEAEKKGikfakdaaslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqqeeeeeaRKNLEKQ 1375
Cdd:TIGR00606 922 QQEKEELISSKETSNKKA----------QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY-------------LKQKETE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1376 MLALQAQLAEA---KKKVDDDLGTIEG---LEENKKKLLKDMESLSQRLEEkamaYDKLEKTKNRLQQELDDLMVdldhq 1449
Cdd:TIGR00606 979 LNTVNAQLEECekhQEKINEDMRLMRQdidTQKIQERWLQDNLTLRKRENE----LKEVEEELKQHLKEMGQMQV----- 1049
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 212450 1450 RQIVSNLEKKQKKFDQMLAEEKNISAR---YAEERDRAEAEAREKE 1492
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGRqkgYEKEIKHFKKELREPQ 1095
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
951-1175 |
5.60e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 951 LQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEE 1030
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1031 KaknLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGD 1110
Cdd:COG4942 105 E---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1111 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1175
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1050-1322 |
5.83e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 5.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1050 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeavqknnalkvIRELQAQ 1129
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE--------------IAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1130 IAELQEDLesekASRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelkkaieeetknheaqIQEI 1207
Cdd:COG3883 81 IEERREEL----GERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------LSKI 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1208 RQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVE 1287
Cdd:COG3883 128 ADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
250 260 270
....*....|....*....|....*....|....*
gi 212450 1288 LAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAAS 1322
Cdd:COG3883 208 AEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1119-1378 |
7.62e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 7.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1119 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRtKREQEVAELKKAIEEetk 1198
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA------ALARRIR-ALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1199 nHEAQIQEIRQRHATALEELSEQLEQAKRFkANLEKNKQGLESDNKELAceVKVLQQVKAESEHKRKKLDAQVQELTakv 1278
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDA--VRRLQYLKYLAPARREQAEELRADLA--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1279 tegerlrvELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1358
Cdd:COG4942 161 --------ELAALRAELEAERAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260
....*....|....*....|
gi 212450 1359 QEQQEEEEEARKNLEKQMLA 1378
Cdd:COG4942 226 EALIARLEAEAAAAAERTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1640-1863 |
9.45e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 9.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1640 EGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFaaserarrhaEQE 1719
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1720 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAqks 1793
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAEL--- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1794 ENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELE-AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1376-1863 |
2.40e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1376 MLALQAQLAEAKKKVDDDLGTIEG-LEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1454
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGrKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1455 NLEKKQKKFDQMLAEEK------NISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1528
Cdd:COG4717 120 KLEKLLQLLPLYQELEAleaelaELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1529 SKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRM----- 1603
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvl 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1604 ------LVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1677
Cdd:COG4717 280 flvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1678 RDEIfaqskesekKLKGLEAEILQLQEEFAASERARRHAEQERDELADEiansasgksaLLDEKRRLEARIAQLEEELEE 1757
Cdd:COG4717 360 EEEL---------QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE----------LKEELEELEEQLEELLGELEE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1758 EQSnmellnerfrktTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvkskfkATISTLEAKIAQLE 1837
Cdd:COG4717 421 LLE------------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED------GELAELLQELEELK 482
|
490 500
....*....|....*....|....*....
gi 212450 1838 EQLEQEAKERAAAN---KLVRRTEKKLKE 1863
Cdd:COG4717 483 AELRELAEEWAALKlalELLEEAREEYRE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
975-1354 |
2.94e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQLEKVTAEAKIKKMEEEILLLED--QNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1052
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGD--EEAVQKNNALKVIRELQ--A 1128
Cdd:COG4717 176 QEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKEARllL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1129 QIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR 1208
Cdd:COG4717 253 LIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1209 QRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEvKVLQQVKAESEHKRKKLDAQVQELtakvtegERLRVEL 1288
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEY-------QELKEEL 404
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1289 AEKANKLQNELDNVSSLLEEAEKKGIKfaKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEE 1354
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEED 468
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1102-1340 |
3.52e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1102 LQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqqelrtk 1181
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1182 rEQEVAELKKAIEEETKNHEAQIQEIRQRhATALEELSEQLEQAKRFKAN----LEKNKQGLESDNKELACEVKVLQQVK 1257
Cdd:COG4942 82 -EAELAELEKEIAELRAELEAQKEELAEL-LRALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1258 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1337
Cdd:COG4942 160 AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
...
gi 212450 1338 TRQ 1340
Cdd:COG4942 240 AER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
897-1117 |
3.84e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 897 EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-- 974
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM---------EDRIAECTSQLAEEEEKAKNLAKLKNKQEMM 1045
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212450 1046 ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKN 1117
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
860-1090 |
5.60e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 5.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 860 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELEEILH 935
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 936 DLESRVEEEEERNQILQneKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAE--AKIKKMEEEILLLEDQNSKFLKEKKL 1013
Cdd:COG4942 98 ELEAQKEELAELLRALY--RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArrEQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1014 MEdriaectSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRkldgettDLQDQIAELQAQIEE 1090
Cdd:COG4942 176 LE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE-------ELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1495-1736 |
5.85e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1495 ALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1574
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1575 LEVNMQAMKAQferdLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAI 1654
Cdd:COG4942 88 LEKEIAELRAE----LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1655 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGK 1734
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
..
gi 212450 1735 SA 1736
Cdd:COG4942 244 PA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1077-1863 |
6.46e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.81 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1077 LQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL----KVIRELQAQIAELQEDLESEKASRNKAEKQKR 1152
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLqenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1153 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIqeirqrhaTALEELSEQLEQAK-RFKAN 1231
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1232 LEKNKQGLESDNKELACEVKvlqqvkaESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1311
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1312 KGIKFAKDAASLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1388
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1389 KVDddlgtiEGLEENKKKLlkdmESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1468
Cdd:pfam05483 367 TEQ------QRLEKNEDQL----KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1469 EEKNISARYaeerdraeaEAREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLE 1548
Cdd:pfam05483 437 KEQELIFLL---------QAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1549 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQARDEQnEEKKRMLVKQVRELEAELEderkqralavaa 1628
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDEL-ESVREEFIQKGDEVKCKLD------------ 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1629 kkKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAA 1708
Cdd:pfam05483 570 --KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1709 serARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLeeeleeeqsnMELLNERFRKTTLQVDTLNSELAGERS 1788
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----------VKLQKEIDKRCQHKIAEMVALMEKHKH 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1789 AAQKSenarqqLERQNKEL---KAKLQElEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1863
Cdd:pfam05483 715 QYDKI------IEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1395-1940 |
6.97e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 57.93 E-value: 6.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1395 GTIEGLEENKKKLlkdmESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLdhqRQIVSNLEKKQKKFDQMLAEEKNiS 1474
Cdd:pfam12128 241 PEFTKLQQEFNTL----ESAELRLSHLHFGYKSDETLIASRQEERQETSAEL---NQLLRTLDDQWKEKRDELNGELS-A 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1475 ARYAEERDRAEAEAREKETKALSLARALEEALEAKeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQV-EE 1553
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQE-----QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1554 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQardEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAkkkmE 1633
Cdd:pfam12128 388 NNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT----P 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1634 MDLKDLEGQIEAANKARDEaikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEE-FAAS--- 1709
Cdd:pfam12128 461 ELLLQLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAgtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1710 -ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR-----------RLEARIAQLEEELEEE 1758
Cdd:pfam12128 537 lHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1759 QSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEE 1838
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1839 QLeQEAKERAAANKLVRRTEK--KLKEVfmqVEDERRHADQYKEQMEkanARMKQLKRQLEEAEEEATRANASRrklqre 1916
Cdd:pfam12128 697 KH-QAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIA---ARRSGAKAELKALETWYKRDLASL------ 763
|
570 580
....*....|....*....|....
gi 212450 1917 lDDATEANEGLSREVSTLKNRLRR 1940
Cdd:pfam12128 764 -GVDPDVIAKLKREIRTLERKIER 786
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1077-1859 |
7.84e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 57.52 E-value: 7.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1077 LQDQIAELQAQIEELKIQLAKKEEELQAALargdeeavqknNALKVIrelqaqiaeLQEDLESEKASRNKAEKQKRDLSE 1156
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTF---------WSPELKKERALRKEEAARISVLKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1157 ELEALKTELED-TLDTTAAQQELRTKRE------------QEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLE 1223
Cdd:pfam10174 61 QYRVTQEENQHlQLTIQALQDELRAQRDlnqllqqdfttsPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1224 QakrFKANLEKNKQGLESDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQELTA----KVTEGERLRVELAE 1290
Cdd:pfam10174 141 E---MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHLEVlldqKEKENIHLREELHR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1291 KaNKLQNELDNVSSLLEEAEKKGIKFakdaASLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNNLQEQQEEEE 1366
Cdd:pfam10174 218 R-NQLQPDPAKTKALQTVIEMKDTKI----SSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKID 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1367 EARKNLEK---QMLALQAQLAEAKKKVDDDLGTIEGLEEN-------KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQ 1436
Cdd:pfam10174 293 QLKQELSKkesELLALQTKLETLTNQNSDCKQHIEVLKESltakeqrAAILQTEVDALRLRLEEKESFLNKKTKQLQDLT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1437 QELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLaraleealeakeef 1512
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL-------------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1513 erqnkqlrADMEDLMSSKDDVGKNV-HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQ 1591
Cdd:pfam10174 439 --------TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----A 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1592 ARDEQNEEKKRMLVKQvreLEAELEDERKQRALAVAAKKKMEmdlkdlegQIEAANKARDEAIKQLRKLQAQMKDYQREL 1671
Cdd:pfam10174 506 SSLASSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1672 EEARASRDEIFAQSKESE-------KKLKGLEAEILQLQEEFAASERARRHAEQERDEladeiansasgKSALLDEkrrl 1744
Cdd:pfam10174 575 GKAQAEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE---- 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1745 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAgerSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKA 1824
Cdd:pfam10174 640 EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS---STQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA 716
|
810 820 830
....*....|....*....|....*....|....*
gi 212450 1825 TISTLEAKIAQLEeqLEQEAKERAAANKLVRRTEK 1859
Cdd:pfam10174 717 AISEKDANIALLE--LSSSKKKKTQEEVMALKREK 749
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1027-1226 |
8.11e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.76 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1027 EEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1106
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE----ALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1107 ------------------ARGDEEAVQKNNAL--------KVIRELQAQIAEL---QEDLESEKASRNKAEKQKRDLSEE 1157
Cdd:COG3883 93 ralyrsggsvsyldvllgSESFSDFLDRLSALskiadadaDLLEELKADKAELeakKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1158 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAK 1226
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1581-1748 |
9.06e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.32 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1581 AMKAQFER--DLQARD---EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1655
Cdd:COG1579 1 AMPEDLRAllDLQELDselDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1656 QLRKLQA--QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAsg 1733
Cdd:COG1579 81 QLGNVRNnkEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL-- 158
|
170
....*....|....*
gi 212450 1734 kSALLDEKRRLEARI 1748
Cdd:COG1579 159 -EELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1703-1941 |
9.73e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.31 E-value: 9.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1703 QEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSE 1782
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1783 LAGERSAAQKSENARQQLERQNKeLKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLK 1862
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPP-LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1863 EVFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1941
Cdd:COG4942 178 ALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1470-1922 |
9.86e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1470 EKNISARYAEERDRAEAEAREKETKALslARALEEALEAKEEFERQNKQLRADMEDLmsskdDVGKNVHELEKSKRTLEQ 1549
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAEL--QEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1550 QVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1626
Cdd:COG4717 140 ELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1627 AAKKKMEMDLKDLEGQIEAANKArdEAIKQLRKLQAQM-------------KDYQRELEEARASRDEIFAQSKESEKKLK 1693
Cdd:COG4717 220 EELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1694 gleAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTT 1773
Cdd:COG4717 298 ---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1774 LQVDTLNSELAGERSAAQKSEnARQQLERQNKELKAKLQELEGSVKSKFKA-TISTLEAKIAQLEEQLEQEAKERAAANK 1852
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1853 LVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1922
Cdd:COG4717 454 ELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLERASE 523
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1558-1940 |
1.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.08 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1558 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELEDERKQRALAVAAKKKMEM--D 1635
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEELREELEKLEKllQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1636 LKDLEGQIEAANKARDEAIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKGLEAEILQLQE 1704
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1705 EFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARI------------AQLEEELEEEQSNMELLNERFRKT 1772
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1773 TLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANK 1852
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLS-PEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1853 LVRRTEKK--LKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLS 1928
Cdd:COG4717 366 EELEQEIAalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELE 445
|
410
....*....|..
gi 212450 1929 REVSTLKNRLRR 1940
Cdd:COG4717 446 EELEELREELAE 457
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
862-1852 |
1.13e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 57.37 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 862 EELQAK-DEELMKVKEKQTK-VEAELEEMERKHQQLLEekNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 939
Cdd:TIGR01612 699 DDLKSKiDKEYDKIQNMETAtVELHLSNIENKKNELLD--IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 940 RveeeeernqilQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIA 1019
Cdd:TIGR01612 777 E-----------KDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1020 ECTSQLAEEEEKAKNLAklkNKQEMMITDLEERLKKEEKTRQeLEKAKRKLDgettDLQDQIAELQAQIEE--LKIQLAK 1097
Cdd:TIGR01612 846 NKVDKFINFENNCKEKI---DSEHEQFAELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1098 KEEELqAALARGDEEAVQK--NNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELedTLDTTAA- 1174
Cdd:TIGR01612 918 KVDEY-IKICENTKESIEKfhNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAk 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1175 -----------QQELRTKRE----QEVAELKKA---IEEETKNHEAQIQEIRQRHATALEELSEQLEqaKRFKANLEK-N 1235
Cdd:TIGR01612 995 nnelikyfndlKANLGKNKEnmlyHQFDEKEKAtndIEQKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlN 1072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1236 KQGLESDNKELACEVKVLQQVK------------AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVS 1303
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI 1152
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1304 SLLEEAEKKGIkFAKDAASLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLQEQQEEEEEARKNLEKQML 1377
Cdd:TIGR01612 1153 NDLEDVADKAI-SNDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGKLFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1378 AlqaQLAEAKKKVDDDLGTIEGLEENkkklLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDD----LMVDLDHQRQIv 1453
Cdd:TIGR01612 1229 E---KIDEEKKKSEHMIKAMEAYIED----LDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI- 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1454 SNLEKKQKKFDQMLAEEKNIS------ARYAEERDRAEAEAREKETKALSLARALEEALEakeeferqnKQLRADMEDLM 1527
Cdd:TIGR01612 1301 SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI---------KKIIDEVKEYT 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1528 SSKDDVGKNVH-ELEKSKrTLEQQVEEmRTQLEELEDELQATEDAK---------LRLEVNMQAMKAQFERDLQARDEQN 1597
Cdd:TIGR01612 1372 KEIEENNKNIKdELDKSE-KLIKKIKD-DINLEECKSKIESTLDDKdidecikkiKELKNHILSEESNIDTYFKNADENN 1449
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 EEKKrMLVKQVreleaELEDERKQRALAVA---AKKKMEMDLKDLEGQIEAANKARDEA---IKQLRKLQAQMKDYQRE- 1670
Cdd:TIGR01612 1450 ENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDv 1523
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1671 --------------------------LEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1724
Cdd:TIGR01612 1524 tellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE 1603
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1725 D------EIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnerfrkTTLQVDTLNSELAGERSAAQKSENARQ 1798
Cdd:TIGR01612 1604 NfenkflKISDIKKKINDCLKETESIEKKI-----------------------SSFSIDSQDTELKENGDNLNSLQEFLE 1660
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 212450 1799 QLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANK 1852
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKELD-ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1082-1382 |
1.13e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1082 AELQAQIEELKiqlakKEEELQAalargDEEAVQKN--NALKVIrelqAQIAELQEDLESEKASRNKAEKQKRDLSEELE 1159
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQDleQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1160 ALKTELEDTLDTTAAQQELRTkREQEVAELKKAIEEETKN-HEAQIQEIRQRHA-----TALEELSEQLEQAKRFKANLE 1233
Cdd:PRK11281 105 ALKDDNDEETRETLSTLSLRQ-LESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQperaqAALYANSQRLQQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1234 KNKQGLESDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELtakvteGERLRVELAEKANKLQNELdnvsSLLEEA- 1309
Cdd:PRK11281 184 VGGKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAi 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1310 -EKKGIKFAKDAASLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNNLQeqqeeeeeaRKNLE-KQML--ALQ 1380
Cdd:PRK11281 251 nSKRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQ 320
|
..
gi 212450 1381 AQ 1382
Cdd:PRK11281 321 SE 322
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1600-1891 |
1.16e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1600 KKRMLVKQVRE---LEAELEDERKQRALAVA---AKKKMEMDLKDlegQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1673
Cdd:COG3206 124 RKNLTVEPVKGsnvIEISYTSPDPELAAAVAnalAEAYLEQNLEL---RREEARKALEFLEEQLPELRKELEEAEAALEE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1674 ARASRDEIF--AQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN--SASGKSALLDEKRRLEARIA 1749
Cdd:COG3206 201 FRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1750 QleeeleeeqsnmelLNERFRKTTLQVdtlnselagersaaqksenarQQLERQNKELKAKLQELEGSVKSKFKATISTL 1829
Cdd:COG3206 281 E--------------LSARYTPNHPDV---------------------IALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212450 1830 EAKIAQLEEQLEQEAKERAAANKLvrrtEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQ 1891
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARLAEAL 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1287-1896 |
1.42e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 56.57 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1287 ELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEE 1366
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1367 EARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL 1446
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1447 DHQRQIVSNLEKKQKKFDQMLAEeknisaryaeerdraeaeareketkalslaraleealeakeeferqnkqlradmedl 1526
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQ--------------------------------------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1527 msskddvgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVK 1606
Cdd:TIGR04523 220 ----------ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKELEK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1607 QVRELEAELEDERKQRALAVAakKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1687 ESEKKLKGLEAEilqlqeefaaserarrhaeqerdeladeiansasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1766
Cdd:TIGR04523 367 EKQNEIEKLKKE-----------------------------------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1767 ERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKE 1846
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-NTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 212450 1847 RAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1205-1442 |
1.51e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1205 QEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtegERL 1284
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI---AEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1285 RVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEetrqklnLSSRIRQLEEEKNNLQEQQEE 1364
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPA-------RREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1365 EEEARKNLEKQMLALQAQLAEakkkvdddlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1442
Cdd:COG4942 169 LEAERAELEALLAELEEERAA--------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1287-1934 |
1.63e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1287 ELAEKANKLQNELDNVSSLleEAEKKGIKFA-KDAASLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNNLQEQQEEE 1365
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1366 EEARKNLEKQMLALQAQlaeAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQelddlMVD 1445
Cdd:pfam12128 314 DAAVAKDRSELEALEDQ---HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRS-----KIK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1446 LDHQRQIVSNLEKKQKKFD----QMLAEEKNISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQ 1518
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1519 LRADMEDLMSSKDDVGKNVHELEKSKRTL-----------------EQQVEEMRTQLEELEDELQA---TEDAKLRLEVN 1578
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasealrqaSRRLEERQSALDELELQLFPqagTLLHFLRKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1579 M--QAMKAQFERDLQARDEQNEEKKRMLVKQVRELEA-ELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1655
Cdd:pfam12128 546 DweQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1656 QLRKLQAQMKDYQRELEEARASrdeiFAQSKESEKKLKG-LEAEILQLQEefaASERARRHAEQERDELADEIANSASGK 1734
Cdd:pfam12128 626 QLVQANGELEKASREETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKH 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1735 SALLDEKRR--LEARIAQLeeeleeeqsnmELLNERFRKTTLQVDTLNSELAGERSAAQKSENArqqLERQNK-ELKAKL 1811
Cdd:pfam12128 699 QAWLEEQKEqkREARTEKQ-----------AYWQVVEGALDAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASLG 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1812 QELEgsvkskfkaTISTLEAKIAQLEEQLEQEAKERAAanklVRRTEKKLKEVFMQvederrHADQYKEQMEKANARMK- 1890
Cdd:pfam12128 765 VDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLATQLSNIERAISe 825
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 212450 1891 ---QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1934
Cdd:pfam12128 826 lqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1368-1750 |
1.77e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1368 ARKNLEKQMLALQAQLAEAKKKvdddlgtiegleenkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL----- 1442
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQ---------------------LAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhln 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1443 --MVDLDHQRQI---VSNLEKKQKKfdqmLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNK 1517
Cdd:PRK04863 339 lvQTALRQQEKIeryQADLEELEER----LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1518 QLRADMEDLMSSKDDVGKNVHELEKskrtLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQARDEQN 1597
Cdd:PRK04863 415 QYQQAVQALERAKQLCGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 EEKKRMLVKQV-RELeaeLEDERKQRALAVAAkKKMEMDLKDLEGQIE---AANKARDEAIKQLRK---LQAQMKDYQRE 1670
Cdd:PRK04863 487 GEVSRSEAWDVaREL---LRRLREQRHLAEQL-QQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKnldDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1671 LEEARASRDEIFAQSKES----EKKLKGLEAEILQL----QEEFAASERARRHAEQERDELADE------IANSASGKSA 1736
Cdd:PRK04863 563 LEARLESLSESVSEARERrmalRQQLEQLQARIQRLaaraPAWLAAQDALARLREQSGEEFEDSqdvteyMQQLLERERE 642
|
410
....*....|....
gi 212450 1737 LLDEKRRLEARIAQ 1750
Cdd:PRK04863 643 LTVERDELAARKQA 656
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1607-1938 |
2.12e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.20 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1607 QVRELEAELEDerKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYqrelEEARASRDEIFAQSK 1686
Cdd:PRK02224 188 SLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEH----EERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1687 ESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1766
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1767 ERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkFKATISTLEAKIAQLEEQLEQEAKE 1846
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-LRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1847 RAAANKLVRRTEKKLKEVFMQVEDERR------------------HAD---QYKEQMEKANARMKQLKRQLEEAEEEATR 1905
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegspHVEtieEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350
....*....|....*....|....*....|...
gi 212450 1906 ANASrRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:PRK02224 501 AEDL-VEAEDRIERLEERREDLEELIAERRETI 532
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1215-1729 |
2.91e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 55.68 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1215 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1294
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1295 LQNELDNVSSlLEEAEKKGIKFAKDAASLEsqlqdtqellQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEk 1374
Cdd:PRK01156 265 LSMELEKNNY-YKELEERHMKIINDPVYKN----------RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1375 QMLALQAQLAEAKKKVDD---DLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKL-----------EKTKNRLQQELD 1440
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiseilkiqEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1441 DLMVDLDHQRQIVSNLEKKQKKFDQMLAE-------------------------EKNISARYAEERDRAEAEAREKETKA 1495
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDElsrnmemlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1496 LSLaraleeALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQAT--EDAKL 1573
Cdd:PRK01156 493 KDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLklEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1574 RLEVNMQAMKAQFERDLQARDEQNEEKKRML---VKQVRELEAELEDERKQRALAVaakKKMEMDLKDLEGQIEAAnKAR 1650
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKSYIDKSI---REIENEANNLNNKYNEI-QEN 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1651 DEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN 1729
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
989-1351 |
3.14e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 55.25 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 989 KIKKMEEEILLLEDQNSK--FLKEKKLMEdriaECTSQLAEEEEKAKNlaklknkqemMITDLEERLKKEEKTRQELEKA 1066
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrFKKAKKALD----EIEELLDDIEEDIKQ----------ILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1067 KRKLDGETTDLQDQ-------IAELQAQIEELKIQLAKKEEELQAalarGDEEAvqknnALKVIRELQAQIAELQEDLES 1139
Cdd:pfam06160 127 KDKYRELRKTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMED 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1140 EKASRNKAEKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKAIEE-ETKNHEAQIQEIRQRhataL 1215
Cdd:pfam06160 198 IPPLYEELKTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----I 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1216 EELSEQLEQAKRFKANLEKNKQGLESD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELTAKVtegERLR 1285
Cdd:pfam06160 273 DQLYDLLEKEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIV 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1286 VELAEKA---NKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1351
Cdd:pfam06160 350 ERLEEKEvaySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1030-1165 |
3.77e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.22 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1030 EKAK-NLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLakkEEELQAALAR 1108
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1109 GDEEAVQknnalkVIRELQAQIAELQEDLESEKASrnkaEKQKRdLSEELEALKTEL 1165
Cdd:PRK00409 582 AKKEADE------IIKELRQLQKGGYASVKAHELI----EARKR-LNKANEKKEKKK 627
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1127-1346 |
4.20e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1127 QAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQE 1206
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1207 IRQ--RHATALEEL--SEQLEQakrFKANLEKNKQGLESDNKELacevKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1282
Cdd:COG3883 95 LYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1283 RLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSS 1346
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1369-1631 |
4.91e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1369 RKNLEKQMLALQAQLAEAKKKvdddlgtiegleenKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDH 1448
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKE--------------EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1449 QRQivsNLEKKQKKFDQMLAEeknisaryaeerdrAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1528
Cdd:COG4942 95 LRA---ELEAQKEELAELLRA--------------LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1529 SKDdvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQV 1608
Cdd:COG4942 158 DLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEALI 229
|
250 260
....*....|....*....|...
gi 212450 1609 RELEAELEDERKQRALAVAAKKK 1631
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALK 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1070-1247 |
5.22e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1070 LDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAV--QKNNALKVIRELQAQIAELQEDLESEKASRNKA 1147
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLseEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1148 EKQKRDL---------SEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEetknheaQIQEIRQRHATALEEL 1218
Cdd:COG3206 246 RAQLGSGpdalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA-------LRAQLQQEAQRILASL 318
|
170 180
....*....|....*....|....*....
gi 212450 1219 SEQLEQAKRFKANLEKNKQGLESDNKELA 1247
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELP 347
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1001-1243 |
5.94e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.55 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1001 EDQNSKFLKEKKLMEdRIAECTSQLAEEEEKAKNLAKLKNKQEmmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIqLAKKEEELQaaLARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNK-------AEKQKRD 1153
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1154 LSEELEALKTELEDTLDTTAAQQELRtKREQEVAELKKAIEEEtknhEAQIQEIRQRHATALEELSEQLEQAkRFKANLE 1233
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIR-EIKEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 212450 1234 KNkqGLESDN 1243
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1302-1875 |
6.10e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1302 VSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1381
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1382 QLAEAKKKVDDdlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1461
Cdd:pfam05557 91 KLNEKESQLAD-------AREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1462 KFDQMLAEEKNISARYAEERDRAEaEAREKETKALSLARaleealeakeeFERQNKQLRADMEDLMSSKDDVGKNVHELE 1541
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSE-IVKNSKSELARIPE-----------LEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1542 KSKRTLEQQvEEMRTQLEELEDELQATEdAKLRLEVNMQAMKAQFER---DLQARDEQNEEKKRMLVKQVRELEAELEDE 1618
Cdd:pfam05557 232 DLKRKLERE-EKYREEAATLELEKEKLE-QELQSWVKLAQDTGLNLRspeDLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1619 RKQRalavaakKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQSKESEKKLKGL 1695
Cdd:pfam05557 310 EKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1696 E--AEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR--- 1770
Cdd:pfam05557 383 EeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRlre 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1771 -KTTLQVDTLNSELAGERSAA-----QKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEA 1844
Cdd:pfam05557 463 qKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNF 542
|
570 580 590
....*....|....*....|....*....|....
gi 212450 1845 KERAAANKLVRRTEKK---LKEVFMQVEDERRHA 1875
Cdd:pfam05557 543 KEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1530-1750 |
6.86e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1530 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQfERDLQARDEQNEEKKRMLVKQVR 1609
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1610 ELEAELEDERKQRALAVAAKKKMEMD--LKDLEGQIEAANKARDEAIK-------QLRKLQAQMKDYQREL-EEARASRD 1679
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1680 EIFAQSKESEKKLKGLEAEILQLQEEFAA-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1750
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1548-1760 |
6.96e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1548 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVA 1627
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1628 AKKKMEMDLKDLEGQIEAANKArdEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFA 1707
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 212450 1708 ASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1760
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1539-1699 |
8.22e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1539 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlqardeqneEKKRMLVKQVRELEA---EL 1615
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---------EEQLGNVRNNKEYEAlqkEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1616 EDERKQRAlavaakkkmemdlkDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGL 1695
Cdd:COG1579 99 ESLKRRIS--------------DLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
....
gi 212450 1696 EAEI 1699
Cdd:COG1579 165 REEL 168
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1475-1847 |
9.20e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.75 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1475 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1554
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1555 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMlvkQVRELEAELEDERKQRALAVAAKKKMEM 1634
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNSLAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1635 DLKDLEGQIEAANkardeaiKQLRKLQAQMKDYQRE--LEEARASRDEIFAqskeSEKKLKGLEAEIlqlqeEFAASERA 1712
Cdd:pfam07888 205 DTQVLQLQDTITT-------LTQKLTTAHRKEAENEalLEELRSLQERLNA----SERKVEGLGEEL-----SSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1713 RRHAEQERDEL-ADEIANSASGKSALLDEKRrleariAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQ 1791
Cdd:pfam07888 269 RTQAELHQARLqAAQLTLQLADASLALREGR------ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1792 KSE---------NARQQLE--RQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEQLEQEAKER 1847
Cdd:pfam07888 343 KLEvelgrekdcNRVQLSEsrRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
861-1145 |
9.54e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 9.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfaEAEEMRARLAAKKQELEEilhdlesr 940
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 941 veeeeeRNQILQNEKKKMQghiqdleeqldeeegaRQKLQLEKVtaeakikkmeeEILLLEDQNSKFLKEKKLMeDRIAE 1020
Cdd:COG3883 84 ------RREELGERARALY----------------RSGGSVSYL-----------DVLLGSESFSDFLDRLSAL-SKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1021 CTSQLAEEEEKAKnlAKLKNKQEmmitDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEE 1100
Cdd:COG3883 130 ADADLLEELKADK--AELEAKKA----ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 212450 1101 ELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1145
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1538-1934 |
9.80e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1538 HELEKSKRTL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQ--FERDLQARDEQNE--EKKRM 1603
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQekIERYQEDLEELTErlEEQEE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1604 LVKQVRELEAELEdERKQRAlavaakkkmEMDLKDLEGQIEAANKARDEaiKQLRKLQAQMKdyQRELEEARA------- 1676
Cdd:COG3096 369 VVEEAAEQLAEAE-ARLEAA---------EEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdl 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1677 SRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQl 1751
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1752 eeeleeeqsnmellnerfrkttlqVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgsvkskfkatisTLEA 1831
Cdd:COG3096 514 ------------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1832 KIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKeqmeKANARMKQLKRQLEEAEEEATRANASR- 1910
Cdd:COG3096 558 LLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL----AAQDALERLREQSGEALADSQEVTAAMq 633
|
410 420 430
....*....|....*....|....*....|
gi 212450 1911 ------RKLQRELDDATEANEGLSREVSTL 1934
Cdd:COG3096 634 qllereREATVERDELAARKQALESQIERL 663
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1375-1940 |
1.04e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.28 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1375 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLlKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMV---------- 1444
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNRLKEI-EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEkvfqgtdeql 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1445 -DLDHQRQiVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKEtkaLSLARALEEALEAKEEFERQNKQLRADM 1523
Cdd:TIGR00606 304 nDLYHNHQ-RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1524 EDLMSSKDDVG--KNVHELEKskRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlQARDEQNEEKK 1601
Cdd:TIGR00606 380 DGFERGPFSERqiKNFHTLVI--ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1602 RMLVKQVRELEAELEDERKQRAlavaAKKKMEMDLKDLEgqieaankaRDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1681
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQ----ELRKAERELSKAE---------KNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1682 FAQSKESEKKLKGLEaeiLQLQEEFAASERARRHAEQERDELADEIANSASGKS------ALLDEKRRLEARIAQLEEEL 1755
Cdd:TIGR00606 524 MEQLNHHTTTRTQME---MLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKEL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1756 EEEQSNMELLNERFRKTTLQVDTLNSELAgersAAQKSENARQQLERQNKELKAKlqelegsvkSKFKATISTLEAKIAQ 1835
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKLF----DVCGSQDEESDLERLKEEIEKS---------SKQRAMLAGATAVYSQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1836 LEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKqlKRQLEEAEEEATRANASRRKlQR 1915
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLAPGRQSIIDLK-EK 744
|
570 580
....*....|....*....|....*
gi 212450 1916 ELDDATEANEGLSREVSTLKNRLRR 1940
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1332-1718 |
1.19e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1332 ELLQEETRQKLNLSSRIRQLEEEK---NNLQEQQEEEEEARKNLEKQMLALQAQLAEAKkkvdddlgTIEGLEENKKKLL 1408
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQyrlVEMARELAELNEAESDLEQDYQAASDHLNLVQ--------TALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1409 KDMESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMVDL-DHQ-------------RQIVSNLEKKQKKFDQML 1467
Cdd:PRK04863 355 ADLEELEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLaDYQqaldvqqtraiqyQQAVQALERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1468 AEEKNISARYAEERDRAEA---EAREKETKaLSLARALEEALEAKEEFERqnkQLRADMEdlMSSKDDVGKNVHELEKSK 1544
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEateELLSLEQK-LSVAQAAHSQFEQAYQLVR---KIAGEVS--RSEAWDVARELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1545 RTLEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQARDEQNEEKKRMLvkqvRELEAELEDERKQRAL 1624
Cdd:PRK04863 509 RHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQ----EELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1625 AVAAKKKMEMDLKDLEGQIEAANK------ARDEAIKQLRK-----------LQAQMKDYQRELEEARASRDEIFAQSKE 1687
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREqsgeefedsqdVTEYMQQLLERERELTVERDELAARKQA 656
|
410 420 430
....*....|....*....|....*....|..
gi 212450 1688 sekklkgLEAEILQL-QEEFAASERARRHAEQ 1718
Cdd:PRK04863 657 -------LDEEIERLsQPGGSEDPRLNALAER 681
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
814-1247 |
1.20e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 53.82 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 814 KAFAKKQQQLSALKILQRNCAAY-----LKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEM 888
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 889 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQ 968
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 969 LDEEEGARQKLQ-LEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQE---M 1044
Cdd:TIGR00618 586 IPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehaL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1045 MITDLEER-LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI 1123
Cdd:TIGR00618 666 SIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1124 RELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaQQELRTKREQEVAELKKAIEEETKNHEA- 1202
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF-------FNRLREEDTHLLKTLEAEIGQEIPSDEDi 818
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 212450 1203 ------QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1247
Cdd:TIGR00618 819 lnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
859-1198 |
1.21e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 53.75 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 859 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHdle 938
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILT--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 939 srveeeeernqilqnEKKKMQGHIQDLEEQLDEEeGARQKLqlekvTAEAKIKkmeeeILLLEDQNSKFLKEKKLMEDRI 1018
Cdd:PLN02939 164 ---------------EKEALQGKINILEMRLSET-DARIKL-----AAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1019 AECTSQLAEEEE--KAKNLAkLKNKQEMM------ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAqiee 1090
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1091 LKIQ-LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRdLSEELEALKTELEDTL 1169
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340
....*....|....*....|....*....
gi 212450 1170 DTTAAQQELRTKREQEVAELKKAIEEETK 1198
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1539-1817 |
1.26e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 53.59 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1539 ELEKSKRTLEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARdeQNEEKKR-----------MLV 1605
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRelerirqeeiaMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1606 KQVRELE--------------AELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL 1671
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1672 EEARASRDEIFAQsKESEKKLKGLEAEILQLQEEFAASERaRRHAEQERDEladeiansasGKSALLDEKRR---LEARI 1748
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEE----------RKQAMIEEERKrklLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1749 AQLEEELEEEQSNMELLNERFRKTTL----QVDTLNSELAGERSAAQKSENARQQLeRQNKELKAKLQELEGS 1817
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1026-1290 |
1.28e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1026 AEEEEKAKNLAKLKNKQEMMITDLEErlkKEEKTRQELEKAKRKLDG-----------ETTDLQDQIAELQAQIEELkiq 1094
Cdd:PRK04863 833 ADPEAELRQLNRRRVELERALADHES---QEQQQRSQLEQAKEGLSAlnrllprlnllADETLADRVEEIREQLDEA--- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1095 lakkeEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELE-----ALKTELEDTL 1169
Cdd:PRK04863 907 -----EEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDAAEMLA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1170 DTTAAQQELRTKREQEVAELKKAiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEK----NKQGLE----S 1241
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRA-REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpADSGAEerarA 1060
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 212450 1242 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAE 1290
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1584-1922 |
1.28e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1584 AQFERDLQ-ARDEQNEEKKRmLVKQVRELEaelEDERKQRAL----------------AVAAKKKMEM---DLKDLEGQI 1643
Cdd:COG3096 288 LELRRELFgARRQLAEEQYR-LVEMARELE---ELSARESDLeqdyqaasdhlnlvqtALRQQEKIERyqeDLEELTERL 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1644 EAANKARDEAIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR---HAEQER 1720
Cdd:COG3096 364 EEQEEVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcgLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1721 DELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLnerfrkttlqvdtlnSELAGERSAAQKSENARQQL 1800
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV---------------CKIAGEVERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1801 eRQNKELKAKLQELEgsvkskfkatisTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKevfmqvederrHADQYKE 1880
Cdd:COG3096 502 -RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELEE 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 212450 1881 QMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1922
Cdd:COG3096 558 LLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1375-1922 |
1.71e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1375 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEkamaYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1454
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISN----IDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1455 NLEKK-----------QKKFDQMLAEEKNISARyAEERDRAEAEAREKETKalslaraleealeaKEEFERQNKQLRADM 1523
Cdd:PRK01156 215 ITLKEierlsieynnaMDDYNNLKSALNELSSL-EDMKNRYESEIKTAESD--------------LSMELEKNNYYKELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1524 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQARDEQN------ 1597
Cdd:PRK01156 280 ERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilel 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 ---EEKKRMLVKQVRELEAELEDERKQR----ALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRE 1670
Cdd:PRK01156 359 egyEMDYNSYLKSIESLKKKIEEYSKNIermsAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1671 LEEARASRDEIFAQS------------------KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAS 1732
Cdd:PRK01156 439 LDELSRNMEMLNGQSvcpvcgttlgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSI 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1733 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRktTLQVDTLNSELAGERSA-AQKSENARQQLERQNKELKAKL 1811
Cdd:PRK01156 519 NEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK--SLKLEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1812 QELEG---SVKSKFKATISTLEAKIAQLEEQLeqeakeraaanKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANAR 1888
Cdd:PRK01156 597 NDLESrlqEIEIGFPDDKSYIDKSIREIENEA-----------NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
570 580 590
....*....|....*....|....*....|....
gi 212450 1889 MKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1922
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1081-1358 |
1.74e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 53.32 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKnnaLKviRELQAQIAE------LQEDLESEKASRNKAEKQK--- 1151
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LK--KEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1152 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKAIEEETKNHEAQiQEIRQRHATALEElSEQLEQAKRF 1228
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDR-PEIKEKMEAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1229 KANLEKNKQGLESD-NKELACEV-KVLQQVKAESEHKRKKLDAQVQELTAK--VTEGERLRVELAEKANKLQNELD---- 1300
Cdd:PLN03229 584 KAEVASSGASSGDElDDDLKEKVeKMKKEIELELAGVLKSMGLEVIGVTKKnkDTAEQTPPPNLQEKIESLNEEINkkie 663
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 1301 ---NVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1358
Cdd:PLN03229 664 rviRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1060-1923 |
1.78e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1060 RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQlakkEEELQAA---LARGDEEAVQKNNalkvIRELQAQIAELQED 1136
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAAsdhLNLVQTALRQQEK----IERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1137 LESEKASRNKAEKQKRDLSEELEA-------LKTELEDTLDTTAAQQELRTKREQEVAELKKA------IEEETKNHEAQ 1203
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAaeeevdeLKSQLADYQQALDVQQTRAIQYQQAVQALERAkqlcglPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1204 IQEIR---QRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELTAKVT 1279
Cdd:PRK04863 444 LEEFQakeQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1280 EGERlRVELAEKANKLQNELDNVSSLLEEAEKkgikfakDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlq 1359
Cdd:PRK04863 524 ELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQ----- 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1360 eqQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQEL 1439
Cdd:PRK04863 591 --LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY-------MQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1440 DDLmvdldHQRQiVSNLEKKQKKFDQM-------------LAEEKNISARYAEER------DraeaeareketkaLSLAR 1500
Cdd:PRK04863 662 ERL-----SQPG-GSEDPRLNALAERFggvllseiyddvsLEDAPYFSALYGPARhaivvpD-------------LSDAA 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1501 aleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK------SKRTL----------------EQQVE 1552
Cdd:PRK04863 723 -------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKavvvkiADRQWrysrfpevplfgraarEKRIE 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1553 EMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQ-----ARDEQNEEKKRMLVKQVRELEAELED----ERKQR 1622
Cdd:PRK04863 790 QLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADhesqEQQQR 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1623 ALAVAAKKKMEMdLKDLEGQIEAAnkARDEAIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKGLEAEI 1699
Cdd:PRK04863 865 SQLEQAKEGLSA-LNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSDPEQF 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1700 LQLQEEFAASERARRHAEQERDELADEIANSASGKSAllDEKRRLEARIAqleeeleeeqsnmelLNERFRkttlqvdtl 1779
Cdd:PRK04863 938 EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD---------------LNEKLR--------- 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1780 nselagersaaQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATISTLEAKIAQLEEQLE-------QEAKERAAA 1850
Cdd:PRK04863 992 -----------QRLEQAEQERTRAREQLRQAQAQLAqyNQVLASLKSSYDAKRQMLQELKQELQdlgvpadSGAEERARA 1060
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1851 NKlvrrtekklKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1923
Cdd:PRK04863 1061 RR---------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1092-1350 |
2.07e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.13 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1092 KIQLAKKEEELQAALARGDEEAVQknnalkvirELQAQIAELQEdlesEKASRNKAEKQKR------DLSEELEALKTEL 1165
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEIVE---------ALQSALNWLEE----RKGSLERAKQYQQvidnfpKLSAELRQQLNNE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1166 ED---TLDTTAAQQELrtkrEQEVAELKKAIEEETknHEAQIQEIRQRH-ATALEELSEQLEQAKRFKANLEKNKQGLES 1241
Cdd:PRK10929 92 RDeprSVPPNMSTDAL----EQEILQVSSQLLEKS--RQAQQEQDRAREiSDSLSQLPQQQTEARRQLNEIERRLQTLGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1242 DNKELACEVKVLQQvkAESEHKRKKLD----AQV-----QELTakvtegeRLRVELAEK-ANKLQNELDNVSSLL----- 1306
Cdd:PRK10929 166 PNTPLAQAQLTALQ--AESAALKALVDelelAQLsannrQELA-------RLRSELAKKrSQQLDAYLQALRNQLnsqrq 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 212450 1307 ---EEAEKKGIKFAKDAASLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1350
Cdd:PRK10929 237 reaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1081-1337 |
2.63e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 52.91 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQLAKKEeelQAALARGDEEAVQKNNAlKVIRELQAQIAEL---QEDLES--EKASRNKAEKQKRDLS 1155
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDD---AAQNALADKERAEADRQ-RLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1156 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKAIEEE---TKNH-EAQIQEIRQRHATALEELSEQLE 1223
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1224 QAKRFKANLEKNKQGLESDNKelacevkvlqqvKAESEHKRKKLDAQVQELTAKVTEgerlrvelaEKANklqneldnvs 1303
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAE---------SDAN---------- 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 212450 1304 SLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1337
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1287-1918 |
3.06e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1287 ELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLQEQQEE 1364
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1365 EEEA-----RKNLEKQMLALQAQLAEAKK-------KVDDDLGTIEGLEENKKKLLKDmeslsqrlEEKAMAYDKLEKTK 1432
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEIND--------KEKQVSLLLIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1433 NrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEF 1512
Cdd:pfam05483 252 K--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1513 ERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAMKAQFERD 1589
Cdd:pfam05483 330 TEEKE---AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKFKNNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1590 LQARDEQNEEKKRMLV--KQVRELEAELEDERKQRALAVAAKKKmemDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDY 1667
Cdd:pfam05483 407 LEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1668 QRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAaserarrHAEQERDELADEIANSASGKSALLDEKRRLEAR 1747
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDII-------NCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1748 IAQLEEELE----EEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKlqeleGSVKSKfk 1823
Cdd:pfam05483 557 FIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-----GSAENK-- 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1824 aTISTLEAKIAQLEEQLEqeakerAAANKLVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANARMKQLKrqleeaeeea 1903
Cdd:pfam05483 630 -QLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---------- 688
|
650
....*....|....*
gi 212450 1904 tranasrrKLQRELD 1918
Cdd:pfam05483 689 --------KLQKEID 695
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1701-1922 |
3.85e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1701 QLQEEFAASERARRHAEQERDELADEIansasgksalldekRRLEARIAQLEEeleeeQSNMELLNERFRKTTLQVDTLN 1780
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKEL--------------EEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1781 SELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvkskfkATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKK 1860
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS------PVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ 299
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1861 LKEVFMQVEDE-RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRK---LQRELDDATE 1922
Cdd:COG3206 300 IAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAElrrLEREVEVARE 365
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
985-1223 |
3.93e-06 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 52.07 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 985 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS----QLAEEEEKAKNLAKLKNKqemmITDLEErlKKEEKTR 1060
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1061 QELEK--------AKRKLDGETTDLQDQIAELQAQIEELKIQLA--KKEEELQAALARGDEEAVQKNNALKVIRELQAQI 1130
Cdd:pfam09731 261 QELVSifpdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVR 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1131 A--ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEvAELKKAIEEETKNHEAQIQEIr 1208
Cdd:pfam09731 341 AadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNEL- 418
|
250
....*....|....*
gi 212450 1209 qrhATALEELSEQLE 1223
Cdd:pfam09731 419 ---LANLKGLEKATS 430
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
893-1747 |
4.24e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 893 QQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQIlqnekKKMQGHIQDLEEQLDEE 972
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-----ERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 973 EGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKF-----LKEKKLME--------DRIAECTSQLAEEEEKAKN-LAKL 1038
Cdd:PRK04863 368 NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyqqavqalERAKQLCGLPDLTADNAEDwLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1039 KNKQEMMIT---DLEERLKKEEKTRQELEKAK---RKLDGETT--DLQDQIAELQAQIEELKIQlAKKEEELQAALARGD 1110
Cdd:PRK04863 448 QAKEQEATEellSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVSrsEAWDVARELLRRLREQRHL-AEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1111 EEAVQKNNALKVIRELQaQIAELQEDLESEkasrnkaekqkrdLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK 1190
Cdd:PRK04863 527 QRLRQQQRAERLLAEFC-KRLGKNLDDEDE-------------LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1191 KAIEEetknHEAQIQEIRQRHAtALEELSEQleqakrFKANLEkNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQ 1270
Cdd:PRK04863 593 ARIQR----LAARAPAWLAAQD-ALARLREQ------SGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1271 VQELTAKVT-EGERLRVeLAEKANK-----------------------------LQNELDNVSSLLEEAEK--------K 1312
Cdd:PRK04863 661 IERLSQPGGsEDPRLNA-LAERFGGvllseiyddvsledapyfsalygparhaiVVPDLSDAAEQLAGLEDcpedlyliE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1313 GIKFAKDAASLESQLQDTQELLQEETRQkLNLS--------------SRIRQLEEEKNNLQEQQEEEEEARKNLE----- 1373
Cdd:PRK04863 740 GDPDSFDDSVFSVEELEKAVVVKIADRQ-WRYSrfpevplfgraareKRIEQLRAEREELAERYATLSFDVQKLQrlhqa 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1374 -KQMLALQAQLAEAkkkVDDDlgtiegleenkkkllKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqRQI 1452
Cdd:PRK04863 819 fSRFIGSHLAVAFE---ADPE---------------AELRQLNRRRVELERALADHESQEQQQRSQLEQA-------KEG 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1453 VSNLEKKQKKFDqMLAEEKNIsaryaeerDRAEaEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskDD 1532
Cdd:PRK04863 874 LSALNRLLPRLN-LLADETLA--------DRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF----EQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1533 VGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELE 1612
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQ 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1613 AELeDERKQRalavaakkkmemdLKDLEGQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARASRDEIFAQSKESEKK 1691
Cdd:PRK04863 1013 AQL-AQYNQV-------------LASLKSSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRDELHARLSANRSR 1075
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 212450 1692 LKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALL------DEKRRLEAR 1747
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
859-1167 |
4.32e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 859 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQL-QAETELFAEAEEMRARLAAKKQELeeilhDL 937
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQL-----DK 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 938 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEeillledQNSKFLKEKKLMEDR 1017
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALET-------WYKRDLASLGVDPDV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1018 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEektRQELEKAKRKLDGETTDLQDQiaeLQAQIEELKIQLAK 1097
Cdd:pfam12128 770 IAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQR---RPRLATQLSNIERAISELQQQ---LARLIADTKLRRAK 843
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1098 KEEELQAAlargDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQ------KRDLSEELEALKTELED 1167
Cdd:pfam12128 844 LEMERKAS----EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLaqledlKLKRDYLSESVKKYVEH 915
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1005-1163 |
4.56e-06 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.78 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1005 SKFLK-EKKLMEDR---------IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGET 1074
Cdd:COG2433 350 NKFERvEKKVPPDVdrdevkarvIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1075 TDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEeavqknnalkvIRELQAQIAELQEDLESEkasrnkaEKQKRDL 1154
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEARSEERREIRKDRE-----------ISRLDREIERLERELEEE-------RERIEEL 491
|
....*....
gi 212450 1155 SEELEALKT 1163
Cdd:COG2433 492 KRKLERLKE 500
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
884-1482 |
5.23e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.98 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 884 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqghiq 963
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 964 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED--------------------RIAECts 1023
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1024 qLAEEEEKAKNLAKLK-NKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQIEELKIQLAKKEEEL 1102
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1103 QAALA-RGDEEAVQKNNALKVIRELqaqiaeLQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK 1181
Cdd:TIGR01612 1698 EIGIIeKIKEIAIANKEEIESIKEL------IEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAG 1771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1182 REQEVAElkkaiEEETKNheaqiqEIRQRHATALEELSEQLEQAKRFKANLeknkqglesDNKElacevkvLQQVKAESE 1261
Cdd:TIGR01612 1772 CLETVSK-----EPITYD------EIKNTRINAQNEFLKIIEIEKKSKSYL---------DDIE-------AKEFDRIIN 1824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1262 HKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVS---------------------SLLEEAEKKGIKFAKDA 1320
Cdd:TIGR01612 1825 HFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLlfdilnktkdayagiigkkyySYKDEAEKIFINISKLA 1904
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1321 ASLESQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNNLQEQQEEEEEARKNlEKQMLAL- 1379
Cdd:TIGR01612 1905 NSINIQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIi 1983
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1380 --QAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEE---------------KAMAYDKLEKTKNRLQQELDDL 1442
Cdd:TIGR01612 1984 feNQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKF 2063
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 212450 1443 MVDLDHQ--RQIVSNLEKKQKKFDQMLAEEKNISARYAEERD 1482
Cdd:TIGR01612 2064 GIDFDVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1345-1569 |
5.41e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1345 SSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvdddlgtIEGLEENKKKLLKDMESLSQRLEEKAMA 1424
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR-------IAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1425 YDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKNIsaRYAEERDRAEAEAREKETKAL-SLARAL 1502
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYL--KYLAPARREQAEELRADLAELaALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1503 EEALEAKEEFERQNKQLRADMEDLMSSKDDVgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1569
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEELEALIARLE 233
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1569-1731 |
5.41e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 51.57 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1569 EDAKLRLEVNMQAMKAQFErDLQAR-DEQNEEKKRMLV--KQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEA 1645
Cdd:pfam05667 327 EELQQQREEELEELQEQLE-DLESSiQELEKEIKKLESsiKQVEEELEELKEQNEELEKQYKVKKKTLDLLPDAEENIAK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1646 ANKARDEAIKQLRKLQAQMKDYQREL-EEARASRDEIFAQSKESEKKL---KGLEAEILQLQEEFAASERARRHAEQERD 1721
Cdd:pfam05667 406 LQALVDASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKEDESQRKLeeiKELREKIKEVAEEAKQKEELYKQLVAEYE 485
|
170
....*....|
gi 212450 1722 ELADEIANSA 1731
Cdd:pfam05667 486 RLPKDVSRSA 495
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1101-1278 |
6.20e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1101 ELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRT 1180
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1181 KREQEvaelkkAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVkvlqqvkAES 1260
Cdd:COG1579 88 NKEYE------ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL-------AEL 154
|
170
....*....|....*...
gi 212450 1261 EHKRKKLDAQVQELTAKV 1278
Cdd:COG1579 155 EAELEELEAEREELAAKI 172
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1121-1296 |
6.67e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.35 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1121 KVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL---EALKTELEDTLDTTAAQqelRTKREQEVAELKKAIEEEt 1197
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQALLAELAGA---GAAAEGRAGELAQELDSE- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1198 knheaqiQEIRQRHATALEELSEQLEQAKRfkanleknkqglesdnkELAcevkVLQQVKAESEHKRKKLDAQVQELtak 1277
Cdd:PRK09039 129 -------KQVSARALAQVELLNQQIAALRR-----------------QLA----ALEAALDASEKRDRESQAKIADL--- 177
|
170
....*....|....*....
gi 212450 1278 vteGERLRVELAEKANKLQ 1296
Cdd:PRK09039 178 ---GRRLNVALAQRVQELN 193
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1318-1747 |
6.79e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 6.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1318 KDAASLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQlaEAKKKVDDDLgti 1397
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMA---RELAELNEAESDLEQDYQAASDHLNLVQTALRQQ--EKIERYQADL--- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1398 egleenkkkllkdmESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMVDL-DHQ-------------RQIVSNL 1456
Cdd:PRK04863 358 --------------EELEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLaDYQqaldvqqtraiqyQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1457 EKKQKKFDQMLAEEKNISARYAEERDRAEA---EAREKETKaLSLARALEEALEAKEEFERQnkqLRADMEdlMSSKDDV 1533
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEateELLSLEQK-LSVAQAAHSQFEQAYQLVRK---IAGEVS--RSEAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1534 GKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQARDEQNEEKKRMLvkqvRELEA 1613
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQ----EELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1614 ELEDERKQRALAVAAKKKMEMDLKDLEGQIEaankardeaikQLRKLQAQMKDYQRELEEARASRDEIFAQSKesekklk 1693
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQ-----------RLAARAPAWLAAQDALARLREQSGEEFEDSQ------- 627
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 212450 1694 GLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEAR 1747
Cdd:PRK04863 628 DVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1076-1709 |
8.51e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.06 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1076 DLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLS 1155
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1156 EELEA---LKTELEDTLDTTAAQQELRTKREQEVAELKKAIE---EETKNHEAQIQEIRQRH--ATALEELSEQLEQAKR 1227
Cdd:PRK01156 267 MELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEnkkQILSNIDAEINKYHAIIkkLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1228 FKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLdaqvqeltakvtegERLRVELAEKANKLQNELDNVSSLLE 1307
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI--------------ERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1308 EAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNlqeqqeeeeEARKNLEKQMLALQA 1381
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSN---------HIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1382 QLAEAKKKVDDdlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1461
Cdd:PRK01156 484 KIREIEIEVKD-------IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1462 KFDQMLAEEKNISARYAEERdraeaeaREKETKALSLARAleealeakeeferqnkqlrADMEDLMSSKDDVGKNVHELE 1541
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSK-------RTSWLNALAVISL-------------------IDIETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1542 KSKRTLEQQVEEMRT----QLEELEDELQATEDAKLRLEVNMQAMkaqferdlqardeqneEKKRMLVKQVRELEAELED 1617
Cdd:PRK01156 601 SRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILI----------------EKLRGKIDNYKKQIAEIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1618 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEaikqLRKLQAQMKDYQRELEEARASRDEIFaqskESEKKLKGLEA 1697
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR----LESTIEILRTRINELSDRINDINETL----ESMKKIKKAIG 736
|
650
....*....|..
gi 212450 1698 EILQLQEEFAAS 1709
Cdd:PRK01156 737 DLKRLREAFDKS 748
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
980-1443 |
8.59e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 980 QLEKVTAEA-------KIKKMEEEILLLEDQNSKFLKEKKLMEDRIAEC-TSQLAEEEEKAKNLAKLKNKQEMMITDLEE 1051
Cdd:TIGR01612 1154 DLEDVADKAisnddpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1052 RLKKEEKTRQELEKAKRKLDG------ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI-- 1123
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDLDEikekspEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIed 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1124 -----------RELQAQIAELQED--------------------------LESEKASRNKAEKQKRDLSEE--------- 1157
Cdd:TIGR01612 1314 fseesdindikKELQKNLLDAQKHnsdinlylneianiynilklnkikkiIDEVKEYTKEIEENNKNIKDEldkseklik 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1158 -------LEALKTELEDTLD----------TTAAQQELRTKREQEVAELKKAIE------------EETKNHEAQIQEIR 1208
Cdd:TIGR01612 1394 kikddinLEECKSKIESTLDdkdidecikkIKELKNHILSEESNIDTYFKNADEnnenvlllfkniEMADNKSQHILKIK 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1209 QRHATA-----LEELSEQLEQAKRFKANLEKNKQGLESD---------------NKELACEVK-VLQQVKAESE------ 1261
Cdd:TIGR01612 1474 KDNATNdhdfnINELKEHIDKSKGCKDEADKNAKAIEKNkelfeqykkdvtellNKYSALAIKnKFAKTKKDSEiiikei 1553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1262 ---HKRKKLDAQVQELTAKVTEGERLRVE-LAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELlqEE 1337
Cdd:TIGR01612 1554 kdaHKKFILEAEKSEQKIKEIKKEKFRIEdDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESI--EK 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1338 TRQKLNLSSRIRQLEEEKNN---LQEQQEEEEEARKNLEKQmlalqaqlaeaKKKVDDDLGTIEGLEENKKKLLKDME-S 1413
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNlnsLQEFLESLKDQKKNIEDK-----------KKELDELDSEIEKIEIDVDQHKKNYEiG 1700
|
570 580 590
....*....|....*....|....*....|.
gi 212450 1414 LSQRLEEKAMA-YDKLEKTKNRLQQELDDLM 1443
Cdd:TIGR01612 1701 IIEKIKEIAIAnKEEIESIKELIEPTIENLI 1731
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1426-1691 |
9.74e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1426 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAR 1489
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1490 EKETKALSLaraleealeakeeferqnKQLRADMEDLMSSKDDVGKNVHELEKSKR--TLEQQVEEMRTQLEELEDelqa 1567
Cdd:PHA02562 249 DIEDPSAAL------------------NKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKD---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1568 tedaklrlevNMQAMKAQFERDLQARDEQNE--EKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmdlkdlegqiea 1645
Cdd:PHA02562 307 ----------KLKELQHSLEKLDTAIDELEEimDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK------------ 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 212450 1646 ankardeaiKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1691
Cdd:PHA02562 365 ---------AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1607-1929 |
1.00e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 50.07 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1607 QVRELEAELEDERkqralavAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:pfam19220 49 RLLELEALLAQER-------AAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1687 ESEKKLKG-------LEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQ 1759
Cdd:pfam19220 122 ALERQLAAeteqnraLEEENKALREEAQAAEKALQRAEGELATARERLA-------LLEQENRRLQALSEEQAAELAELT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1760 SNMELLNERFRKTTLQVDTLNSELAGERSAAQKSEnarqqlerqnkelkaklqelegsvkskfkatistleakiAQLEEQ 1839
Cdd:pfam19220 195 RRLAELETQLDATRARLRALEGQLAAEQAERERAE---------------------------------------AQLEEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1840 LEQEAKERA-------AANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRK 1912
Cdd:pfam19220 236 VEAHRAERAslrmkleALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQE 315
|
330
....*....|....*..
gi 212450 1913 LQRELDDATEANEGLSR 1929
Cdd:pfam19220 316 MQRARAELEERAEMLTK 332
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
856-1222 |
1.06e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEekniLAEQLQAETELfAEAEEMRARLAAKKQELEEILH 935
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR----LAEYSWDEIDV-ASAEREIAELEAELERLDASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 936 DLEsrveeeeernqilqnekkkmqghiqdleeqldeeegarqKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLME 1015
Cdd:COG4913 686 DLA---------------------------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1016 DRIAECTSQLAEEEEKAKNLAklknkqemmITDLEERLKKEEKTRQElEKAKRKLDGETTDLQDQIAELQAQIEELKIQL 1095
Cdd:COG4913 727 EELDELQDRLEAAEDLARLEL---------RALLEERFAAALGDAVE-RELRENLEERIDALRARLNRAEEELERAMRAF 796
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1096 AKKEEELQAALARGDEEAVQKNNALKVIR-----ELQAQIAELQEDLESEKASR--NKAEKQKRDLSEELEALKTELEDT 1168
Cdd:COG4913 797 NREWPAETADLDADLESLPEYLALLDRLEedglpEYEERFKELLNENSIEFVADllSKLRRAIREIKERIDPLNDSLKRI 876
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1169 L--DTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQL 1222
Cdd:COG4913 877 PfgPGRYLRLEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1040-1295 |
1.12e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1040 NKQEMMITDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK 1116
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1117 NNALKVIRELQAQIAELQEdlesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK---REQEVAELKKAI 1193
Cdd:COG1340 81 DELNEKLNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1194 EEETKNHE--AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKElacevkvLQQVKAESEHKRKKLDAQV 1271
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE-------ADELHKEIVEAQEKADELH 229
|
250 260
....*....|....*....|....
gi 212450 1272 QELTAKVTEGERLRVELAEKANKL 1295
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQ 253
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1026-1390 |
1.18e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1026 AEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKakrkldgETTDLQDQIAELQAQIEELKIQLAKKEEELQAA 1105
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQE-------ELEQLREELEQAREELEQLEEELEQARSELEQL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1106 LARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQE 1185
Cdd:COG4372 79 EEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1186 VAELKKAIEEETKNHEAQIQEIRQRhatALEELSEQLEQAKRFKANLEKNKQGLESDNKELAcEVKVLQQVKAESEHKRK 1265
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQ---ALDELLKEANRNAEKEEELAEAEKLIESLPRELA-EELLEAKDSLEAKLGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1266 KLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLS 1345
Cdd:COG4372 235 LSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALE 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 212450 1346 SRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKV 1390
Cdd:COG4372 315 DALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1057-1334 |
1.23e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.53 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1057 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALK 1121
Cdd:pfam00038 18 DKVRF-LEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1122 VIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKAIEEETKNHE 1201
Cdd:pfam00038 97 LRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1202 aqIQEIRQRH-ATALEELSEQLE-QAKRFKANLEKN-KQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKV 1278
Cdd:pfam00038 160 --MDAARKLDlTSALAEIRAQYEeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1279 TEGERLRVELAEKANKLQNELDNVSSLLEEAEKkgiKFAKDAASLESQLQDTQELL 1334
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISELEA---ELQETRQEMARQLREYQELL 290
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1558-1937 |
1.24e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1558 LEELEdELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLK 1637
Cdd:PTZ00121 1029 IEELT-EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQD--EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1638 DLEGQIEAANKARdEAIKQLRKLqaqmkdyqRELEEARasRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1717
Cdd:PTZ00121 1106 TETGKAEEARKAE-EAKKKAEDA--------RKAEEAR--KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1718 QERDELA---DEIANSASGKSAllDEKRRLEAriAQLEEELEEEQSNMELLNERFRKTTLQVDtlnselagerSAAQKSE 1794
Cdd:PTZ00121 1175 AKKAEAArkaEEVRKAEELRKA--EDARKAEA--ARKAEEERKAEEARKAEDAKKAEAVKKAE----------EAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1795 NARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAqleEQLeQEAKERAAANKLVRRTEKKLKEVFMQVEDERRH 1874
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DEL-KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1875 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1937
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
985-1310 |
1.26e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.22 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 985 TAEAKIKKMEEEILLL---EDQNSKFLKE---------KKLMEDR------IAECTSQLAEEEEKAKNLAKLKN-----K 1041
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEEFSQFVELTEsgdyvE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1042 QEMMITDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQIEELKIQ---------------LAKKEEELQAAL 1106
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeiqdLKEQIDENLALL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1107 ARGDEEAVQKNNAlkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEV 1186
Cdd:PRK04778 273 EELDLDEAEEKNE-----EIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1187 aELKKAIEEETKNHEAQIQEIRQRHATA----------LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQV 1256
Cdd:PRK04778 348 -ESVRQLEKQLESLEKQYDEITERIAEQeiayselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1257 KAESEHKRKKL------DAQVQELTAKVTEGERLRVELaekaNKLQNELDNVSSLLEEAE 1310
Cdd:PRK04778 427 LHEIKRYLEKSnlpglpEDYLEMFFEVSDEIEALAEEL----EEKPINMEAVNRLLEEAT 482
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
667-691 |
1.29e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 47.34 E-value: 1.29e-05
10 20
....*....|....*....|....*
gi 212450 667 YKESLTKLMATLRNTNPNFVRCIIP 691
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
981-1149 |
1.54e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 981 LEKVTAEAKIKKMEEEIllledqnSKFLKE-KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQ-EMMITDLEERLKKEEK 1058
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRErRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1059 T----RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvqKNNAL-KVIRELQAQIAEL 1133
Cdd:PRK12704 97 NldrkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEA--KEILLeKVEEEARHEAAVL 174
|
170
....*....|....*.
gi 212450 1134 QEDLESEkaSRNKAEK 1149
Cdd:PRK12704 175 IKEIEEE--AKEEADK 188
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
911-1469 |
1.90e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 911 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 990
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 991 K-KMEEEILLLEDQN--SKFLKEKKLMEDRIAECTSQLAEEEEKAKNlaklknkqemmITDLEERLKKEEKTRQeleKAK 1067
Cdd:PRK01156 228 NnAMDDYNNLKSALNelSSLEDMKNRYESEIKTAESDLSMELEKNNY-----------YKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1068 RKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQ--AALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1145
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1146 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhataLEELSEQL--- 1222
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1223 ---------------EQAKRFKANLEKNKQGLESDNKELACEVKVL-----QQVKAESEHKRKKL------DAQVQELTA 1276
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIdekivDLKKRKEYLESEEInksineYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1277 KVTEGERLRVELAEKANKLQNELDNVSSL-LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLN-LSSRIRQLEEE 1354
Cdd:PRK01156 530 DLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNdLESRLQEIEIG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1355 KNNLQEQQEEEEEARKNlEKQMLALQAQLAEAKKKVDDdlgTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNR 1434
Cdd:PRK01156 610 FPDDKSYIDKSIREIEN-EANNLNNKYNEIQENKILIE---KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKK 685
|
570 580 590
....*....|....*....|....*....|....*
gi 212450 1435 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1469
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1050-1436 |
2.10e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1050 EERLKKEEKTRQELEKAKRKLDGETTDLQD-------QIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV 1122
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1123 IRELQAQIAELQEDLESEKASRNKAEKQKRdlsEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieeETKNHEA 1202
Cdd:pfam10174 438 LTTLEEALSEKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK-----EHASSLA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1203 QIQEIRQRHATALE-ELSEQLEQAKRFKANLEKNKQGLESD--NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVT 1279
Cdd:pfam10174 510 SSGLKKDSKLKSLEiAVEQKKEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILR 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1280 EGERLRVELAEKANKLQN-----------ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQ--------EETRQ 1340
Cdd:pfam10174 590 EVENEKNDKDKKIAELESltlrqmkeqnkKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQleelmgalEKTRQ 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1341 KLN-----LSSRIRQLEEEKNNLQEQQEEEeeaRKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLs 1415
Cdd:pfam10174 670 ELDatkarLSSTQQSLAEKDGHLTNLRAER---RKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMAL- 745
|
410 420
....*....|....*....|.
gi 212450 1416 qRLEEKAMAYDKLEKTKNRLQ 1436
Cdd:pfam10174 746 -KREKDRLVHQLKQQTQNRMK 765
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
855-1162 |
2.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 855 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERkhqqLLEEKNILAEQLQAETELFAEAEEmraRLAAKKQELEEil 934
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEK-- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 935 hdLESRVEEEEERNQILQNEKKKMQGhiqdleeqldeeegarqkLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKklm 1014
Cdd:PRK03918 530 --LKEKLIKLKGEIKSLKKELEKLEE------------------LKKKLAELEKKLDELEEELAELLKELEELGFES--- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 edrIAECTSQLAEEEEKAKNLAKLKNKQEmmitDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQIEELKIQ 1094
Cdd:PRK03918 587 ---VEELEERLKELEPFYNEYLELKDAEK----ELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKK 655
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1095 LAKKE-EELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1162
Cdd:PRK03918 656 YSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1321-1750 |
2.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1321 ASLESQLQ-DTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEkQMLALQAQLAEAKKKVDDDLGTIEG 1399
Cdd:COG4717 45 AMLLERLEkEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1400 LEEN------KKKLLKDMESLSQRLEE---KAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQkkFDQMLAEE 1470
Cdd:COG4717 124 LLQLlplyqeLEALEAELAELPERLEEleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE--LQDLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1471 KNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKR----- 1545
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1546 ------TLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMlVKQVRELEAELEDER 1619
Cdd:COG4717 282 vlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR-IEELQELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1620 KQRALAVAAKKKMEMdLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEkklkgLEAEI 1699
Cdd:COG4717 361 EELQLEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-----LEEEL 434
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 212450 1700 LQLQEEFAASERARRHAEQERDELADEIANSASGK--SALLDEKRRLEARIAQ 1750
Cdd:COG4717 435 EELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
852-1255 |
2.28e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 852 KPLLQVTRQEEELQAKD--EELMKVKEKQTKVEAELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 929
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 930 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLK 1009
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1010 EKKLMEDRIAECTSQLAEEEEKAKNLaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIE 1089
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1090 ELKIQLAKKeEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESE-KASRNKAEKQKRDLSEELEALK------ 1162
Cdd:pfam07888 224 TAHRKEAEN-EALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAElHQARLQAAQLTLQLADASLALRegrarw 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1163 -TELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANL---EKNKQG 1238
Cdd:pfam07888 303 aQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQ 382
|
410
....*....|....*..
gi 212450 1239 LESDNKELACEVKVLQQ 1255
Cdd:pfam07888 383 LQAEKQELLEYIRQLEQ 399
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1274-1628 |
2.29e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.91 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1274 LTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA---EKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1350
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELaglTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1351 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEK 1430
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1431 TKNRLQQELDDlmvdldhQRQIVSNLEKKqkkFDQMLAEEKNISARYAEERDRAEAEAReketkalSLARALEEALEAKE 1510
Cdd:pfam19220 196 RLAELETQLDA-------TRARLRALEGQ---LAAEQAERERAEAQLEEAVEAHRAERA-------SLRMKLEALTARAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1511 EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE--VNM-----QAMK 1583
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerAEMltkalAAKD 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1584 AQFER------DLQARDEQ----NEEKKRMLVKQVRELEAELEDERKQRALAVAA 1628
Cdd:pfam19220 339 AALERaeeriaSLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1517-1736 |
2.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1517 KQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1577
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1578 NMQAMKAQFERDLQARDEQNEEKKrmlvkQVRELEAELEDERKQralAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1657
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKA-----ELEAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1658 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSA 1736
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1149-1387 |
2.53e-05 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 49.18 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1149 KQKRDLSEELEALKTELEDT----------LDTTAAQQEL-RTKREQEVAE----LKKAIEEETKNHEAQIQE----IRQ 1209
Cdd:pfam07902 78 KSLEEMLSQLKELNLELTDTknsnlwskikLNNNGMLREYhNDTIKTEIVEsaegIATRISEDTDKKLALINEtisgIRR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1210 RHATALEELSEqleqakRFKANLEKNKQGLESDNKELACEVKV-LQQVKAESEHKRKKLDAQVQELTAKVTEG------- 1281
Cdd:pfam07902 158 EYQDADRQLSS------SYQAGIEGLKATMASDKIGLQAEIQAsAQGLSQRYDNEIRKLSAKITTTSSGTTEAyeskldd 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1282 ---------ERLRVELAEKANKL----QNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQEL----------LQEET 1338
Cdd:pfam07902 232 lraeftrsnQGMRTELESKISGLqstqQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQDAEKNyssltqtvkgLQSTV 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 212450 1339 R-QKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAK 1387
Cdd:pfam07902 312 SdPNSKLESRITQLAGLIEQKVTRGDVESIIRQSGDSIMLAIKAKLPQSK 361
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1063-1219 |
2.61e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.57 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1063 LEKAKRKLDGETTDLQDQIAELQAQIEelkiQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA 1142
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1143 SRNKAEKQKRDLsEELEALKTELEDTLDTTAAQQE-LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1219
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1258-1435 |
2.66e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1258 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLESQLQD--TQELLQ 1335
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNvrNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1336 EETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDlgtIEGLEENKKKLLKDMESLS 1415
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELA 169
|
170 180
....*....|....*....|.
gi 212450 1416 QRLEEKAMA-YDKLEKTKNRL 1435
Cdd:COG1579 170 AKIPPELLAlYERIRKRKNGL 190
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
977-1150 |
3.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 977 QKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLE------ 1050
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1051 --------------------ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGD 1110
Cdd:COG3883 113 sfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 212450 1111 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQ 1150
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1063-1224 |
3.41e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1063 LEKAKrkldgeTTDLQDQIAELQAQieelkiqLAKKEEE---LQAALARGDEEAvqknnalkviRELQAQIAELQEDLES 1139
Cdd:PRK09039 71 LERQG------NQDLQDSVANLRAS-------LSAAEAErsrLQALLAELAGAG----------AAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1140 EKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1219
Cdd:PRK09039 128 EKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....*
gi 212450 1220 EQLEQ 1224
Cdd:PRK09039 190 QELNR 194
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1595-1747 |
3.73e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.13 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1595 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE--------AANKARD----EAIKQLRKLQA 1662
Cdd:COG1842 19 DKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEkweekarlALEKGREdlarEALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1663 QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEilqlQEEFAASERARRHAEQERDELADEIANSASGKSALLDEK- 1741
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAK----KDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKi 174
|
....*.
gi 212450 1742 RRLEAR 1747
Cdd:COG1842 175 EEMEAR 180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1376-1598 |
4.02e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1376 MLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQivsN 1455
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1456 LEKKQKKFDQMLAE--EKNISARYAEE----RDRAEAEAReketkALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1529
Cdd:COG3883 81 IEERREELGERARAlyRSGGSVSYLDVllgsESFSDFLDR-----LSALSKIADADADLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1530 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNE 1598
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1253-1381 |
4.21e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1253 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAAslESQLQDTQE 1332
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 212450 1333 LLQEETRqklnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1381
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1064-1320 |
4.62e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1064 EKAKRKLDGETTDLQDQIAELqaqiEELKIQLAKKEEELQAALArgdeeavqknnalkvirelqaQIAELQEDLEsekas 1143
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASL----EELERELEQKAEEAEALLK---------------------EAEKLKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1144 rnkaeKQKRDLSEELEALKTELEDtldttaaqqelrtKREQEVAELKKAIEEETKN-HEAQIQEIRQRHATALEELSEQL 1222
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-------------EAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1223 EQAKRfKANLEKNKQGLESDNKELACEVKVLQ-QVKAESEHKRKKLDAQVQE----LTAKVTEGERLRVELAEKANKLQN 1297
Cdd:PRK00409 617 NKANE-KKEKKKKKQKEKQEELKVGDEVKYLSlGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKKPKT 695
|
250 260 270
....*....|....*....|....*....|...
gi 212450 1298 ELDNVSSL----------LEEAEKKGIKFAKDA 1320
Cdd:PRK00409 696 VKPKPRTVsleldlrgmrYEEALERLDKYLDDA 728
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
931-1147 |
4.74e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 931 EEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKE 1010
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1011 KKlMEDRIAECTSQLAEEE------EKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1084
Cdd:COG3883 95 LY-RSGGSVSYLDVLLGSEsfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1085 QAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKA 1147
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1402-1938 |
5.07e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1402 ENKKKLLKDMESLSQRLEEKAMAYD-------KLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS 1474
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAkkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1475 ARYAEERDRAEAEAReketkalslaraleealeakeeFERQNKQLRADMEDLMSSKddvgkNVHELEKSKRTLEQQVEEM 1554
Cdd:TIGR00618 243 AYLTQKREAQEEQLK----------------------KQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1555 RTQLEELEDELQATEDAKLRLEVNMQAM-KAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKK-- 1631
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqh 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1632 -MEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASE 1710
Cdd:TIGR00618 376 tLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1711 RARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAqleeELEEEQSNMELLNERFRKTTlQVDTLNSELAGERSAA 1790
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1791 QKSENARQQLERQNKELKAKLQELEGSVKSkFKATIsTLEAKIAQLEEQLEQEAKEraAANKLVRRTEKKLKEVFMQVED 1870
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRAS-LKEQM-QEIQQSFSILTQCDNRSKE--DIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1871 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
975-1116 |
5.12e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLK---------NKQEMM 1045
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1046 ITDLEERLK----KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK 1116
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1244-1894 |
5.45e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1244 KELACEVKVLQQVkaeSEHKRKKLDAQVQELTAkvtegerlrVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKdaasl 1323
Cdd:pfam07111 76 RRLEEEVRLLRET---SLQQKMRLEAQAMELDA---------LAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1324 ESQLQDTQELLQEEtrqklnLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEEN 1403
Cdd:pfam07111 139 QRELEEIQRLHQEQ------LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1404 KKKLLKDMESLSQRLEEKAMA---YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEE 1480
Cdd:pfam07111 213 LEAQVTLVESLRKYVGEQVPPevhSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1481 RDRAEAEAREKETKALSLARALEEALEAkeeferqnkQLRADMEDLMSSKDDVGKNVHELEK--SKRTLEQQVEEMRTQL 1558
Cdd:pfam07111 293 SDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDLEHRDSVKQLRGQVAELQEqvTSQSQEQAILQRALQD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1559 EELEDELQATEDAKLRLEVNmQAMKAQfeRDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKD 1638
Cdd:pfam07111 364 KAAEVEVERMSAKGLQMELS-RAQEAR--RRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1639 LEGQIEAANK--ARDEAIKQLRKLQAQM--------KDYQRELEEARASRDEIFAQSKesekklkgLEAEILQLQeefaa 1708
Cdd:pfam07111 441 AVRKVHTIKGlmARKVALAQLRQESCPPpppappvdADLSLELEQLREERNRLDAELQ--------LSAHLIQQE----- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1709 SERARRHAEQERdeladeiansasgksalldekRRLEARIAQLEEELEEEQSNMELLNERfrkttlqvdtLNSELAGERS 1788
Cdd:pfam07111 508 VGRAREQGEAER---------------------QQLSEVAQQLEQELQRAQESLASVGQQ----------LEVARQGQQE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1789 AAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKiaqLEEQLEQEAKERAAANKLVRRT--EKKLKEVFM 1866
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQHRAtqEKERNQELR 633
|
650 660
....*....|....*....|....*...
gi 212450 1867 QVEDERRhadqyKEQMEKANARMKQLKR 1894
Cdd:pfam07111 634 RLQDEAR-----KEEGQRLARRVQELER 656
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
998-1392 |
5.63e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 998 LLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLaklKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDL 1077
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL---EIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEEL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1078 QDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE-DLESEKASRNKAEKQKRDLSE 1156
Cdd:pfam02463 739 KLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLkAQEEELRALEEELKEEAELLE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1157 ELEALKTELEDTLDTTAAQQELRTKREQEvaELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNK 1236
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEK 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1237 QGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKF 1316
Cdd:pfam02463 897 EEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVN 976
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1317 AKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1392
Cdd:pfam02463 977 LMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLED 1052
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1642-1922 |
5.71e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1642 QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKGLEAEILQLQEEfaasERARRHAE 1717
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1718 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnERFRKTTLQVDTLnSELAGERSAAQKSENAR 1797
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEM-EQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1798 QQLERQNKELKAKLQELEgsvKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRT-EKKLKEVFMQ-VEDERRHA 1875
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 212450 1876 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1922
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1134-1488 |
5.81e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 5.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1134 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaiEEETKNheaQIQEIRQrhat 1213
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR---QEERKR---ELERIRQ---- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1214 alEELSEQLEQAKRfkanLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVElaekan 1293
Cdd:pfam17380 368 --EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQR------ 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1294 klqneldNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNL--SSRIRQLEEEKNnlqeqqeeeeeaRKN 1371
Cdd:pfam17380 436 -------EVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELekEKRDRKRAEEQR------------RKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1372 LEKQMLALQAQLAEakkkvdddlgtieglEENKKKLL-KDMESlsqrlEEKAMAydklEKTKNRLQQELDDLMVDLDHQR 1450
Cdd:pfam17380 497 LEKELEERKQAMIE---------------EERKRKLLeKEMEE-----RQKAIY----EEERRREAEEERRKQQEMEERR 552
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 212450 1451 QIVSNLEK---KQKKFDQMLAEEKNISARYAEERDRAEAEA 1488
Cdd:pfam17380 553 RIQEQMRKateERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1049-1223 |
6.28e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 45.72 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1049 LEERLKKEEKTRQELEKakrKLDGETTDLQDQIAElqaQIEELKIQLAKKEEELQAALARGDEEAVQKNNalKVIRELQA 1128
Cdd:pfam01442 2 LEDSLDELSTYAEELQE---QLGPVAQELVDRLEK---ETEALRERLQKDLEEVRAKLEPYLEELQAKLG--QNVEELRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1129 QIAELQEDLEseKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKAIEEETKNHEAQ 1203
Cdd:pfam01442 74 RLEPYTEELR--KRLNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQ 151
|
170 180
....*....|....*....|....
gi 212450 1204 ----IQEIRQRHATALEELSEQLE 1223
Cdd:pfam01442 152 lsqrLQELREKLEPQAEDLREKLD 175
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
996-1146 |
6.45e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 996 EILLLEDQNSKFLkekklmEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLkkeektrQELEKAKRKLDGETT 1075
Cdd:PRK09039 67 DLLSLERQGNQDL------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 1076 DLQDQIAELQAQIEELKIQLAKKEEELQAALARGdeeavqknnalkviRELQAQIAELQEDLESEKASRNK 1146
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQLAALEAALDASEKRD--------------RESQAKIADLGRRLNVALAQRVQ 190
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
855-1102 |
6.49e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 48.20 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 855 LQVTRQEEelqaKDEELMKVKEKQTKVEAE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 933
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 934 LHDLESrveEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLkEKKL 1013
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1014 MEDRIAectsqLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKldgettDLQDQIaeLQAQIEELKI 1093
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM--RKATEERSRL 568
|
....*....
gi 212450 1094 QLAKKEEEL 1102
Cdd:pfam17380 569 EAMEREREM 577
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
986-1132 |
7.12e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 47.75 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 986 AEAKIKKM--EEEILLLEDQNSKFLKEKKLMEDRIA---ECTSQLAEEEEKAKNL--AKLKNKQEMMITDLEERLKKEEK 1058
Cdd:pfam13166 344 LEAKRKDPfkSIELDSVDAKIESINDLVASINELIAkhnEITDNFEEEKNKAKKKlrLHLVEEFKSEIDEYKDKYAGLEK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1059 TRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDE-EAVQKNNALKVIRELQAQIAE 1132
Cdd:pfam13166 424 AINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADEINKLLKAFGFGELElSFNEEGKGYRIIRKGGSQAAE 498
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
853-1226 |
7.55e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 853 PLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 931
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 932 EILHDLESrvEEEEERNQILQnekkkmqghiqdleeqldeeegARQKLQLekvtaeakIKKMEEEILLLEDQNskflkek 1011
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1012 klMEDRIAECTSQLAEEEEKA-------KNLAKLKNKQEMMITDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1078
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1079 ----DQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvqknnalkviRELQAQIAELQEDLESEKASRNKAEKQKRDL 1154
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQL----------RQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1155 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKAIEEETKNHEAQiqeirQRHATALEE----LSEQLEQ 1224
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 212450 1225 AK 1226
Cdd:PRK04863 1114 AK 1115
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1560-1837 |
7.70e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1560 ELEDELQATEDAKLRLEvnmqAMKAQFERDLQARDEQNEEKKRmlvkqvrELEAELEDERKQRALAVAAKKKMEMDLKDL 1639
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAE-------ARAAKDKDAVAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1640 EGQIEAANKARdEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEF-----AASERARR 1714
Cdd:PRK05035 509 KAGARPDNSAV-IAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEvdpkkAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1715 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMEllnerfrkTTLQVDTLNSELAGERSAAQKSE 1794
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE--------PEEPVDPRKAAVAAAIARAKARK 659
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 212450 1795 NARQQLErqnkelkAKLQELEGSVKSKFKATISTLEAKIAQLE 1837
Cdd:PRK05035 660 AAQQQAN-------AEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1213-1416 |
7.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1213 TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtegERLRVELAEKA 1292
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1293 NKLQNELDNVSSLLEEAEKKGI-KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKN 1371
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 212450 1372 LEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQ 1416
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1036-1142 |
8.30e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1036 AKLKNKQEMM---ITDLEERLKKEEKTRQELEKAKRKLDGET-TDLQDQIAELQAQIEELKIQLaKKEEELQAALARGDE 1111
Cdd:COG0542 400 ARVRMEIDSKpeeLDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARW-EAEKELIEEIQELKE 478
|
90 100 110
....*....|....*....|....*....|.
gi 212450 1112 EAVQKNNalkVIRELQAQIAELQEDLESEKA 1142
Cdd:COG0542 479 ELEQRYG---KIPELEKELAELEEELAELAP 506
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1319-1529 |
8.56e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1319 DAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDL---- 1394
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1395 ---GTIEGLE-----ENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM 1466
Cdd:COG3883 97 rsgGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1467 LAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1529
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
861-1358 |
8.94e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.59 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEA-------ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 933
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKshsitlkEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 934 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEeillLEDQNSKFLKE 1010
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1011 KKLMEDRIAECT----------SQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQLAKKEEELQAALAR----------GDEEA--------VQKNNALKVIRELQAQIAELQEDLESEKA 1142
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlGEEKSnhiinhynEKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1143 SRNKAEKQKRDLSE----ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-IEEETKNHEAQIQEIRQRHATALEE 1217
Cdd:PRK01156 505 RKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1218 LSEQLEQAKRFKANLEKNKQGLESDnkelacevkvLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQN 1297
Cdd:PRK01156 585 NRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDN 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1298 ------ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1358
Cdd:PRK01156 655 ykkqiaEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1402-1676 |
9.79e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 9.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1402 ENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfdqmlaeeknisaryAEER 1481
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------------ALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1482 DRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKDdvgknVHELEKSKRTLEQQVEEMRTQLEEL 1561
Cdd:COG4942 84 ELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPED-----FLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1562 EDELQatedaklrlevnmqamkaqferDLQARDEQNEEKKrmlvKQVRELEAELEDERKQRALAVAAKKKMemdLKDLEG 1641
Cdd:COG4942 156 RADLA----------------------ELAALRAELEAER----AELEALLAELEEERAALEALKAERQKL---LARLEK 206
|
250 260 270
....*....|....*....|....*....|....*
gi 212450 1642 QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARA 1676
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1010-1212 |
1.06e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.62 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1010 EKKLMEDRIaectsQLAEEEEKAKNLAklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQ------DQIAE 1083
Cdd:PLN03188 1046 EKKLEQERL-----RWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRCAEELKEAMQmameghARMLE 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1084 LQAQIEELKIQLAKKEEELQAAL---ARGDEEAVQKNNALKVIRELQAQIAELqedleseKASRnkaEKQKRDLSEELEA 1160
Cdd:PLN03188 1115 QYADLEEKHIQLLARHRRIQEGIddvKKAAARAGVRGAESKFINALAAEISAL-------KVER---EKERRYLRDENKS 1184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1161 LKTELEDTLDTTAAQQELRT-------------KR----EQEVAELKKAIEEETKNHEAQIQEIRQRHA 1212
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVrlkeaeealtvaqKRamdaEQEAAEAYKQIDKLKRKHENEISTLNQLVA 1253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1177-1973 |
1.11e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1177 ELRTKREQEVAELKKAIEEEtknheaqiqeiRQRHatalEELSEQLEQAKRFKANLEknkQGLESDNKELACEVKVLQQV 1256
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAE-----------QYRL----VEMARELAELNEAESDLE---QDYQAASDHLNLVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1257 KAEsehkrKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELdnvssllEEAEKkgikfakDAASLESQLQDTQELLQE 1336
Cdd:PRK04863 348 EKI-----ERYQADLEELEERLEEQNEVVEEADEQQEENEARA-------EAAEE-------EVDELKSQLADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1337 -ETR-----QKLNLSSRIRQL-----------EEEKNNLQEQQEEEEEARKNLEKQMLALQA---QLAEAKKKVDDDLGT 1396
Cdd:PRK04863 409 qQTRaiqyqQAVQALERAKQLcglpdltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1397 IEGLE--ENKKKLLKDMES---LSQRLEEkamaydklektknrLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEk 1471
Cdd:PRK04863 489 VSRSEawDVARELLRRLREqrhLAEQLQQ--------------LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1472 nisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsSKDDVGKNVHEL-----EKSKRT 1546
Cdd:PRK04863 554 ----------DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA-ARAPAWLAAQDAlarlrEQSGEE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1547 LE--QQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVR-ELEAELEDE----- 1618
Cdd:PRK04863 623 FEdsQDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLNALAERFGgVLLSEIYDDvsled 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1619 ---------RKQRALAV----AAKKKME------MDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARASRD 1679
Cdd:PRK04863 699 apyfsalygPARHAIVVpdlsDAAEQLAgledcpEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQWRYSRFPEV 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1680 EIFAQsKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAS---------GKSALLDEKRRLEARIAQ 1750
Cdd:PRK04863 777 PLFGR-AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALAD 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1751 LEEELEEEQSNMELLNERF--------RKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELkAKLQELEGSVKSKf 1822
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIVSVLQSD- 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1823 KATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTE------------------KKLKEVFMQVEDERrhaDQYKEQMEK 1884
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaaemlaknsdlnEKLRQRLEQAEQER---TRAREQLRQ 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1885 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDAT-----EANEGLSREVSTLKNRLRRggpitfssSRSGRRQLHIE 1959
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsGAEERARARRDELHARLSA--------NRSRRNQLEKQ 1082
|
890
....*....|....
gi 212450 1960 GASLELSDDDAESK 1973
Cdd:PRK04863 1083 LTFCEAEMDNLTKK 1096
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1093-1433 |
1.14e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1093 IQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1172
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1173 AAQQELRTKREQEVAELKK---AIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACE 1249
Cdd:COG4372 104 ESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1250 VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQD 1329
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1330 TQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLK 1409
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLL 343
|
330 340
....*....|....*....|....
gi 212450 1410 DMESLSQRLEEKAMAYDKLEKTKN 1433
Cdd:COG4372 344 QLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
812-1247 |
1.25e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 812 ARKAFAKKQQQLSALKILQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELMKVKEKQ 878
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 879 TKV-----------------------------EAELEEMERKHQQLLEEKNILAEQLQAETELFAE----AEEMRARLAA 925
Cdd:COG4913 319 DALreeldeleaqirgnggdrleqlereierlERELEERERRRARLEALLAALGLPLPASAEEFAAlraeAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 926 KKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEeegARQKL--QLEKVTAEAKIK------KMEEEI 997
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA---LRDALaeALGLDEAELPFVgelievRPEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 998 ---------------LLLEDQN-SKFLK-------EKKLMEDRIAECTSQLAEEEEKAKNLA-KLKNK---------QEM 1044
Cdd:COG4913 476 wrgaiervlggfaltLLVPPEHyAAALRwvnrlhlRGRLVYERVRTGLPDPERPRLDPDSLAgKLDFKphpfrawleAEL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1045 ------MITDLEERLKKEEK--TRQEL--------EKAKRKLDGET-----------TDLQDQIAELQAQIEELKIQLAK 1097
Cdd:COG4913 556 grrfdyVCVDSPEELRRHPRaiTRAGQvkgngtrhEKDDRRRIRSRyvlgfdnraklAALEAELAELEEELAEAEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1098 KEEELQAALARGD--EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKqkrdLSEELEALKTELEDTLDTTAAQ 1175
Cdd:COG4913 636 LEAELDALQERREalQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDEL 711
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1176 QELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQL---EQAKRFKANLEKNKQGLESDNKELA 1247
Cdd:COG4913 712 KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAAlgdAVERELRENLEERIDALRARLNRAE 786
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1038-1469 |
1.41e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 46.77 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1038 LKNKQEMMITDLEERlKKEEKTR---QELEKAKR-KLDGETtdlQDQIAELQAQIEELK-IQLAKKEEELQAAlargdEE 1112
Cdd:pfam06160 4 LRKKIYKEIDELEER-KNELMNLpvqEELSKVKKlNLTGET---QEKFEEWRKKWDDIVtKSLPDIEELLFEA-----EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1113 AVQKNN---ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaAQQELRTKREQeVAEL 1189
Cdd:pfam06160 75 LNDKYRfkkAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRE------LRKTLLANRFS-YGPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1190 KKAIEEETKNHEAQIQEirqrhataLEELSEQ--LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVkaesehkrkkL 1267
Cdd:pfam06160 148 IDELEKQLAEIEEEFSQ--------FEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE----------L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1268 DAQVQELTAKVTEGER-----LRVELAEKANKLQNELDNVSSLLEEAEKKgiKFAKDAASLESQLQDTQELLQEETRQKL 1342
Cdd:pfam06160 210 PDQLEELKEGYREMEEegyalEHLNVDKEIQQLEEQLEENLALLENLELD--EAEEALEEIEERIDQLYDLLEKEVDAKK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1343 NLSSRIRQLEEEKNNLqeqqeeeeearknlEKQMLALQAQLAEAKKK---VDDDLGTIEGLEENKKKLLKDMESLSQRLE 1419
Cdd:pfam06160 288 YVEKNLPEIEDYLEHA--------------EEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERLE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 212450 1420 EKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1469
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
975-1224 |
1.52e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.61 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQLEKVTAE-AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS-QLAEEEEkaknlAKLKNKQEmmitdleeR 1052
Cdd:COG0497 151 AGLEELLEEYREAyRAWRALKKELEELRADEAERARELDLLRFQLEELEAaALQPGEE-----EELEEERR--------R 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELkiqlAKKEEELQAALARGDEeavqknnALKVIRELQAQIAE 1132
Cdd:COG0497 218 LSNAEKLREALQEALEALSGGEGGALDLLGQALRALERL----AEYDPSLAELAERLES-------ALIELEEAASELRR 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1133 LQEDLESEKASRNKAE---------KQK-RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETknheA 1202
Cdd:COG0497 287 YLDSLEFDPERLEEVEerlallrrlARKyGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAA----E 362
|
250 260
....*....|....*....|...
gi 212450 1203 QIQEIRQRHATALEE-LSEQLEQ 1224
Cdd:COG0497 363 KLSAARKKAAKKLEKaVTAELAD 385
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
975-1142 |
1.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQlekvTAEAKIKKMEEE--ILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEEr 1052
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQIEELKIQLAKKEEELQAAL------ARGDEEAVQK-----NN 1118
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASLeaeleaLQAREASLQAqlaqlEA 341
|
170 180
....*....|....*....|....
gi 212450 1119 ALKVIRELQAQIAELQEDLESEKA 1142
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARE 365
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1247-1462 |
1.57e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1247 ACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQ 1326
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1327 LQDTQELLQEETRQKLNLSSRIRQLE--------EEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTie 1398
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1399 gLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKK 1462
Cdd:COG3883 159 -LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
862-1277 |
1.64e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.86 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 862 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFaeaeemRARLAAKKQELEEilhdlesrv 941
Cdd:pfam15818 14 EELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVF------KKQLQMKMCALEE--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 942 eeeeernqilqnEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEI---LLLEDQNSKFLKEkklMEDRI 1018
Cdd:pfam15818 79 ------------EKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLqlhLLAKEDHHKQLNE---IEKYY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1019 AECTSQLA---EEEEKA-----------KNLAKLKNKQEMMITDLEERLKK-----------------EEKT-----RQE 1062
Cdd:pfam15818 144 ATITGQFGlvkENHGKLeqnvqeaiqlnKRLSALNKKQESEICSLKKELKKvtsdlikskvtcqykmgEENInltikEQK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1063 LEKAKRKLDGEtTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRElQAQIAELQEDLESEKA 1142
Cdd:pfam15818 224 FQELQERLNME-LELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQREKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1143 SRNKA---------EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHAt 1213
Cdd:pfam15818 302 KENEEkflnlqnehEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENS- 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1214 alEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAK 1277
Cdd:pfam15818 381 --EMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQVLEKSFK 442
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
856-1335 |
1.80e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLAAKKQELEE 932
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 933 IlHDLESRVEEEEERNqilqnekKKMQGHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK 1011
Cdd:pfam05557 199 I-PELEKELERLREHN-------KHLNENIENKLLLKEEVEDLKRKLeREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1012 KLMEDRIAECTSQLAEEEEKAKNLAKLKNkqemmiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEEL 1091
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQLQQREIVLKEEN------SSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1092 --KIQLAKKEEE-LQAALARGDEEAVQKN---NALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1165
Cdd:pfam05557 345 qrRVLLLTKERDgYRAILESYDKELTMSNyspQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1166 eDTLDTTAAQQELRTKREqEVAELKKAIEEetknHEAQIQEIRQRHatalEELSEQLEqakrfkanleknKQGLESDNKE 1245
Cdd:pfam05557 425 -QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQK----NELEMELE------------RRCLQGDYDP 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1246 LACEVKVLQQVKAeSEHKRKKldAQVQELTAKVTEGERLRVELAEKANKLQNELDnvSSLLEEAEKKGIKFAKDAASLES 1325
Cdd:pfam05557 483 KKTKVLHLSMNPA-AEAYQQR--KNQLEKLQAEIERLKRLLKKLEDDLEQVLRLP--ETTSTMNFKEVLDLRKELESAEL 557
|
490
....*....|
gi 212450 1326 QLQDTQELLQ 1335
Cdd:pfam05557 558 KNQRLKEVFQ 567
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1539-1750 |
1.84e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1539 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamKAQferdlQARDEQNEEKKrmlvkQVRELEAELEDE 1618
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK----------QAE-----QAAKQAEEKQK-----QAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1619 RKQRALAVAAKKKMEmdlkdlegqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKGLEAE 1698
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 212450 1699 ILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1750
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1635-1866 |
1.96e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1635 DLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLK-GLEAEILQLQEEFAASERAR 1713
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQpGEEEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1714 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQK 1792
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLEF 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1793 SENARQQLE-RQN--------------------KELKAKLQELEGSvkskfKATISTLEAKIAQLEEQLEQEAKE----- 1846
Cdd:COG0497 294 DPERLEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaar 368
|
250 260
....*....|....*....|
gi 212450 1847 RAAANKLVRRTEKKLKEVFM 1866
Cdd:COG0497 369 KKAAKKLEKAVTAELADLGM 388
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1124-1312 |
2.01e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1124 RELQAQIAELQEdLESEKAsrnKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelKKAIEEETKNHEAQ 1203
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELA------ALEARLEAAKTE-----LEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1204 IQEIRQRhataLEELSEQLEQAKRFK--ANLEKNKQGLESDNKELAcevKVLQQVKAESEHKRKKLDAQVQELTAKVTEG 1281
Cdd:COG1579 68 IEEVEAR----IKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 212450 1282 ERLRVELAEKANKLQNELDNVSSLLEEAEKK 1312
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
854-1301 |
2.09e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 854 LLQVTRQEEELQAKDEELMKVKEKQTKVEAEL-----------EEMERKHQQLLEEKNILAEqlqAETELFAEAEEMRAR 922
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAGTLLHF 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 923 LAAKKQELE---------EILH--DLESRVEEEEERNQI------LQNEKKKMQGHIQDLEEQLDEEEGARQKLQlekvT 985
Cdd:pfam12128 540 LRKEAPDWEqsigkvispELLHrtDLDPEVWDGSVGGELnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQ----S 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 986 AEAKIKKMEEEILLLedqNSKFLKEKKLMEDriAECTSQLAEEEEKAKNLAKlKNKQEMMITDLEERLKKEEKTRQELEK 1065
Cdd:pfam12128 616 AREKQAAAEEQLVQA---NGELEKASREETF--ARTALKNARLDLRRLFDEK-QSEKDKKNKALAERKDSANERLNSLEA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1066 AKRKLDgetTDLQDQIAELQAQIEELKIQLAKK----EEELQAALARGDEEAVQKNNALKvirelqAQIAELQEDLESEK 1141
Cdd:pfam12128 690 QLKQLD---KKHQAWLEEQKEQKREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDL 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1142 ASRNKAEKQKRDLSEELEALKTELEDTldttaaqqelrTKREQEVAELKKAIEE----ETKNHEAQIQEIRQRHATALEE 1217
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQ 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1218 LSEQLEQAKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEH-KRKKLDAQVQELTAKVTE----GERLRVELAEKA 1292
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQVRLSEN---LRGLRCEMSKlATLKEDANSEQAQGSIGErlaqLEDLKLKRDYLS 906
|
....*....
gi 212450 1293 NKLQNELDN 1301
Cdd:pfam12128 907 ESVKKYVEH 915
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1043-1177 |
2.27e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.61 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1043 EMMITDLEERLKKE--EKTRQELEKAKRKLDGETTDLQD------------QIAELQAQIEELKIQLAKKEEELQAALAR 1108
Cdd:COG3524 164 EELVNQLSERAREDavRFAEEEVERAEERLRDAREALLAfrnrngildpeaTAEALLQLIATLEGQLAELEAELAALRSY 243
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1109 GDEEAVQknnalkvIRELQAQIAELQEDLESEKA--SRNKAEKQKRDLSEELEALKTEL---EDTLDTTAAQQE 1177
Cdd:COG3524 244 LSPNSPQ-------VRQLRRRIAALEKQIAAERArlTGASGGDSLASLLAEYERLELERefaEKAYTSALAALE 310
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1691-1850 |
2.71e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1691 KLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLnerfr 1770
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1771 KTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEG---SVKSKFKATISTLEAKIAQLEEQLEQEAKER 1847
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAelaELEAELEEKKAELDEELAELEAELEELEAER 165
|
...
gi 212450 1848 AAA 1850
Cdd:COG1579 166 EEL 168
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1086-1204 |
2.74e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 46.23 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1086 AQIEELKIQLAKKEEELQAALARGDEEAVQKnnalkvIRELQAQIAELQEDLESEKAsRNKAEKQkrdLSEELEALKTEL 1165
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 212450 1166 EDTLDTTAAQQELRTKREQEVAELKKAIEEE-TKNHEAQI 1204
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAEV 520
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1539-1677 |
2.84e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 45.05 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1539 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQ-NEEKKRMLVKQVRELEAELED 1617
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1618 ERKqrALAVAAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1677
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
804-1392 |
2.86e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 804 QAVCRGYLARKAFAKKQQQLSALKILQRncAAYLKLrhwQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEA 883
Cdd:PRK10246 261 RRQQALQQALAAEEKAQPQLAALSLAQP--ARQLRP---HWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 884 eleemeRKHQQLLEEKNILAEQLQAETE-------------LFAEAEEMRARLAAKKQELEEILHDLES----------- 939
Cdd:PRK10246 336 ------KQSAELQAQQQSLNTWLAEHDRfrqwnnelagwraQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltad 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 940 ---RVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEillLEDQNSKFLKEKKL--M 1014
Cdd:PRK10246 410 evaAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQR---YKEKTQQLADVKTIceQ 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 EDRIAECTSQLAeeeekaknlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQIEEL 1091
Cdd:PRK10246 487 EARIKDLEAQRA----------QLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDAlekEVKKLGEEGAALRGQLDAL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1092 KIQLAKKEEELQAALArgDEEAVQKN-----NALKVIRELQAQIA---------ELQEDLESEK----ASRNKAEKQKRD 1153
Cdd:PRK10246 557 TKQLQRDESEAQSLRQ--EEQALTQQwqavcASLNITLQPQDDIQpwldaqeehERQLRLLSQRhelqGQIAAHNQQIIQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1154 LSEELEALKTELEDTLDTTA-------AQQELRTKREQEVAELKKaieeetknHEAQIQEIRQRHAtALEELSEQLEQAK 1226
Cdd:PRK10246 635 YQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSWQQ--------RQNELTALQNRIQ-QLTPLLETLPQSD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1227 RFKANLE----KNKQGLESDNKELACEVKVLQQvkAESEHKRKKLDAQVQ---ELTAKVTEG----------ERLRVELA 1289
Cdd:PRK10246 706 DLPHSEEtvalDNWRQVHEQCLSLHSQLQTLQQ--QDVLEAQRLQKAQAQfdtALQASVFDDqqaflaalldEETLTQLE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1290 EKANKLQNELDNVSSLLEEAEK----------KGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlq 1359
Cdd:PRK10246 784 QLKQNLENQRQQAQTLVTQTAQalaqhqqhrpDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR---- 859
|
650 660 670
....*....|....*....|....*....|...
gi 212450 1360 eqqeeeeearknleKQMLALQAQLAEAKKKVDD 1392
Cdd:PRK10246 860 --------------QQQQALMQQIAQATQQVED 878
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
990-1312 |
3.25e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 990 IKKMEEEILLLE-------DQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMiTDLEERLKKEEKTRQE 1062
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEIL-EEQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1063 LEKA-KRKLDGETTDLQDQIAELQAQIEELKIQLA--KKEEELQAALARgdEEAVQKNNalkvIRELQAQIAELQEDLes 1139
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKLEK--ERSLLDAS----LRELESKFIVAQEDV-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1140 EKASRNKAEKqkrdLSEELEalktELEDTLDTTAAQQelrtkrEQEVAELKkaieeetknheaQIQEIRQRhataLEELS 1219
Cdd:PLN02939 288 SKLSPLQYDC----WWEKVE----NLQDLLDRATNQV------EKAALVLD------------QNQDLRDK----VDKLE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1220 EQLEQAKRFKANLEKnkqglesdnkelaceVKVLQQ-VKAESEHkrkkLDAQVQELTAKVTEGERLRVELAekanklqne 1298
Cdd:PLN02939 338 ASLKEANVSKFSSYK---------------VELLQQkLKLLEER----LQASDHEIHSYIQLYQESIKEFQ--------- 389
|
330
....*....|....
gi 212450 1299 lDNVSSLLEEAEKK 1312
Cdd:PLN02939 390 -DTLSKLKEESKKR 402
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1610-1856 |
3.25e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1610 ELEAELeDERKQRALAVAAKKKMEMDLK---DLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1687 ES------EKKLKGLEAEILQLQEEFA-----------ASERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1745
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAeynsqlvslqtQPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1746 ARIAQleeeleeeqsnMELLNErFRKTTLQVDTLNSELaGERSAAQKSENArQQLERQnkelkakLQELEGSVKSKfkat 1825
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQ-------LQLLQEAINSK---- 253
|
250 260 270
....*....|....*....|....*....|.
gi 212450 1826 isTLEAKIAQLEEQLEQEAKERAAANKLVRR 1856
Cdd:PRK11281 254 --RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1539-1940 |
3.25e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1539 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQARDEQNEEKKRMLVKQVRELEAELEDE 1618
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1619 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQlrklqaqmkdyqreleearASRDEIFAQSKESEKKLKGLEA- 1697
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-------------------TSIREISCQQHTLTQHIHTLQQq 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1698 -EILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQv 1776
Cdd:TIGR00618 388 kTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1777 dtlnsELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEqLEQEAKERAAANKLVRR 1856
Cdd:TIGR00618 467 -----SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1857 TEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeeeATRANASRRKLQRELDDATEANEGLSREVSTLKN 1936
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
....
gi 212450 1937 RLRR 1940
Cdd:TIGR00618 613 EQHA 616
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1009-1392 |
3.51e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 45.82 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1009 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE------EKTRQELEKAKRKLDGETTDLQDQIA 1082
Cdd:pfam13166 89 EESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDEcwkkikRKKNSALSEALNGFKYEANFKSRLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1083 ELQAQIEELKIQLAkkEEELQAALARGDEEAVQKnNALKVIRELQAQIAELQEDLESEKASRNKA--EKQKR-DLSEELE 1159
Cdd:pfam13166 169 EIEKDNFNAGVLLS--DEDRKAALATVFSDNKPE-IAPLTFNVIDFDALEKAEILIQKVIGKSSAieELIKNpDLADWVE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1160 ALKTELEDTLDTTA-AQQELRTKReqeVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLeqakrfkanleknKQG 1238
Cdd:pfam13166 246 QGLELHKAHLDTCPfCGQPLPAER---KAALEAHFDDEFTEFQNRLQKLIEKVESAISSLLAQL-------------PAV 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1239 LESDNKELACEVKVlQQVKAESEHKRKKLDAQVQELTAKVTEGERlRVELAEKANKLQNELDNVSSLLEEAEK---KGIK 1315
Cdd:pfam13166 310 SDLASLLSAFELDV-EDIESEAEVLNSQLDGLRRALEAKRKDPFK-SIELDSVDAKIESINDLVASINELIAKhneITDN 387
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1316 FAKDAASLESQLQdtQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1392
Cdd:pfam13166 388 FEEEKNKAKKKLR--LHLVEEFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRDHKPGADE 462
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
861-1195 |
3.54e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLleEKNILA-------------EQLQAETELFAEAEEMRAR---LA 924
Cdd:pfam06160 99 EEDIKQILEELDELLESEEKNREEVEELKDKYREL--RKTLLAnrfsygpaideleKQLAEIEEEFSQFEELTESgdyLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 925 AKK--QELEEILHDLESRVEEEEERNQILQNEKKKmqghiqdleeqldeeegarqklQLEKVtaEAKIKKMEEEILLLED 1002
Cdd:pfam06160 177 AREvlEKLEEETDALEELMEDIPPLYEELKTELPD----------------------QLEEL--KEGYREMEEEGYALEH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1003 QNskFLKEKKLMEDRIAECTSQLA--EEEEKAKNLAKLKNKqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:pfam06160 233 LN--VDKEIQQLEEQLEENLALLEnlELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELK--IQLAKKEEELQAALArgdeeavqknnalKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1158
Cdd:pfam06160 307 NKELKEELERVQqsYTLNENELERVRGLE-------------KQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQL 373
|
330 340 350
....*....|....*....|....*....|....*....
gi 212450 1159 EALKTELEDTLDTTAA--QQELRTKreQEVAELKKAIEE 1195
Cdd:pfam06160 374 EEIEEEQEEFKESLQSlrKDELEAR--EKLDEFKLELRE 410
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1075-1246 |
3.79e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 43.38 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1075 TDLQDQIAELQAQIEELKIQLakkeEELQAALARGDEEAVQKNNALkvIRELQAQIAELQEDLESEKASRNKAEKQKRDL 1154
Cdd:pfam08614 10 NRLLDRTALLEAENAKLQSEP----ESVLPSTSSSKLSKASPQSAS--IQSLEQLLAQLREELAELYRSRGELAQRLVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1155 SEELEALKTELEdtldttAAQQELRtKREQEVAELkkaiEEETKNHEAQIQEIRQRHATALEE---LSEQLEQAkrfkan 1231
Cdd:pfam08614 84 NEELQELEKKLR------EDERRLA-ALEAERAQL----EEKLKDREEELREKRKLNQDLQDElvaLQLQLNMA------ 146
|
170
....*....|....*
gi 212450 1232 lEKNKQGLESDNKEL 1246
Cdd:pfam08614 147 -EEKLRKLEKENREL 160
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1460-1938 |
3.93e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1460 QKKFDQMLAEEKNISAryaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQnkQLRADMEDLMSSKDDVGKNVHE 1539
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD--QITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1540 LEKSKRTLeQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDER 1619
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1620 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEarasrdEIFAQSKESEKKLKGLEAEI 1699
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL------DGFERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1700 LQLQEEFAaserarRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMellneRFRKTTLQVDTL 1779
Cdd:TIGR00606 400 IERQEDEA------KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL-----KFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1780 NSELAGERSAAQKSENARQQLERQNKELKAKLQElEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1859
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKE-VKSLQNE-KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1860 KLKEVFmqvEDERRHADQYKEQMEKANARmKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:TIGR00606 547 KDEQIR---KIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1350-1896 |
4.44e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.12 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1350 QLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEenkKKLLKDMESLSQRLEEkAMAYDKLE 1429
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLE---KREAEAEEALREQAEL-NRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1430 KTKNRLQQELDDLMVDLdhqRQIVSNLekkqkkfdqmlaeeKNISARYAEERDRAEAEAREKETKalslaraleealeak 1509
Cdd:pfam05557 86 EALNKKLNEKESQLADA---REVISCL--------------KNELSELRRQIQRAELELQSTNSE--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1510 eeferqnkqlradMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRT---QLEELEDELQATEDAKLRLEvNMQAMKAQF 1586
Cdd:pfam05557 134 -------------LEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVK-NSKSELARI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1587 ---ERDLQARDEQNE------EKKRMLVKQVRELEAELEDERKQRALAVA---AKKKMEMDLK----------------- 1637
Cdd:pfam05557 200 pelEKELERLREHNKhlneniENKLLLKEEVEDLKRKLEREEKYREEAATlelEKEKLEQELQswvklaqdtglnlrspe 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1638 DLEGQI------EAANKARDEAI-KQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKGLEAEILQLQEEFAASE 1710
Cdd:pfam05557 280 DLSRRIeqlqqrEIVLKEENSSLtSSARQLEKARRELEQELAQYLK-------KIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1711 RARRHAEQERDELADEIANSASGKSaLLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAA 1790
Cdd:pfam05557 353 KERDGYRAILESYDKELTMSNYSPQ-LLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1791 QKSENARQQLERQnkELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAKeraaanklvrrtekKLKEVFMQVED 1870
Cdd:pfam05557 432 SLADPSYSKEEVD--SLRRKLETLELER-QRLREQKNELEMELERRCLQGDYDPK--------------KTKVLHLSMNP 494
|
570 580
....*....|....*....|....*.
gi 212450 1871 ERRHADQYKEQMEKANARMKQLKRQL 1896
Cdd:pfam05557 495 AAEAYQQRKNQLEKLQAEIERLKRLL 520
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
876-1152 |
4.61e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 876 EKQTKVEAELEEMERKHQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEK 955
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRD---ELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 956 KKMQGHIQDLEEQLDEEEGARQKLQlEKVTAEAKIKKMEEEILLLED--QNSKFLKEKklmEDRIAECTSQLAEEEEKAK 1033
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELA-ELNKAGGSIDKLRKEIERLEWrqQTEVLSPEE---EKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1034 NLAKLKNKqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEA 1113
Cdd:COG1340 154 KALEKNEK----LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 212450 1114 VQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKR 1152
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1123-1381 |
4.74e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1123 IRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieEETKNHEA 1202
Cdd:COG1340 10 LEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELK----EERDELNE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1203 QIQEIRQRhATALEELSEQLEQAKRFKANLEKNKQGLE----------SDNKELACEVKVLQQ---VKAESEHKRKKLDA 1269
Cdd:COG1340 86 KLNELREE-LDELRKELAELNKAGGSIDKLRKEIERLEwrqqtevlspEEEKELVEKIKELEKeleKAKKALEKNEKLKE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1270 QVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEkkgiKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIR 1349
Cdd:COG1340 165 LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD----ELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260 270
....*....|....*....|....*....|..
gi 212450 1350 QLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1381
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
856-1630 |
4.87e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERK----HQ--QLLEEknilAEQLQAETELFAE-AEEMRARLAAKKQ 928
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyQQavQALEK----ARALCGLPDLTPEnAEDYLAAFRAKEQ 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 929 ELEEILHDLESRVEEEEE-RNQILQNEK--KKMQGHIQD----LEEQLDEEEGARQKLQLEKVTA-EAKIKKMEEEIlll 1000
Cdd:COG3096 452 QATEEVLELEQKLSVADAaRRQFEKAYElvCKIAGEVERsqawQTARELLRRYRSQQALAQRLQQlRAQLAELEQRL--- 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1001 edqnskflkekklmedriaectSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:COG3096 529 ----------------------RQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQlAKKEEELQAALARGDEeavQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1160
Cdd:COG3096 587 LEQLRARIKELAAR-APAWLAAQDALERLRE---QSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1161 LkteledTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR---QRHATALEELS---EQLEQAKRFKANL-- 1232
Cdd:COG3096 663 L------SQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYFSALygpARHAIVVPDLSavkEQLAGLEDCPEDLyl 736
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1233 -EKNKQG-----LESDNKELACEVKVLQQVKAESEHK------RKKLDAQVQELTAkvtEGERLRVELAEKA---NKLQN 1297
Cdd:COG3096 737 iEGDPDSfddsvFDAEELEDAVVVKLSDRQWRYSRFPevplfgRAAREKRLEELRA---ERDELAEQYAKASfdvQKLQR 813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1298 ELDNVSSLLeeAEKKGIKFAKDAAslesqlqdtqELLQEetrqklnLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQML 1377
Cdd:COG3096 814 LHQAFSQFV--GGHLAVAFAPDPE----------AELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1378 ALQAQLAEAKKKVDDDLGT-IEGLEENKKKLLKDMESLSQ------RLEEKAMA-------YDKLEKTKNRLQQELDDLM 1443
Cdd:COG3096 875 LLNKLLPQANLLADETLADrLEELREELDAAQEAQAFIQQhgkalaQLEPLVAVlqsdpeqFEQLQADYLQAKEQQRRLK 954
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1444 VDLDHQRQIVSNLEK-KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKAlslaraleealeakeefeRQNKQLRAD 1522
Cdd:COG3096 955 QQIFALSEVVQRRPHfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQL------------------RQAQAQYSQ 1016
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1523 MEDLMSSkddvgknvheLEKSKRTLEQQVEEMRTQLEELedELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR 1602
Cdd:COG3096 1017 YNQVLAS----------LKSSRDAKQQTLQELEQELEEL--GVQADAEAEERARIRRDELHEELSQNRSRRSQLEKQLTR 1084
|
810 820 830
....*....|....*....|....*....|....
gi 212450 1603 M------LVKQVRELEAELEDERKQralAVAAKK 1630
Cdd:COG3096 1085 CeaemdsLQKRLRKAERDYKQEREQ---VVQAKA 1115
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1088-1226 |
4.93e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1088 IEELKIQLAKKEEELQAalargdEEAVQKNNALKVIRELQAQ--IAELQEDLESE-KASRNKAEKQKRDLSEELEALKTE 1164
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1165 LEDTldttaaqqelrTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSE----QLEQAK 1226
Cdd:PRK12704 102 LELL-----------EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEAK 156
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1607-1797 |
5.06e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1607 QVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1686
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1687 ESEKKLKGLEA--------------------------EILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDE 1740
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1741 KRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENAR 1797
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1782-1894 |
5.17e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1782 ELAGERSAAQKSENARQ--QLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1859
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|....*
gi 212450 1860 KLKEvfmqVEDERRHADQYKEQMEkanaRMKQLKR 1894
Cdd:COG2433 477 LERE----LEEERERIEELKRKLE----RLKELWK 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1138-1387 |
5.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1138 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRT-KREQEVAELkkaiEEETKNHEAQIQEIRQRHATALE 1216
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEfRQKNGLVDL----SEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1217 ELSEQLEQAKRFKANLEKNKQGLESDNKElacevKVLQQVKAEsehkRKKLDAQVQELTAKVTEGERLRVELAEKANKLQ 1296
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQS-----PVIQQLRAQ----LAELEAELAELSARYTPNHPDVIALRAQIAALR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1297 NELDnvssllEEAEKKGIKFAKDAASLESQLQdtqeLLQEETRQKLNLSSRIRQLEEEKNNLQEQqeeeeeaRKNLEKQM 1376
Cdd:COG3206 305 AQLQ------QEAQRILASLEAELEALQAREA----SLQAQLAQLEARLAELPELEAELRRLERE-------VEVARELY 367
|
250
....*....|.
gi 212450 1377 LALQAQLAEAK 1387
Cdd:COG3206 368 ESLLQRLEEAR 378
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
988-1203 |
5.62e-04 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 43.83 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 988 AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAecTSQLAEEEEKAKNLAKLKnkqemmITDLEERLKKEEKTRQELEKAK 1067
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDDAPAELRELRQELA--ALQAKAEAAPKEILASLS------LEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1068 RKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV-IRELQAQIAELQEDLESEKASRNK 1146
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAeLAALKAQIDMLEQELLSNNNRQDL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1147 AEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKAIEEETKNHEAQ 1203
Cdd:pfam12795 182 LKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
811-1294 |
5.71e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.13 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 811 LARKAFAKKQQQLSALKILQRNCAAYlklrhwqwwrVFTKVKPllQVTRQEEELQAKD--EELMKVKEKQTKVEAELEEM 888
Cdd:pfam07111 201 LLRKQLSKTQEELEAQVTLVESLRKY----------VGEQVPP--EVHSQTWELERQEllDTMQHLQEDRADLQATVELL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 889 ERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQEL-----EEIL--------HDLESRVEEEEERNQILQ--- 952
Cdd:pfam07111 269 QVRVQSL---THMLALQEEELTRKIQPSDSLEPEFPKKCRSLlnrwrEKVFalmvqlkaQDLEHRDSVKQLRGQVAElqe 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 953 ------NEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIaecTSQLA 1026
Cdd:pfam07111 346 qvtsqsQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWL---ETTMT 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1027 EEEEKAKNLAKLKN------KQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEE 1100
Cdd:pfam07111 423 RVEQAVARIPSLSNrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAH 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1101 ELQAALARGDEEA-VQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELedtldttAAQQELR 1179
Cdd:pfam07111 503 LIQQEVGRAREQGeAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL-------TQQQEIY 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1180 TKREQE-VAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELAceVKVLQQVKA 1258
Cdd:pfam07111 576 GQALQEkVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEG--QRLARRVQE 653
|
490 500 510
....*....|....*....|....*....|....*.
gi 212450 1259 ESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1294
Cdd:pfam07111 654 LERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
984-1214 |
5.96e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 984 VTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKaknLAKLKNKQEMMITDLEERLKKEEKTRQEL 1063
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1064 EKAKRKL--DGETTD-----------------------LQDQIAELQAQIEELKIQLAKKEEELQAalargdeeavQKNN 1118
Cdd:COG3883 89 GERARALyrSGGSVSyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEA----------KLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1119 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETK 1198
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250
....*....|....*.
gi 212450 1199 NHEAQIQEIRQRHATA 1214
Cdd:COG3883 239 AAAAAASAAGAGAAGA 254
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1405-1864 |
6.36e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 44.68 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1405 KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQM-----LAEEKNISARYAE 1479
Cdd:pfam05622 3 SEAQEEKDELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLqkqleQLQEENFRLETAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1480 ERDRAEAEAREKETKALSLaraleealeakeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRTQLE 1559
Cdd:pfam05622 83 DDYRIKCEELEKEVLELQH----------------RNEELTSLAEEAQALKDEMDILRESSDKVKK-LEATVETYKKKLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1560 ELEDelqATEDAKLRLEVNMQAM--KAQFERDLQ---ARDEQNEEKKRmlvkQVRELEAELEDERKQralavaaKKKMEM 1634
Cdd:pfam05622 146 DLGD---LRRQVKLLEERNAEYMqrTLQLEEELKkanALRGQLETYKR----QVQELHGKLSEESKK-------ADKLEF 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1635 DLKDLEGQIEAANKARD----------EAIKQLRKLQAQmkdyQRELEEARASRDEIFAQSKESEKKLKGLE--AEILQL 1702
Cdd:pfam05622 212 EYKKLEEKLEALQKEKErliierdtlrETNEELRCAQLQ----QAELSQADALLSPSSDPGDNLAAEIMPAEirEKLIRL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1703 QEEFAASERARRHAEQERDELAdeiansasgkSALLDEKRRleariaqleeELEEEQSNMELLNERFRKTTLQVDTLNSE 1782
Cdd:pfam05622 288 QHENKMLRLGQEGSYRERLTEL----------QQLLEDANR----------RKNELETQNRLANQRILELQQQVEELQKA 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1783 LAGERSAAQKSENARQQLERQNKELK---AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1859
Cdd:pfam05622 348 LQEQGSKAEDSSLLKQKLEEHLEKLHeaqSELQKKKEQIEELEPKQDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVE 427
|
....*
gi 212450 1860 KLKEV 1864
Cdd:pfam05622 428 KAKSV 432
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1010-1392 |
6.59e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 44.63 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1010 EKKLMEDRIAECTSQLAEEEEkaknlAKLKNKQEMMIT---------DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1080
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEA-----AKAQVLEELESTkrlieelklNLERAQTEEAQAKQDSELAKLRVEEMEQGIADE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 I-AELQAQIEELKIQLAKKEEELQAAlaRGDEEAVQKNNALKVI-RELQAQIAElqedlESEKASRnKAEKQKRDLSEEL 1158
Cdd:pfam05701 118 AsVAAKAQLEVAKARHAAAVAELKSV--KEELESLRKEYASLVSeRDIAIKRAE-----EAVSASK-EIEKTVEELTIEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1159 EALKTELEdtldttAAQQELRTKREQEVAeLKKAIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKANLEKNKQG 1238
Cdd:pfam05701 190 IATKESLE------SAHAAHLEAEEHRIG-AALAREQDKLNWEKELKQAEEE----LQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1239 LESDNKELACEVkvlqqvkaesehkrkklDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA--EKKGIKF 1316
Cdd:pfam05701 259 LLDLKAELAAYM-----------------ESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAkdEVNCLRV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1317 AkdAASLESQLQDTQELLqEETRQKLNLSS-RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1392
Cdd:pfam05701 322 A--AASLRSELEKEKAEL-ASLRQREGMASiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEE 395
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1544-1698 |
6.59e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1544 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1617
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1618 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKg 1694
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 212450 1695 LEAE 1698
Cdd:PRK12704 184 EEAD 187
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1650-1815 |
6.81e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1650 RDEAIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkGLEAEILQLQEEFAASERARRHAEQERDELADEiAN 1729
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1730 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNErfrkttlQVDTLNSELAGERSAAQKSENARQQLERQ------ 1803
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 212450 1804 --NKELKAKLQELE 1815
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1019-1162 |
6.82e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1019 AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELqaqiEELKIQLAKK 1098
Cdd:PRK12705 35 AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL----DNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1099 EEELQAALARGDEEAVQKNNALKVIRELQAQ------IAELQEDLESEKASRNKAEKQKRDLSEELEALK 1162
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
813-1195 |
6.82e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 6.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 813 RKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVkpLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKH 892
Cdd:COG4717 159 RELEEELEELEAELAELQEELEELLEQLSLATEEELQDL--AEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 893 QQLLEEKNIlaEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEE 972
Cdd:COG4717 237 EAAALEERL--KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 973 EGARQKLQLEKVTAEAKIKKMEEEILLLEDQnskfLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1052
Cdd:COG4717 315 ELEEEELEELLAALGLPPDLSPEELLELLDR----IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1053 LKKEEktrqelekakrkldgettdlqdQIAELQAQIEELKIQLAKKEEELQAALARGDEEavqknnalkvirELQAQIAE 1132
Cdd:COG4717 391 LEQAE----------------------EYQELKEELEELEEQLEELLGELEELLEALDEE------------ELEEELEE 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1133 LQEDLESekasrnkAEKQKRDLSEELEALKTELEDTLDTTAAqQELRTKREQEVAELKKAIEE 1195
Cdd:COG4717 437 LEEELEE-------LEEELEELREELAELEAELEQLEEDGEL-AELLQELEELKAELRELAEE 491
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
984-1092 |
7.82e-04 |
|
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves repeated cycles of substrate binding and release. Hsp70 activity is ATP dependent. Hsp70 proteins are made up of two regions: the amino terminus is the ATPase domain and the carboxyl terminus is the substrate binding region.
Pssm-ID: 394970 [Multi-domain] Cd Length: 598 Bit Score: 44.56 E-value: 7.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 984 VTAEAKIKKMEEEILLledQNSKFLKEKKlmEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKtrQEL 1063
Cdd:pfam00012 480 VSAKDKGTGKEQEITI---EASEGLSDDE--IERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGD--KVP 552
|
90 100 110
....*....|....*....|....*....|....
gi 212450 1064 EKAKRKLDGETTDL-----QDQIAELQAQIEELK 1092
Cdd:pfam00012 553 EAEKSKVESAIEWLkdeleGDDKEEIEAKTEELA 586
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1636-1894 |
8.07e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1636 LKDLEGQIEAANKARDEAIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKGLEAEILQLQEEFAASERarRH 1715
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1716 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNERFRKTTLQVDTLNSELAGERS 1788
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1789 AAQKSENARQQLERQNKELKAKLQElegsVKSKFKATISTLEAKIAQLEEQLEQeakeraaanklVRRTEKKLKEVFMQV 1868
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQ----ARNERKKTLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 212450 1869 EDE-RRHADQYKEQMEKANARMKQLKR 1894
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1087-1255 |
8.28e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1087 QIEELKIQLAKKEEELQAALARGDEEavqknnaLKVIRELQAQIAELQEDLESEKASRNKAEKQKRDL-SEELEALKTEL 1165
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKE-------LELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1166 EDTLDTTAAQQELRTKREQEVAELKKAIEEETknheAQIQEIRqrhataleelsEQLEQAKRFkanLEKNKQGLESDNKE 1245
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLT----NKKSELN-----------TEIAEAEKK---LEQCRGFTFKEIEK 275
|
170
....*....|
gi 212450 1246 LACEVKVLQQ 1255
Cdd:smart00787 276 LKEQLKLLQS 285
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
988-1173 |
8.45e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 988 AKIKKMEEEILLLEDQ----NSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL 1063
Cdd:PHA02562 174 DKIRELNQQIQTLDMKidhiQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1064 EKAKRKLDGETTDLQDQIAELQ-----------------------AQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL 1120
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctqqisegpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1121 ---KVIRELQAQIAELQEDLESE-------KASRNKAEKQKRDLSEELEALKTELEDTLDTTA 1173
Cdd:PHA02562 334 eqsKKLLELKNKISTNKQSLITLvdkakkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
988-1168 |
8.82e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 43.47 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 988 AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAEcTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAK 1067
Cdd:PRK06669 2 PKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKE-KERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1068 RKLDGETTDLQDQIAELQAQIEELKIQLAK-KEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQEDLesekasRNK 1146
Cdd:PRK06669 81 EELLKKTDEASSIIEKLQMQIEREQEEWEEeLERLIEEAKAEGYEEGYEKGRE-----EGLEEVRELIEQL------NKI 149
|
170 180
....*....|....*....|..
gi 212450 1147 AEKQKRDLSEELEALKTELEDT 1168
Cdd:PRK06669 150 IEKLIKKREEILESSEEEIVEL 171
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1022-1198 |
8.89e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1022 TSQLAEEEEKAKNLAKLKNKQEmmitdleERLKKEEKT--RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1099
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEALLeaKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1100 EELQaalargdeeavQKNNALKvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldtTAAQQ--- 1176
Cdd:PRK12704 103 ELLE-----------KREEELE---KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE-------EAKEIlle 161
|
170 180
....*....|....*....|..
gi 212450 1177 ELRTKREQEVAELKKAIEEETK 1198
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIEEEAK 183
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
1010-1226 |
9.09e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1010 EKKLMEDRIAECTSQLAEE-EEKAKNLAKLKNKQEMMITDLEERLKK---EEKTRQELEKAKRKLDGETTDLQDQIAELQ 1085
Cdd:pfam13166 262 GQPLPAERKAALEAHFDDEfTEFQNRLQKLIEKVESAISSLLAQLPAvsdLASLLSAFELDVEDIESEAEVLNSQLDGLR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1086 AQIEELK------IQLAKKEEELQAALARGDE--EAVQKNNAlkVIRELQAQIAELQEDLESEKASRNKAEKQKrdLSEE 1157
Cdd:pfam13166 342 RALEAKRkdpfksIELDSVDAKIESINDLVASinELIAKHNE--ITDNFEEEKNKAKKKLRLHLVEEFKSEIDE--YKDK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1158 LEALKTELEDTLDTTAAQQELRTKREQEVAELkkaiEEETKNHEAQIQEIRQR-HATALEELSEQLEQAK 1226
Cdd:pfam13166 418 YAGLEKAINSLEKEIKNLEAEIKKLREEIKEL----EAQLRDHKPGADEINKLlKAFGFGELELSFNEEG 483
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1598-1861 |
9.43e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1598 EEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1677
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1678 RDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEE 1757
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1758 EQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLE 1837
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250 260
....*....|....*....|....
gi 212450 1838 EQLEQEAKERAAANKLVRRTEKKL 1861
Cdd:COG4372 270 EKDTEEEELEIAALELEALEEAAL 293
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1022-1184 |
9.47e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.57 E-value: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1022 TSQLAEEEEKAkNLAKLKNKQEmmitdleeRLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1101
Cdd:pfam00529 55 DYQAALDSAEA-QLAKAQAQVA--------RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1102 LQAALARGDEEAVQKNNALkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEAL--KTELEDTLDTTAAQQELR 1179
Cdd:pfam00529 126 LARRRVLAPIGGISRESLV----TAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELK 201
|
....*
gi 212450 1180 TKREQ 1184
Cdd:pfam00529 202 LAKLD 206
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1595-1718 |
9.51e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1595 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE------------AANKARDEAIKQLRKLQA 1662
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKkleekaqaaltkGNEELAREALAEKKSLEK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1663 QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEilqlQEEFAASERARRHAEQ 1718
Cdd:pfam04012 98 QAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAK----KNLLKARLKAAKAQEA 149
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1057-1333 |
9.82e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.53 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1057 EKTRQELEKAKRKLDgETTD----LQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAE 1132
Cdd:pfam04108 17 TDARSLLEELVVLLA-KIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1133 LQE-----------DLESEKASRNKAEKQKRDLSEELEALKTELeDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE 1201
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDL-KRFDDDLRDLQKELESLSSPSESISLIPTLLKELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1202 AQIQEIRQrHATALEELSEQLEQAKR-FKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTE 1280
Cdd:pfam04108 175 SLEEEMAS-LLESLTNHYDQCVTAVKlTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 212450 1281 GerlrVELAEKANKLQNELDNVSSLLEEAEKkgiKFAKDAASLESQLQDTQEL 1333
Cdd:pfam04108 254 L----LSALQLIAEIQSRLPEYLAALKEFEE---RWEEEKETIEDYLSELEDL 299
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1201-1437 |
9.88e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 9.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1201 EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELAcevkvlqqvkaeSEHKRKKLDAQVQELTAKVTE 1280
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD------------LSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1281 GERLRVELAEKANKLQNELDNVSSLLEEAEKKGIkfakdAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQE 1360
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPV-----IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1361 Q-QEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLeenkKKLLKDMESLSQRLEEKAMAYDKLEktkNRLQQ 1437
Cdd:COG3206 306 QlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL----PELEAELRRLEREVEVARELYESLL---QRLEE 376
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
982-1382 |
9.89e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 44.23 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 982 EKVTAEAKIKKMEEeillLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMIT------DLEERLKK 1055
Cdd:NF033838 109 EKSEAELTSKTKKE----LDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTyktlelEIAESDVE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1056 EEKTRQELEKAKRKldgETTDlQDQIAELQAQIEELKIQlAKKEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQE 1135
Cdd:NF033838 185 VKKAELELVKEEAK---EPRD-EEKIKQAKAKVESKKAE-ATRLEKIKTDREKAEEEAKRRADA-----KLKEAVEKNVA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1136 DLESEKASRnkaeKQKRDLSEEL--EALKTELEDTLDTTAAQQELRT---KREQEVAELKKAIEEETKNHEAQIQEIRQR 1210
Cdd:NF033838 255 TSEQDKPKR----RAKRGVLGEPatPDKKENDAKSSDSSVGEETLPSpslKPEKKVAEAEKKVEEAKKKAKDQKEEDRRN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1211 HATALEELSEqLEQAkrfkanleknkqglESDNKELACEVKVLQQVKAES--EHKRKKLDAQVQELTAKVTEGERL---R 1285
Cdd:NF033838 331 YPTNTYKTLE-LEIA--------------ESDVKVKEAELELVKEEAKEPrnEEKIKQAKAKVESKKAEATRLEKIktdR 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1286 VELAEKANKLQNELDNVSSLLEEA---------EKKGIKFAKDAASLESQLQDTQellqeetrqklnlssrirQLEEekn 1356
Cdd:NF033838 396 KKAEEEAKRKAAEEDKVKEKPAEQpqpapapqpEKPAPKPEKPAEQPKAEKPADQ------------------QAEE--- 454
|
410 420
....*....|....*....|....*.
gi 212450 1357 nlqeqqeeeEEARKNLEKQMLALQAQ 1382
Cdd:NF033838 455 ---------DYARRSEEEYNRLTQQQ 471
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1665-1863 |
1.10e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1665 KDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFaasERARRHAEQERDELADEIAnsasgksalldekrRL 1744
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEI---HKLRNEFEKELRERRNELQ--------------KL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1745 EARIAQLEeeleeeqsnmELLNERfrkttlqvdtlNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFK- 1823
Cdd:PRK12704 88 EKRLLQKE----------ENLDRK-----------LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELEr 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 212450 1824 -ATISTLEAKiAQLEEQLEQEAKERAAanKLVRRTEKKLKE 1863
Cdd:PRK12704 147 iSGLTAEEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1199-1428 |
1.12e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1199 NHEAQIQEIRQRHATaleelsEQLEQAKRFKANLEKnKQGLESDNKELacevKVLQQVKAESEHKrkkldAQVQELTAKV 1278
Cdd:PHA02562 180 NQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK-----AEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1279 TEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgIKFAKDAA---SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1355
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1356 NNLQEQQEEEEEARK-----------------NLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL 1418
Cdd:PHA02562 323 DELEEIMDEFNEQSKkllelknkistnkqsliTLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
250
....*....|
gi 212450 1419 EEKAMAYDKL 1428
Cdd:PHA02562 403 YHRGIVTDLL 412
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
846-954 |
1.13e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 846 RVFTKVKPLLQVTRQEEELQAKDEELmkVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAA 925
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 212450 926 KKQELEEILHDLESRVEEEEERNQILQNE 954
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1607-1894 |
1.15e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1607 QVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLR-------KLQAQMKDYQRELEEARASRD 1679
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKelreeaqELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1680 EIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEEQ 1759
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1760 SNMELLNErFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELegsvkskfKATISTLEAKIAQLEEQ 1839
Cdd:COG1340 161 KLKELRAE-LKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1840 LEQEAKEraaanklVRRTEKKLKEVFMQVEDERRHADQyKEQMEKANARMKQLKR 1894
Cdd:COG1340 232 IIELQKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1003-1833 |
1.24e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1003 QNSKFLKEKKLMEDRIAECTSQLAEEEekaknLAKLKNK-----QEMMITDLEERLKkeektrqeLEKAKRKLDGETTDL 1077
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKSELSKIYEDD-----IDALYNElssivKENAIDNTEDKAK--------LDDLKSKIDKEYDKI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1078 QDQiaelqaQIEELKIQLAKKEEelqaalargdeeavQKNNALKVIRELQAQI-AELQEDLESEKASRNKAEKQkrdLSE 1156
Cdd:TIGR01612 713 QNM------ETATVELHLSNIEN--------------KKNELLDIIVEIKKHIhGEINKDLNKILEDFKNKEKE---LSN 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1157 ELEALKTELEDTLDTTAAQQELRTKREQEVAeLKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK------- 1229
Cdd:TIGR01612 770 KINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddflnkv 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1230 ---ANLEKN-KQGLESDNKELAcevKVLQQVKAESEhkrkklDAQVQELTAKVTEGERLrveLAEKANKLQNELDNVSSL 1305
Cdd:TIGR01612 849 dkfINFENNcKEKIDSEHEQFA---ELTNKIKAEIS------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTL 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1306 LEEAEKkgIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlqeqQEEEEEARKNLEKQMLALQAQLAE 1385
Cdd:TIGR01612 917 KKVDEY--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKD----KFDNTLIDKINELDKAFKDASLND 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1386 AKKKVDDDLGTIEGLEENKKKLLKDMesLSQRLEEKamaydklEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQ 1465
Cdd:TIGR01612 991 YEAKNNELIKYFNDLKANLGKNKENM--LYHQFDEK-------EKATNDIEQKIEDA-------NKNIPNIEIAIHTSIY 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1466 MLAEE------KNISARYAEERDRAEA------EAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDV 1533
Cdd:TIGR01612 1055 NIIDEiekeigKNIELLNKEILEEAEInitnfnEIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKI 1127
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1534 GKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFERDLQARDEQNEekkrmLVKQVRE 1610
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAE 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1611 LEAELEDERKQRALAVAAKKKMEmdlKDLEGQIEAANKARDEAIKQlrkLQAQMKDYqreleearasrDEIFAQSKESEK 1690
Cdd:TIGR01612 1202 IEKDKTSLEEVKGINLSYGKNLG---KLFLEKIDEEKKKSEHMIKA---MEAYIEDL-----------DEIKEKSPEIEN 1264
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1691 KLkGLEAEILQLQEEFAAS-ERARRH--AEQERDELADEIANSA-------SGKSALLDEKRRLEARIAQleeeleeEQS 1760
Cdd:TIGR01612 1265 EM-GIEMDIKAEMETFNIShDDDKDHhiISKKHDENISDIREKSlkiiedfSEESDINDIKKELQKNLLD-------AQK 1336
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1761 NMELLNERFRKTTLQVDTLnsELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKS-KFKATISTLEAKI 1833
Cdd:TIGR01612 1337 HNSDINLYLNEIANIYNIL--KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKiKDDINLEECKSKI 1408
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1791-1981 |
1.26e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1791 QKSENARQQLERQNKELKAKLQELEGSVkSKFKA---------TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKL 1861
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1862 KEVFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateaneglsrevstLKNRLRRG 1941
Cdd:COG3206 250 GSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAA--------------LRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 212450 1942 GPITFSSSRSGRRQLHIEGASLELSDDDAESKGSDVNEAQ 1981
Cdd:COG3206 311 AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE 350
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
976-1220 |
1.28e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 43.63 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 976 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKE--KKLMEDRIAECTSQLAEEEEKAKNlaklknkqemmITDLEERL 1053
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSS-----------LKELLTQL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1054 KKEEKTRQELEKAKRKLdgetTDLQDQIaelQAQIEELKIQLAKKEEElqaalarGDEEAVQKNNALKVIRELQAQIAEL 1133
Cdd:COG5391 375 QDEIKSRESLILTDSNL----EKLTDQN---LEDVEELSRSLRKNSSQ-------RAVVSQQPEGLTSFSKLSYKLRDFV 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1134 QEDleSEKASRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHAT 1213
Cdd:COG5391 441 QEK--SRSKSIESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKS 516
|
....*..
gi 212450 1214 ALEELSE 1220
Cdd:COG5391 517 VKEQLDR 523
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1536-1864 |
1.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1536 NVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkrmlvkqVRELEAEL 1615
Cdd:COG4372 39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--------LESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1616 EDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGL 1695
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1696 EAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQ 1775
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1776 VDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVR 1855
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
....*....
gi 212450 1856 RTEKKLKEV 1864
Cdd:COG4372 351 LDNDVLELL 359
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1517-1736 |
1.42e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1517 KQLRADMEDLMSSKDDVGKnvhELEKSKrtleQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERdlQARDEQ 1596
Cdd:COG3883 26 SELQAELEAAQAELDALQA---ELEELN----EEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE--RARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1597 NEEKKRMLVKQVreLEAELEDERKQRALAV-----AAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL 1671
Cdd:COG3883 97 RSGGSVSYLDVL--LGSESFSDFLDRLSALskiadADADLLE-ELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1672 EEARASRDEIFAQSKESEKKlkgLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSA 1736
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAA---AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1081-1233 |
1.59e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQAQIEELKIQLAKkeeeLQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1160
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1161 LKTELED------TLDTT-AAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLE 1233
Cdd:pfam00529 129 RRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1425-1867 |
1.59e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1425 YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeEKNISARYAEERDRAEAEAREKETKALsLARALEE 1504
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1505 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1584
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1585 QFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQM 1664
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1665 KDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1744
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1745 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKA 1824
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 212450 1825 TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQ 1867
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1047-1283 |
1.63e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1047 TDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE----EELQAALARGDEEAVQ---KNNA 1119
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQErllaAQLDAAFRQGEHTGLQlilSGEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1120 LKVIRELQAQIAEL----QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1195
Cdd:PRK11637 151 SQRGERILAYFGYLnqarQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1196 EtknhEAQIQEIRQRHAtaleELSEQLEQAKR-FKANLEKnkqglesdnkelacEVKVLQQVKAesehkrKKLDAQVQEL 1274
Cdd:PRK11637 231 D----QQQLSELRANES----RLRDSIARAEReAKARAER--------------EAREAARVRD------KQKQAKRKGS 282
|
....*....
gi 212450 1275 TAKVTEGER 1283
Cdd:PRK11637 283 TYKPTESER 291
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1027-1298 |
1.71e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1027 EEEEKAKNLAKLKNKQEmmitdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1106
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1107 ARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA-----SRNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRTK 1181
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKA------AQQAANAEAEEEVDPKKAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1182 ReqevAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKqgLESDNKELAcevkvlqqVKAESE 1261
Cdd:PRK05035 588 R----AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPE--EPVDPRKAA--------VAAAIA 653
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 212450 1262 HKRKKLDAQVQELTAKVTEGERLRVELAE-----KANKLQNE 1298
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1558-1938 |
1.76e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1558 LEELEDELQATEDAKLRLEvnmqamKAQFErDLQARdeQNEEKKRMLVKQVRE---------LEAELEDERKQRALAVAA 1628
Cdd:pfam05701 69 LEELESTKRLIEELKLNLE------RAQTE-EAQAK--QDSELAKLRVEEMEQgiadeasvaAKAQLEVAKARHAAAVAE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1629 KKKMEMDLKDLEGQIEAANKARDEAIKQLRklqaqmkdyqreleearasrdEIFAQSKESEKKLKGLEAEILQLQEEFAA 1708
Cdd:pfam05701 140 LKSVKEELESLRKEYASLVSERDIAIKRAE---------------------EAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1709 SERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMELL-NERFRKTTLQVDTLNSE 1782
Cdd:pfam05701 199 AHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASALLlDLKAELAAYMESKLKEE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1783 LAGERSAAQKSENARQQLERQNKELkaklQELEGSVKsKFKATISTLEAKIAQLEEQLEQEAKERAAanklVRRTEKKLK 1862
Cdd:pfam05701 278 ADGEGNEKKTSTSIQAALASAKKEL----EEVKANIE-KAKDEVNCLRVAAASLRSELEKEKAELAS----LRQREGMAS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1863 EVFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1938
Cdd:pfam05701 349 IAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRL 428
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1028-1626 |
1.85e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 43.20 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1028 EEEKAKNLAKLKNKQEMMITDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQ 1103
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1104 AALARgdEEAVQKNNALKVIRELQAQIAEL--QEDLESEKASRnkaeKQKRDLSEELEALKTELEDTLDTTAAQQELRTK 1181
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWELerQELLDTMQHLQ----EDRADLQATVELLQVRVQSLTHMLALQEEELTR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1182 REQEVAELKKaieEETKNHEAQIQEIRQRHATALEELSEQ----LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1257
Cdd:pfam07111 289 KIQPSDSLEP---EFPKKCRSLLNRWREKVFALMVQLKAQdlehRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1258 AESEhkrkkldaqVQELTAKVTEGERLRVELAEKANKLQneldnvsslLEEAEKKgIKFAKDA-ASLESQLQDTQELLQE 1336
Cdd:pfam07111 366 AEVE---------VERMSAKGLQMELSRAQEARRRQQQQ---------TASAEEQ-LKFVVNAmSSTQIWLETTMTRVEQ 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1337 ETRQKLNLSSRIRQLEEEKNNLqeqqeEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGT-IEGLEENKKKLLKDMEsLS 1415
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKVHTI-----KGLMARKVALAQLRQESCPPPPPAPPVDADLSLeLEQLREERNRLDAELQ-LS 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1416 QRL--EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfdqmlaeekniSARYAEERDRAEAEAREKET 1493
Cdd:pfam07111 501 AHLiqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLE------------VARQGQQESTEEAASLRQEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1494 KALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELEDELQATEDAKL 1573
Cdd:pfam07111 569 TQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQE-KERNQELRRLQDEARKEEGQRL 647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 212450 1574 rlevnmqamkaqferdlqARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1626
Cdd:pfam07111 648 ------------------ARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
985-1106 |
1.99e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 42.72 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 985 TAEAKIKKMEEEILLLEDQnskflkekklmedrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELE 1064
Cdd:smart00435 274 THEKSMEKLQEKIKALKYQ--------------LKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEE 339
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 212450 1065 KAKRkldgettdlqdQIAELQAQIEELKIQLAKKEEELQAAL 1106
Cdd:smart00435 340 KKKK-----------QIERLEERIEKLEVQATDKEENKTVAL 370
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1077-1315 |
2.00e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1077 LQDQIAELQAQIEELKIQLAKKEEELqaalargdeeAVQKNNaLKVIRELQAQ-IAELQEDLESEKASRNKAEKQKRDLS 1155
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQI----------KTYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1156 EELEALKTELEdtlDTTAAQQELRTKREQ---EVAELKKAIEEETKNHE------------AQIQEIRQRHA-------- 1212
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAAAKiksKIEQFQKVIKMYEKGGVcptctqqisegpDRITKIKDKLKelqhslek 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1213 --TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEhkrkKLDAQVqelTAKVTEGERLRVELAE 1290
Cdd:PHA02562 318 ldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE----ELQAEF---VDNAEELAKLQDELDK 390
|
250 260 270
....*....|....*....|....*....|.
gi 212450 1291 KANKLQN------ELDNVSSLLEEAekkGIK 1315
Cdd:PHA02562 391 IVKTKSElvkekyHRGIVTDLLKDS---GIK 418
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1243-1677 |
2.02e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1243 NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtEGERLRVELAEKANKLqneldnvsslleeaekkgikfakdaas 1322
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKEEKAREV--------------------------- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1323 lesqlqdtqellqeETRQKLNLSSRIRQLEEEKnnlqeqqeeeeearknlEKQMLALQAQLAEAKKKvdddlgTIEGLEE 1402
Cdd:pfam17380 313 --------------ERRRKLEEAEKARQAEMDR-----------------QAAIYAEQERMAMERER------ELERIRQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1403 NKKKllKDMESLSQrlEEKAMAYDK---LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARyae 1479
Cdd:pfam17380 356 EERK--RELERIRQ--EEIAMEISRmreLERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1480 erdraEAEAREKETKALSLARALEEALEAKEEFERQNKqlradMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLE 1559
Cdd:pfam17380 429 -----QEEARQREVRRLEEERAREMERVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKIL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1560 ELEdelqatedaklrLEVNMQAMKaqferdlqardeQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEM-DLKD 1638
Cdd:pfam17380 498 EKE------------LEERKQAMI------------EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeERRR 553
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 212450 1639 LEGQIEAAN--KARDEAIKQLRKLQAQMKDYQRELEEARAS 1677
Cdd:pfam17380 554 IQEQMRKATeeRSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
894-1421 |
2.08e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 894 QLLEEKNILaEQLQAETELfAEAEEMRARLaakkqELEEILHDLESRVEEEEERNQILQNEKKKMQGhiqdleeqldeee 973
Cdd:pfam05557 3 ELIESKARL-SQLQNEKKQ-MELEHKRARI-----ELEKKASALKRQLDRESDRNQELQKRIRLLEK------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 974 garqklqlEKVTAEAKIKKMEEEILLL---EDQNSKFLKEKKLMEDRIAECTSQLAEEeekaknLAKLKNKQEMMITDLE 1050
Cdd:pfam05557 63 --------REAEAEEALREQAELNRLKkkyLEALNKKLNEKESQLADAREVISCLKNE------LSELRRQIQRAELELQ 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1051 ERLKKEEKTRQELEKAKRKLdgetTDLQDQIAELQAQIEELKIQLAKKEEelqaaLARGDEEAVQKNNALKVIRELQAQI 1130
Cdd:pfam05557 129 STNSELEELQERLDLLKAKA----SEAEQLRQNLEKQQSSLAEAEQRIKE-----LEFEIQSQEQDSEIVKNSKSELARI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1131 AELQEDLESEKASRNKAEKQKRD---LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieeetknheaQIQEI 1207
Cdd:pfam05557 200 PELEKELERLREHNKHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQ------------SWVKL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1208 RQRHATAL---EELSEQLEQAKRFKANLEKNKQGLESDnkelaceVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERL 1284
Cdd:pfam05557 268 AQDTGLNLrspEDLSRRIEQLQQREIVLKEENSSLTSS-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKAL 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1285 RVELAEKANKLQNELDNVSSLLEEAEKKgIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLqeqqee 1364
Cdd:pfam05557 341 VRRLQRRVLLLTKERDGYRAILESYDKE-LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGY------ 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 212450 1365 eeearkNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKlLKDMESLSQRLEEK 1421
Cdd:pfam05557 414 ------KQQAQTLERELQALRQQESLADPSYSKEEVDSLRRK-LETLELERQRLREQ 463
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1540-1744 |
2.20e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1540 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1618
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1619 RKQRALAVAAKKKMEMDLKDLEGQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARASRDE-- 1680
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1681 -IFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1744
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1620-1873 |
2.32e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1620 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEI 1699
Cdd:COG4372 10 KARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1700 LQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTL 1779
Cdd:COG4372 90 QAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1780 NSELagERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1859
Cdd:COG4372 170 EQEL--QALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250
....*....|....
gi 212450 1860 KLKEVFMQVEDERR 1873
Cdd:COG4372 248 KEELLEEVILKEIE 261
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1050-1230 |
2.36e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 43.11 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1050 EERLKKEEKTRQELEKAKRKLDGETtdlQDQIAELQAQIEELKI------QLAKKEEELQaalargDEEAVQKNNALKVI 1123
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIK------DKQEKLMRRCKKVL 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1124 RELQAQIAELqedLESEkasrnkaekqkRDLSEELEALKTELEdTLDttAAQQELRTKREQEVAELKKAIEEETKN---- 1199
Cdd:pfam10168 617 QRLNSQLPVL---SDAE-----------REMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSIRKKSslsl 679
|
170 180 190
....*....|....*....|....*....|....
gi 212450 1200 ---HEAQIQEIRQRHAtalEELSEQLEQAKRFKA 1230
Cdd:pfam10168 680 sekQRKTIKEILKQLG---SEIDELIKQVKDINK 710
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
898-1101 |
2.45e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 898 EKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLEsrveeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQ 977
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA----------KTIKAEIEELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 978 KLQLEKVTAEAKIKKMEEEILLLEDQN------SKFLKEKKLME---DRIAECTSQLAEEEEKAKNLAKLKN---KQEMM 1045
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYEKGGvcptctQQISEGPDRITkikDKLKELQHSLEKLDTAIDELEEIMDefnEQSKK 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1046 ITDLEERLKKEEKTRQ-------ELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1101
Cdd:PHA02562 339 LLELKNKISTNKQSLItlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1086-1311 |
2.57e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 42.01 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1086 AQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1165
Cdd:pfam06008 12 PAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1166 EDTLDT-TAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQ-LEQAKRFKANLEKNKQGLESDN 1243
Cdd:pfam06008 92 KNLIDNiKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAeLKAAQDLLSRIQTWFQSPQEEN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1244 KELAcevKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1311
Cdd:pfam06008 172 KALA---NALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1014-1193 |
2.60e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1014 MEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK------EEKTRQELEKaKRKLDGETTDLQDQIAELQAQ 1087
Cdd:COG1842 35 MEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLalekgrEDLAREALER-KAELEAQAEALEAQLAQLEEQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1088 IEELKIQLAKKEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQEDLESEKASR--NKAEKQKRDLSEELEALKT-E 1164
Cdd:COG1842 114 VEKLKEALRQLESKLEELKAKKDTLKARAKAA-----KAQEKVNEALSGIDSDDATSalERMEEKIEEMEARAEAAAElA 188
|
170 180
....*....|....*....|....*....
gi 212450 1165 LEDTLDTTAAQQELRTKREQEVAELKKAI 1193
Cdd:COG1842 189 AGDSLDDELAELEADSEVEDELAALKAKM 217
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
881-1057 |
2.66e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 881 VEAELEEMERKHQQLLEEKNILAEQlQAETELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMqg 960
Cdd:COG2433 378 IEEALEELIEKELPEEEPEAEREKE-HEERELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEA-- 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 961 hiqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEILLLEdqnsKFLKEkklmEDRIAEctsQLAEEEEKAKNLAKLKN 1040
Cdd:COG2433 454 ----------------RSEERREIRKDREISRLDREIERLE----RELEE----ERERIE---ELKRKLERLKELWKLEH 506
|
170
....*....|....*..
gi 212450 1041 KQEMMITDLEERLKKEE 1057
Cdd:COG2433 507 SGELVPVKVVEKFTKEA 523
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1046-1138 |
2.74e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 41.45 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1046 ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRE 1125
Cdd:pfam11932 15 LDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERE 94
|
90
....*....|...
gi 212450 1126 LQAQIAELQEDLE 1138
Cdd:pfam11932 95 LVPLMLKMLDRLE 107
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1543-1698 |
2.91e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 42.05 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1543 SKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD-LQARDEQNEEKKRMLVKQVRELEAE------- 1614
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEaESSREQLQELEEQLATERSARREAEaelerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1615 ------LEDERKQRALAVAAKKKMEMDLKDLEGQIEA---ANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1685
Cdd:pfam09787 121 eelrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 212450 1686 KESEKKLKGLEAE 1698
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
862-959 |
2.94e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 862 EELQAKDEEL-MKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQaetELFAEAE-EMRARLAAKKQELEEIL----- 934
Cdd:PRK00409 519 NELIASLEELeRELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIkelrq 595
|
90 100 110
....*....|....*....|....*....|....*.
gi 212450 935 -----------HDLESRVEEEEERNQILQNEKKKMQ 959
Cdd:PRK00409 596 lqkggyasvkaHELIEARKRLNKANEKKEKKKKKQK 631
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1588-1726 |
2.95e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.03 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1588 RDLQARDEQNEEKKRMLVKQVRELEAELeDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDY 1667
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAEL-DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1668 -------QRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADE 1726
Cdd:pfam00529 133 apiggisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1022-1160 |
2.97e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1022 TSQLAEEEEKAKNLAKlknKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1101
Cdd:COG2268 194 IAEIIRDARIAEAEAE---RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 212450 1102 LQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1160
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEA 329
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1587-1896 |
3.00e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1587 ERDLQARDEQNEE---KKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDL-----------EGQIEAANKARDE 1652
Cdd:COG5185 161 IKDIFGKLTQELNqnlKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGsestllekakeIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1653 AIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEfaASERARRHAEQERDELADEIANSAS 1732
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFEN--TKEKIAEYTKSIDIKKATESLEEQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1733 GKSALLDEkrrLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQ---QLERQNKELKA 1809
Cdd:COG5185 319 AAAEAEQE---LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSfkdTIESTKESLDE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1810 KLQELEGSVKSKFKA---TISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYK------- 1879
Cdd:COG5185 396 IPQNQRGYAQEILATledTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAydeinrs 475
|
330
....*....|....*....
gi 212450 1880 --EQMEKANARMKQLKRQL 1896
Cdd:COG5185 476 vrSKKEDLNEELTQIESRV 494
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1647-1893 |
3.14e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1647 NKARDEAIKQLRKLQA-QMKDYQRELEEARASR--------DEIFAQSKESEKKLKGLEAEILQLqeEFAASERARRHAE 1717
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEELSNERLRKlrslltklSEALDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1718 QERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEeqsNMELLNERFRKTTLQ-VDTLNSELAGERSAAQKSENA 1796
Cdd:PRK05771 93 EELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNF---DLDLSLLLGFKYVSVfVGTVPEDKLEELKLESDVENV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1797 -----------------RQQLERQNKELK-AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEqeakeraaanklvrRTE 1858
Cdd:PRK05771 170 eyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------------SLL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 212450 1859 KKLKEVFMQVEDERRHADQYKEQM-EKANARMKQLK 1893
Cdd:PRK05771 236 EELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1609-1723 |
3.19e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1609 RELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1688
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 212450 1689 EKKLKGLEAEILQLQEEFAASERARRHAEQERDEL 1723
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1175-1386 |
3.36e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1175 QQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ 1254
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1255 QVKAESEHKRKKLDAQ-VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQEL 1333
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 212450 1334 LQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEA 1386
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1427-1630 |
3.40e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1427 KLEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKNISAryaeERDRAEAEAREKETKALSLARALEEAL 1506
Cdd:NF012221 1566 RAEADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEESRAVTKELTTLAQGLDALD 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1507 EAKEEFERQNKQLRAD-----MEDLMSSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1580
Cdd:NF012221 1634 SQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKqLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDID 1713
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 212450 1581 AMKAQFE-RDLQARDEQNEEKKRmlvKQVRELEAELEDERKQRALAVAAKK 1630
Cdd:NF012221 1714 DAKADAEkRKDDALAKQNEAQQA---ESDANAAANDAQSRGEQDASAAENK 1761
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
976-1192 |
3.49e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 976 RQKLQLEKVTAEAKIKKMEEEillLE--DQNskflkekKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERL 1053
Cdd:NF012221 1571 RQRLEQEKQQQLAAISGSQSQ---LEstDQN-------ALETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAG 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1054 KKEEKTRQELekAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgDEEAVQKNnalkvirelQAQIAEL 1133
Cdd:NF012221 1641 ESGDQWRNPF--AGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAK-SEAGVAQG---------EQNQANA 1708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1134 QEDLESekaSRNKAEKQKRD-LSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKA 1192
Cdd:NF012221 1709 EQDIDD---AKADAEKRKDDaLAKQNEAQQAESDANAAANDAQS--RGEQDASAAENKAN 1763
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
975-1278 |
3.52e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 975 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEE-EKAKNLAKLKNK--QEMMITDLEE 1051
Cdd:pfam15964 390 LRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEmDVTKVCGEMRYQlnQTKMKKDEAE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1052 RLKKEEKTR---------QELEKAKRKLDGETTDL-QDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK---NN 1118
Cdd:pfam15964 470 KEHREYRTKtgrqleikdQEIEKLGLELSESKQRLeQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQsfsNE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1119 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-QELRTKREQEVAELkkaiEEET 1197
Cdd:pfam15964 550 AKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKlEEITQKSRSEVEQL----SQEK 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1198 KNHEAQIQEIRQRHatalEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAK 1277
Cdd:pfam15964 626 EYLQDRLEKLQKRN----EELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
.
gi 212450 1278 V 1278
Cdd:pfam15964 702 V 702
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1023-1266 |
3.67e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.72 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1023 SQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA------ 1096
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSedgtqk 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1097 --------------KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE---DLESEKASRNKAEKQKRDLSEELE 1159
Cdd:pfam15905 153 kmsslsmelmklrnKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITELS 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1160 ALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEirqrhataLEELSEQLEQAKRFKANLEKNKQgl 1239
Cdd:pfam15905 233 CVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD--------LNEKCKLLESEKEELLREYEEKE-- 302
|
250 260
....*....|....*....|....*..
gi 212450 1240 ESDNKELACEVKVLQQVKAESEHKRKK 1266
Cdd:pfam15905 303 QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1046-1162 |
3.88e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.54 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1046 ITDLEERLKKEEKTRQELEKAKRKLD-GETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlargdEEAVQKNNALKviR 1124
Cdd:smart00787 177 LRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL-----ESKIEDLTNKK--S 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 212450 1125 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1162
Cdd:smart00787 250 ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1530-1665 |
3.88e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 3.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1530 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVR 1609
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1610 ELEAELEDERKQRALAVAAKkkmemDLKDLEGQIEAANKARDEAIKQLRKLQAQMK 1665
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1055-1162 |
3.89e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1055 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALAR--GDEEAVQK-------NNALKVIRE 1125
Cdd:cd22656 104 ADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAleTLEKALKDlltdeggAIARKEIKD 183
|
90 100 110
....*....|....*....|....*....|....*...
gi 212450 1126 LQAQIAELQEDLESE-KASRNKAEKQKRDLSEELEALK 1162
Cdd:cd22656 184 LQKELEKLNEEYAAKlKAKIDELKALIADDEAKLAAAL 221
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1344-1441 |
3.97e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1344 LSSRIRQLEEEKNNLQEQQEEEEEAR-KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKA 1422
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKELA 495
|
90
....*....|....*....
gi 212450 1423 MAYDKLEKTKNRLQQELDD 1441
Cdd:COG0542 496 ELEEELAELAPLLREEVTE 514
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1456-1939 |
4.05e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.51 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1456 LEKKQKKFDQMLAEEKNISARYAEE---RDRAEAEAREKETKALsLARALEEALEAKEEFERQNKQLRADMEDLMSS--- 1529
Cdd:NF041483 169 LDESRAEAEQALAAARAEAERLAEEarqRLGSEAESARAEAEAI-LRRARKDAERLLNAASTQAQEATDHAEQLRSStaa 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1530 -KDDVGKNVHELEkskRTLEQQVEEMRTQLEELEdelqaTEDAKLRLEVNMQAMKAqferdLQARDEQNEEKKRMLVKQV 1608
Cdd:NF041483 248 eSDQARRQAAELS---RAAEQRMQEAEEALREAR-----AEAEKVVAEAKEAAAKQ-----LASAESANEQRTRTAKEEI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1609 RELEAELEDErkqralAVAAKKKMEMDLKDLEGQieaANKARDEAIKQLRKLQAQmkDYQRELEEARASRDEIFAQSKES 1688
Cdd:NF041483 315 ARLVGEATKE------AEALKAEAEQALADARAE---AEKLVAEAAEKARTVAAE--DTAAQLAKAARTAEEVLTKASED 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1689 EKKLKGLEAEilqlqeefaASERARRHAEQERDELADEIANSASG-KSALLDEKRRLEARIAQleeeleeeqsnmelLNE 1767
Cdd:NF041483 384 AKATTRAAAE---------EAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE--------------LQE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1768 RFRKTTLQVDTLNSELA--GERSAAQKSENARQQLERQNKELKAKLqelegsvkSKFKATISTLEAKIAQLEEQLEQEAK 1845
Cdd:NF041483 441 EARRLRGEAEQLRAEAVaeGERIRGEARREAVQQIEEAARTAEELL--------TKAKADADELRSTATAESERVRTEAI 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1846 ERAA-----ANKLVRRT----EKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRE 1916
Cdd:NF041483 513 ERATtlrrqAEETLERTraeaERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAE 592
|
490 500
....*....|....*....|....*
gi 212450 1917 --LDDATEANEGLSREVSTLKNRLR 1939
Cdd:NF041483 593 eaLADARAEAERIRREAAEETERLR 617
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
977-1177 |
4.25e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 40.82 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 977 QKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKnLAKLKNKQEMM------ITDLE 1050
Cdd:pfam04012 18 DKAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQ-AALTKGNEELArealaeKKSLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1051 ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQL--AKKEEELQAALARGDEEAvqknnalkVIRELQa 1128
Cdd:pfam04012 97 KQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLkaAKAQEAVQTSLGSLSTSS--------ATDSFE- 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 212450 1129 QIAELQEDLESEKASRNKAEkQKRDLSEELEALKTELEDTLDTTAAQQE 1177
Cdd:pfam04012 168 RIEEKIEEREARADAAAELA-SAVDLDAKLEQAGIQMEVSEDVLARLKA 215
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1151-1318 |
4.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1151 KRDLSEELEALKTELEDTLDttAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA 1230
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1231 NLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELT------AKVTEGERLRVELAEKANKLQNELDnvss 1304
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeeAKEILLEKVEEEARHEAAVLIKEIE---- 179
|
170
....*....|....
gi 212450 1305 llEEAEKKGIKFAK 1318
Cdd:PRK12704 180 --EEAKEEADKKAK 191
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1640-1741 |
5.10e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.96 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1640 EGQIEAANKARDEAIKQLrklqaqmKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAAS-ERARRHAEQ 1718
Cdd:cd06503 36 AESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAEIEQ 106
|
90 100
....*....|....*....|...
gi 212450 1719 ERDELADEIANSASGKSALLDEK 1741
Cdd:cd06503 107 EKEKALAELRKEVADLAVEAAEK 129
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
861-1128 |
5.19e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 936
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 937 LEsrveeEEERNqiLQNEKKKMQghiqdleeqldeeeGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1016
Cdd:pfam15921 676 YE-----VLKRN--FRNKSEEME--------------TTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQK 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1017 RIAECTSQLAEEEEKAKNLaklknKQEMMITDLEERLKKEEKTR--QELEKA---KRKLDGETTDLQDQIAELQAQIEEL 1091
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFL-----EEAMTNANKEKHFLKEEKNKlsQELSTVateKNKMAGELEVLRSQERRLKEKVANM 809
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 212450 1092 KIQLAKKE---EELQAALARGDEEAVQ-KNNALKVIRELQA 1128
Cdd:pfam15921 810 EVALDKASlqfAECQDIIQRQEQESVRlKLQHTLDVKELQG 850
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1640-1741 |
5.31e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.39 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1640 EGQIEAANKARDEAikqlrklQAQMKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAA-SERARRHAEQ 1718
Cdd:COG0711 37 ADGLAEAERAKEEA-------EAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 212450 1719 ERDELADEIANSASGKSALLDEK 1741
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1355-1569 |
5.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 5.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1355 KNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD---DLGTIEgLEENKKKLLKDMESLSQRLEEKAMAYDKLEKT 1431
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqKNGLVD-LSEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1432 KNRLQQELDDLMVDLDHQRQ--IVSNLEKKQKKFDQMLAEeknISARYAEE-RDRAEAEAREKETKAL---SLARALEEA 1505
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAE---LSARYTPNhPDVIALRAQIAALRAQlqqEAQRILASL 318
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212450 1506 LEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELekskRTLEQQVEEMRTQLEELEDELQATE 1569
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVARELYESLLQRLEEAR 378
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1073-1152 |
5.67e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1073 ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKR 1152
Cdd:PRK11448 136 PPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1535-1934 |
6.28e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1535 KNVHELEKSKRTLEQQVEEMRTQLEELEDElqateDAKLRLEVNmQAMK--AQFERDLQARDEQNEEKKRMLVKQVRELE 1612
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-----EEKNREEVE-ELKDkyRELRKTLLANRFSYGPAIDELEKQLAEIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1613 AELE--DERKQRALAVAAKK---KMEMDLKDLEGQIEAA----NKARDEAIKQLRKLQA---QMKDYQRELEEarasrDE 1680
Cdd:pfam06160 160 EEFSqfEELTESGDYLEAREvleKLEEETDALEELMEDIpplyEELKTELPDQLEELKEgyrEMEEEGYALEH-----LN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1681 IFAQSKESEKKLKGLEAEILQLqeEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1760
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1761 NMELLNERFrkttlqvdTLNselAGERSAAQKSENARQQLERQNKELKAKLQELEG---SVKSKFK---ATISTLEAKIA 1834
Cdd:pfam06160 313 ELERVQQSY--------TLN---ENELERVRGLEKQLEELEKRYDEIVERLEEKEVaysELQEELEeilEQLEEIEEEQE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1835 QLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKANARMKQLKRQLeeaeeeatraNASR 1910
Cdd:pfam06160 382 EFKESLQSLRKDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVSDEIEDLADEL----------NEVP 449
|
410 420
....*....|....*....|....*..
gi 212450 1911 ---RKLQRELDDATEANEGLSREVSTL 1934
Cdd:pfam06160 450 lnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
877-1352 |
6.40e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 877 KQTKVEAELEEMER-KHQQLLEEKNILAEQLQAETELFAEAEEMRAR---LAAKKQELEEILHDLESRVEEEEERNQILq 952
Cdd:pfam05557 3 ELIESKARLSQLQNeKKQMELEHKRARIELEKKASALKRQLDRESDRnqeLQKRIRLLEKREAEAEEALREQAELNRLK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 953 neKKKMQGHIQDLEEQLDEEEGARQ-KLQLEKVTAEAKIKKMEEEILLLEDQNSKF-LKEKKLMEDRIAECTSQLAEEEE 1030
Cdd:pfam05557 82 --KKYLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRAELELQSTNSELEeLQERLDLLKAKASEAEQLRQNLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1031 KAKNLAKLKNKQemmITDLEERLKKEEKTRQELEKAKRKLdGETTDLQDQIAELQAQIEEL------KIQLAKKEEELQA 1104
Cdd:pfam05557 160 KQQSSLAEAEQR---IKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHLnenienKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1105 ALARgdeeavqknnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL---EALKTELEDTLDTTAAQQELRTK 1181
Cdd:pfam05557 236 KLER--------------EEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLrspEDLSRRIEQLQQREIVLKEENSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1182 REQEVAELKKAI---EEETKNHEAQIQEIRQRhataLEELSEQLE--QAKRFKANLEKN--KQGLESDNKELACE----- 1249
Cdd:pfam05557 302 LTSSARQLEKARrelEQELAQYLKKIEDLNKK----LKRHKALVRrlQRRVLLLTKERDgyRAILESYDKELTMSnyspq 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1250 --------VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELaeKANKLQNELDNVSSLLEEAEkkgikfakdaa 1321
Cdd:pfam05557 378 llerieeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLEREL--QALRQQESLADPSYSKEEVD----------- 444
|
490 500 510
....*....|....*....|....*....|.
gi 212450 1322 SLESQLQDTQELLQEETRQKLNLSSRIRQLE 1352
Cdd:pfam05557 445 SLRRKLETLELERQRLREQKNELEMELERRC 475
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1653-1896 |
6.45e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 40.47 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1653 AIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEE-----------FAASERARRHAEqerd 1721
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtlakaqqvNAESERTLGHAK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1722 ELADEIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLnselagERSAAQKSENa 1796
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEA------ELKAAQDLLS- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1797 rqQLERQNKELKAKLQELEGSVKSKfkatISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHAD 1876
Cdd:pfam06008 159 --RIQTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKN 232
|
250 260
....*....|....*....|
gi 212450 1877 QYKEQMEKANARMKQLKRQL 1896
Cdd:pfam06008 233 QLEETLKTARDSLDAANLLL 252
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1100-1257 |
6.63e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.82 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1100 EELQAALARGDEEAVQ--KNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqqE 1177
Cdd:cd22656 98 ELIDDLADATDDEELEeaKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD-----E 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1178 LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1257
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
992-1167 |
6.67e-03 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 41.65 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 992 KMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEE-----EKAKNLAKLKNK-QEMMITDLEErlkKEEKTRQELEk 1065
Cdd:COG5192 525 KSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEfeelkKKWSSLAQLKSRfQKDATLDSIE---GEEELIQDDE- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1066 akrklDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvQKNNALKviRELQAQIaELQEDLESEKASRN 1145
Cdd:COG5192 601 -----KGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETER-EENARKK--EELRGNF-ELEERGDPEKKDVD 671
|
170 180
....*....|....*....|..
gi 212450 1146 KAEKQKRDLSEELEALKTELED 1167
Cdd:COG5192 672 WYTEEKRKIEEQLKINRSEFET 693
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
873-1020 |
6.71e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.61 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 873 KVKEKQTKVEAELEEMERKHQQLLEEKnilaEQLQAETEL--FAEAEEMRARLAAKKQELEEilhdLESRVEEEEERNQI 950
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEK----EALKKEQDEasFERLAELRDELAELEEELEA----LKARWEAEKELIEE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 951 LQNEKKKMQGHIQDLEEQLDEEEGARQKLQL------EKVTAE--AKI---------KKMeeeillLEDQNSKFLKekkl 1013
Cdd:COG0542 473 IQELKEELEQRYGKIPELEKELAELEEELAElapllrEEVTEEdiAEVvsrwtgipvGKL------LEGEREKLLN---- 542
|
....*..
gi 212450 1014 MEDRIAE 1020
Cdd:COG0542 543 LEEELHE 549
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
856-996 |
7.33e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEelmkVKEKQTKVEAELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 931
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212450 932 EILHDLEsrveeeeernQILQNEKKKMQgHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEE 996
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEE 181
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
856-1167 |
7.39e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 856 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 935
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 936 DLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAE-AKIKKMEEEILLLEDQNSKFLKEKKLM 1014
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAlDELLKEANRNAEKEEELAEAEKLIESL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1015 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1094
Cdd:COG4372 213 PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAA 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1095 LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED 1167
Cdd:COG4372 293 LELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
985-1210 |
7.43e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.98 E-value: 7.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 985 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEmmitdlEERLKKEEKTRQELE 1064
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAE------EKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1065 KAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASR 1144
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 212450 1145 NKAEKQKRdLSEELEALKTELEDTLDTTAAQQELRTKREQEVAElKKAIEEETKNHEAQIQEIRQR 1210
Cdd:TIGR02794 211 AKAEAEAA-AAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR-GAAAGSEVDKYAAIIQQAIQQ 274
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1011-1898 |
7.95e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.35 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1011 KKLMEDRIAECTSQLAEEEEKAKN---------LAKLKNKQEMMITDLEERLK--------KEEKTRQELEKAKRKLDGE 1073
Cdd:NF041483 333 EQALADARAEAEKLVAEAAEKARTvaaedtaaqLAKAARTAEEVLTKASEDAKattraaaeEAERIRREAEAEADRLRGE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1074 TTDLQDQI--------AELQAQIEELKIQ---LAKKEEELQA-ALARGD-------EEAVQK-NNALKVIRELQAQIAEL 1133
Cdd:NF041483 413 AADQAEQLkgaakddtKEYRAKTVELQEEarrLRGEAEQLRAeAVAEGErirgearREAVQQiEEAARTAEELLTKAKAD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1134 QEDLESekASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE-LRTKREQEVAELKKAIEEETKN-HEAQIQEIRQRH 1211
Cdd:NF041483 493 ADELRS--TATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEEVRAAAERAARElREETERAIAARQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1212 ATALEELSeqleqakRFKANLEKNKQGLESDNKELACEVKVLQQVKA-ESEHKRKKLDAQVQELTAKV-TEGERLRVELA 1289
Cdd:NF041483 571 AEAAEELT-------RLHTEAEERLTAAEEALADARAEAERIRREAAeETERLRTEAAERIRTLQAQAeQEAERLRTEAA 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1290 EKANKLQNELDNVS-SLLEEAekkgikfAKDAASLESQLQDTQELLQEETRqklnlSSRIRQLEEEKNNLQEQQEEEEEA 1368
Cdd:NF041483 644 ADASAARAEGENVAvRLRSEA-------AAEAERLKSEAQESADRVRAEAA-----AAAERVGTEAAEALAAAQEEAARR 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1369 RKNLEKqmlALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKA--MAYDKLEKTKNRLQQelddlmvdl 1446
Cdd:NF041483 712 RREAEE---TLGSARAEADQERERAREQSEELLASARKRVEEAQAEAQRLVEEAdrRATELVSAAEQTAQQ--------- 779
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1447 dhQRQIVSNLEKKqkkfdqmlAEEKNISARYAEER--DRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADME 1524
Cdd:NF041483 780 --VRDSVAGLQEQ--------AEEEIAGLRSAAEHaaERTRTEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAA 849
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1525 DLMSSKDdVGKNVHELEKSKRTLEQQVEEMRTqleELEDELQATEDAKLRLEVnmqamkaqferdlQARDEQNEEKKRML 1604
Cdd:NF041483 850 KALAERT-VSEAIAEAERLRSDASEYAQRVRT---EASDTLASAEQDAARTRA-------------DAREDANRIRSDAA 912
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1605 VKQVREL-EAELEDERKQRALAVAAKKKmemdlkdLEGQIEAANKARDEAIKQLRKLQAqmkDYQRELEEARASRDEIFA 1683
Cdd:NF041483 913 AQADRLIgEATSEAERLTAEARAEAERL-------RDEARAEAERVRADAAAQAEQLIA---EATGEAERLRAEAAETVG 982
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1684 QSKESEKKLKGlEAEILQLQEEfAASERARRHAEQERDELADEIANSASgksalldeKRRLEAriaqleeeleeeqsnme 1763
Cdd:NF041483 983 SAQQHAERIRT-EAERVKAEAA-AEAERLRTEAREEADRTLDEARKDAN--------KRRSEA----------------- 1035
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1764 llnerfrktTLQVDTLNSELAGErsAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQE 1843
Cdd:NF041483 1036 ---------AEQADTLITEAAAE--ADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERIVAEATVEGNSLVEKARTD 1104
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1844 AKE-----RAAANKLVRRTEKKLKEVFMQVED-----ERRHADQYKEQMEKANARMKQLKRQLEE 1898
Cdd:NF041483 1105 ADEllvgaRRDATAIRERAEELRDRITGEIEElheraRRESAEQMKSAGERCDALVKAAEEQLAE 1169
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
861-1148 |
8.18e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.82 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 861 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQL---LEEKNILAEQLqaETELFAEAEEMRA------RLAAKKQELE 931
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELrieLRDKTAQAEAL--ERQLAAETEQNRAleeenkALREEAQAAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 932 EILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIL-----------LL 1000
Cdd:pfam19220 153 KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAaeqaereraeaQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1001 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEkakRKLDGETTDLQDQ 1080
Cdd:pfam19220 233 EEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLE---RRLAGLEADLERR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1081 IAELQaQIEELKIQLAKKEEELQAALARGD---EEAVQKNNAL------------KVIRELQAQIAELQEDLESEKASRN 1145
Cdd:pfam19220 310 TQQFQ-EMQRARAELEERAEMLTKALAAKDaalERAEERIASLsdriaeltkrfeVERAALEQANRRLKEELQRERAERA 388
|
...
gi 212450 1146 KAE 1148
Cdd:pfam19220 389 LAQ 391
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1602-1744 |
8.94e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1602 RMLVKQVRELEAELEDERKQRALAVAAKKKMEMdlkdLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEAR------ 1675
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarr 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212450 1676 ---ASRDEIFAQSKESEKKL-KGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1744
Cdd:pfam00529 130 rvlAPIGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1588-1894 |
8.94e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1588 RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLK-------DLEGQIEAANKARDEAIKQLRKL 1660
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1661 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA----DEIANSASGKSA 1736
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1737 LLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEG 1816
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212450 1817 SVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKR 1894
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| Rab5-bind |
pfam09311 |
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow ... |
1041-1300 |
9.03e-03 |
|
Rabaptin-like protein; Members of this family are predominantly found in Rabaptin and allow for binding to the GTPase Rab5. This interaction is necessary and sufficient for Rab5-dependent recruitment of Rabaptin5 to early endosomal membranes.
Pssm-ID: 462752 [Multi-domain] Cd Length: 307 Bit Score: 40.34 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1041 KQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTdlqdqiaelqAQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL 1120
Cdd:pfam09311 27 KLQEMLRQANDQLEKTMKDKKELEDKMNQLSEETS----------NQVSTLAKRNQKSETLLDELQQAFSQAKRNFQDQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1121 KVIRELQAQIAE----LQEDLESEKASRNKAEKQKR-------DLSEELEALKTEL-EDTLDTTAAQQELRTKREQEVAE 1188
Cdd:pfam09311 97 AVLMDSREQVSDelvrLQKDNESLQGKHSLHVSLQQaekfdmpDTVQELQELVLKYrEELIEVRTAADHMEEKLKAEILF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1189 LKKAIEEEtknhEAQIQEIRQRHATALEELSEQLEQAKRFKANLEK---NKQGLESDNKELACEVKVLQQVKAEsehkrk 1265
Cdd:pfam09311 177 LKEQIQAE----QCLKENLEETLQAEIENCKEEIASISSLKVELERikaEKEQLENGLTEKIRQLEDLQTTKGS------ 246
|
250 260 270
....*....|....*....|....*....|....*
gi 212450 1266 kLDAQVQELTAKVTEGERLRVELAEKANKLQNELD 1300
Cdd:pfam09311 247 -LETQLKKETNEKAAVEQLVFEEKNKAQRLQTELD 280
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1629-1859 |
9.67e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1629 KKKMEMDLKDLEGqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE-----SE 1689
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1690 KKLKGLEAEILQLQEEFAasERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1764
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1765 LNERFRKTTLQVDTLnsELAgersaaQKSENARQQLERQNKEL-KAKLQELEGSvkskfkatistLEAKIAQLEEQLEQE 1843
Cdd:PRK10929 178 LQAESAALKALVDEL--ELA------QLSANNRQELARLRSELaKKRSQQLDAY-----------LQALRNQLNSQRQRE 238
|
250
....*....|....*.
gi 212450 1844 AkERAaanklVRRTEK 1859
Cdd:PRK10929 239 A-ERA-----LESTEL 248
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1684-1940 |
9.79e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 9.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1684 QSKESEKKLKGLEAEILQLQEEFaaserarRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1763
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEI-------EELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1764 LLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATisTLEAKIAQLEEQLEqE 1843
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELE-K 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1844 AKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA 1923
Cdd:COG1340 152 AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
250
....*....|....*..
gi 212450 1924 NEGLSREVSTLKNRLRR 1940
Cdd:COG1340 232 IIELQKELRELRKELKK 248
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1048-1202 |
9.84e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 40.13 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212450 1048 DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQknnalkvIRELQ 1127
Cdd:pfam09787 48 ELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAE-------LERLQ 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212450 1128 AQIAELQEDLESEKASRnkaEKQKRDLSEELEALKTELEDTLDTTAAQQELrtkrEQEVAELKKAIEEETKNHEA 1202
Cdd:pfam09787 121 EELRYLEEELRRSKATL---QSRIKDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETLIQKQTMLEA 188
|
|
| |
