|
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 ... |
879-1959 |
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 1513.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 879 TRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 958
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKEKQQKAESELKELEKKHQQLCEEKNILAEQLQAETELFAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 959 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDR 1038
Cdd:pfam01576 81 EARLEEEEERSQQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIKKMEEDILLLEDQNNKLQKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1039 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAK 1118
Cdd:pfam01576 161 ISEFTSNLAEEEEKSKSLNKLKNKHEAMISDLEDRLKKEEKGRQELEKAKRKLEGESSDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1119 KEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1198
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNAALKKLRELEAQLSELQEDLESERAARAKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1199 LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1278
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKASLEKAKQALESENAELQAELRSLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1279 AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE 1358
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQSRLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1359 TRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQR 1438
Cdd:pfam01576 481 TRQKLNLSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALTQR 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1439 LEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALS 1518
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETKALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1519 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEV 1598
Cdd:pfam01576 641 LARALEEALDAKEELERQNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1599 NMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1678
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIEAANKGRDEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1679 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSAL 1758
Cdd:pfam01576 801 KKLQAQMKDLQRELDEARASRDEIFAQSKESEKKLKSLEAELLQLQEDLAAAERARRQAQQERDELAEEIASGNSGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1759 LDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGS 1838
Cdd:pfam01576 881 LDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1839 VKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1918
Cdd:pfam01576 961 VKSKYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRNADQYKDQAEKGNSRLKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 45382679 1919 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESAEAMNREVTTLRSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-802 |
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: 1432.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14920 231 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14920 311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14920 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppVDRIVG 658
Cdd:cd14920 471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD---------------------VDRIVG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14920 530 LDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14920 610 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
99-802 |
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: 1319.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG---------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQ 337
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK-FQKP 576
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 577 RQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQniqracfydnitglhdppvdri 656
Cdd:cd01377 469 KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE---------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 657 vgldqvtgitETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 736
Cdd:cd01377 527 ----------SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVL 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 737 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd01377 597 EGIRICRKGFPNRIIFAEFKQRYSILAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-802 |
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: 1222.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14932 235 TMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14932 315 QKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14932 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppVDRIVG 658
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD---------------------VDRIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTGITETAFGsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14932 534 LDKVAGMGESLHG-AFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEG 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14932 613 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-802 |
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: 1192.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14919 228 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14919 308 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14919 388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppVDRIVG 658
Cdd:cd14919 468 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD---------------------VDRIIG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14919 527 LDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14919 607 IRICRQGFPNRVVFQEFRQRYEILTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
99-802 |
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: 1182.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14921 231 TLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppVDRIVG 658
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD---------------------VDRIVG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14921 530 LDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEG 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14921 610 IRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
99-802 |
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: 1174.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd15896 235 TMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd15896 315 QKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd15896 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppVDRIVG 658
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD---------------------VDRIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTGITEtaFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd15896 534 LDKVSGMSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd15896 612 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
99-802 |
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: 1166.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKpRQ 578
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEiqniqracfydnitglhdppvdRIVG 658
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA----------------------EIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTgITETAFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14911 534 MAQQA-LTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14911 611 IRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-802 |
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: 1127.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPpespkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQE 338
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQ 578
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppVDRIVG 658
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD---------------------VEGIVG 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 LDQVTGITETAFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14930 529 LEQVSSLGDGPPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14930 607 IRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
87-802 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 Cd Length: 674 Bit Score: 1098.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKN 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------VGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 247 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSN-GYI 325
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 326 PIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:pfam00063 307 LCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:pfam00063 387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 566 EQGTHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEiqniqracfydni 645
Cdd:pfam00063 464 TFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDY------------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 646 tglhdppvDRIVGLDQVTGITETafgsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 725
Cdd:pfam00063 530 --------ETAESAAANESGKST----PKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSL 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 726 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:pfam00063 598 VLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
80-814 |
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: 1013.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhQGELERQLLQANPILESFG 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------VGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 240 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRF 319
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 320 LSNG-YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGM 397
Cdd:smart00242 225 LNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 398 NVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFE 477
Cdd:smart00242 305 DPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 478 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDK 557
Cdd:smart00242 384 VNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 558 TFVEKLVQEQGTHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNiq 637
Cdd:smart00242 461 TFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN-- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 638 racfydnitglhdppvdrivgldqvtgitetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:smart00242 538 -------------------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKK 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQS 797
Cdd:smart00242 581 PGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKT 660
|
730
....*....|....*..
gi 45382679 798 KIFFRAGVLAHLEEERD 814
Cdd:smart00242 661 KVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1379 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 912.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 36 VWIPSERHGFEAASIKEERGDEVLVELA---ENGKKALVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 191 VIQYLAHVASSHkgrkdhniPPESpkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGAN 270
Cdd:COG5022 172 IMQYLASVTSSS--------TVEI-------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 271 IETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFS 349
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 350 HDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 429
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 430 AVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 509
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 510 QREGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGTHSKFQKPRQLKDKadFCI 587
Cdd:COG5022 475 VKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 588 IHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEiQNIQracfydnitglhdppvdrivgldqvtgite 667
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDE-ENIE------------------------------ 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 668 tafgsayktKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 747
Cdd:COG5022 600 ---------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFP 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 748 NRIVFQEFRQRYEILTPNA----IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIF 823
Cdd:COG5022 671 SRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATR 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 824 FQAVCRGYLARKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKqtkve 903
Cdd:COG5022 751 IQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKT----- 825
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 904 aeleemerkhqqlLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVeeeeernQILQNEKKKMQGHI 983
Cdd:COG5022 826 -------------IKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYL-------QSAQRVELAERQLQ 885
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 984 QDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS--QLAEEEEKAKNLAKLKN 1061
Cdd:COG5022 886 ELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVESK 965
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1062 KQEmMITDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGDEEavqkn 1138
Cdd:COG5022 966 LKE-TSEEYEDLLKKSTILVREGNKANSELKNfkkELAELSKQYGALQESTKQLK-ELPVEVAELQSASKIISSE----- 1038
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1139 nalkviRELQAQIAELQEdlesekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEET 1218
Cdd:COG5022 1039 ------STELSILKPLQK-------LKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTN 1105
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1219 KNH--EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACevkVLQQVKAESEHKRKKLDAQVQELT 1296
Cdd:COG5022 1106 RNLvkPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDG---LFWEANLEALPSPPPFAALSEKRL 1182
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1297 AKVTEGERLRVELAEKANKLQNELDNVSS----------LLEEAEKKGI------KFAKDAASLESQLQDTQELLQEETR 1360
Cdd:COG5022 1183 YQSALYDEKSKLSSSEVNDLKNELIALFSkifsgwprgdKLKKLISEGWvpteysTSLKGFNNLNKKFDTPASMSNEKLL 1262
|
1370
....*....|....*....
gi 45382679 1361 QKLNLSSRIRQLEEEKNNL 1379
Cdd:COG5022 1263 SLLNSIDNLLSSYKLEEEV 1281
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
99-802 |
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 Cd Length: 633 Bit Score: 859.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSS-----------SSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQD 332
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 333 KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGT 569
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 570 HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkdeiqniqracfydnitglh 649
Cdd:cd00124 467 HPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 650 dppvdrivgldqvtgitetafgsayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 729
Cdd:cd00124 519 --------------------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQ 560
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 730 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd00124 561 LRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
99-802 |
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: 783.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESpkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLAT----KTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14927 236 MATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQK 575
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 576 PR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdeiQNIQRACFYDnitglhdpp 652
Cdd:cd14927 472 PRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY----ENYVGSDSTE--------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 653 vdrivglDQVTGITETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14927 539 -------DPKSGVKEK------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRC 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK-GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14927 606 NGVLEGIRICRKGFPNRILYADFKQRYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
100-802 |
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: 764.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASShkgrkdhnIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT--------GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKP 576
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdeiqniqracfYDNITGLhDPPVD 654
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHL-------------YATFATA-DADSG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 655 RivgldqvtgitetafGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14913 535 K---------------KKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNG 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14913 600 VLEGIRICRKGFPNRILYGDFKQRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
99-802 |
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: 743.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippeSPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK----------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKP 576
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 577 RQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNiqracfydnitglhdppv 653
Cdd:cd14909 467 KPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQ------------------ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 drivgldqvTGITETAFGSAYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14909 529 ---------SGGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCN 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14909 599 GVLEGIRICRKGFPNRMMYPDFKMRYKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
99-802 |
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: 732.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvkHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSD------------GKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKP 576
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 577 RQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdKFVAELWKDEiqniqracfydnitglhdppv 653
Cdd:cd14934 465 KGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKE--------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 drivgldqvtgitETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14934 523 -------------EEAPAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLAC 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14934 590 NGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
100-802 |
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: 716.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippESpkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd01380 306 IVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 497 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK--FQ 574
Cdd:cd01380 386 FNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 KPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSsdkfvaelwkdeiqniqracfydnitglhdppvd 654
Cdd:cd01380 462 KPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKAS---------------------------------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 655 rivgldqvtgitetafgsayKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd01380 506 --------------------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACG 562
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd01380 563 VLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
99-802 |
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: 711.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASShkgrkdhnippesPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM-------------IESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQK 575
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIqniqracfydnITGlhdppv 653
Cdd:cd14929 462 PKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYI-----------STD------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 drivgldqvtgiTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14929 525 ------------SAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCN 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14929 593 GVLEGIRICREGFPNRLLYADFKQRYCILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
100-802 |
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: 704.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnippESPKpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPG----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14917 153 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQK 575
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdeiqniqracfYDNITGLhDPPV 653
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNL-------------FANYAGA-DAPI 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 DRIVGldqvtgitetafgsayKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14917 534 EKGKG----------------KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRC 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14917 598 NGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
101-802 |
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: 685.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 181 GAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES--------GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 261 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQET 339
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 340 MEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 500 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPRQ 578
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 LKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfydnitglhdppvdri 656
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFS-------------------------- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 657 vglDQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 736
Cdd:cd14918 525 ---TYASAEADSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 737 EGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14918 602 EGIRICRKGFPSRILYGDFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-802 |
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: 683.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKP 576
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELwkdeiqniqracfYDNITGlhdppvd 654
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFL-------------FSNYAG------- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 655 rivgldqvtgiTETAFGSAY----KTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 730
Cdd:cd14923 530 -----------AEAGDSGGSkkggKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQL 598
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 731 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14923 599 RCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
100-802 |
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: 681.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGTHSKFQKPR 577
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 578 QLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfydnitglhdppvdr 655
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFS------------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 656 ivGLDQVTGitETAFGSAYK--TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14912 527 --GAQTAEG--ASAGGGAKKggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14912 603 NGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
100-802 |
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: 679.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKPR 577
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 578 QLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfydnitglhdppvdr 655
Cdd:cd14910 472 PAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFS------------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 656 ivglDQVTGITETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14910 527 ----GAAAAEAEEGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNG 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14910 603 VLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
100-802 |
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: 679.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnippespkPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN--------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDN 335
Cdd:cd14916 154 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14916 232 LLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14916 312 EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 496 LFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQ 574
Cdd:cd14916 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 KPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdpp 652
Cdd:cd14916 468 KPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFST--------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 653 vdrIVGLDqvTGitETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14916 527 ---YASAD--TG--DSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRC 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14916 600 NGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
100-802 |
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: 671.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQ 337
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GTHSKFQKP 576
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfydnitglhdppvd 654
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFS------------------------ 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 655 rivglDQVTGITETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14915 527 -----GGQTAEAEGGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14915 602 GVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
100-802 |
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: 640.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14883 303 NVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQK 575
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 576 PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfYDNITGLhdppvdr 655
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT-----------YPDLLAL------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 656 iVGLDQVTGITETAFGsaykTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 735
Cdd:cd14883 521 -TGLSISLGGDTTSRG----TSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGM 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 736 LEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14883 595 LEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
100-802 |
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: 640.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnippespkpVKHqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VKD------MLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQE 338
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---R 415
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd01378 306 SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 496 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGTHSKFQ 574
Cdd:cd01378 386 IFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 KPRQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQniqracfydnitglhdpp 652
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD------------------ 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 653 vdrivgldqvtgitetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd01378 525 ----------------------LDSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKY 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd01378 583 LGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
100-802 |
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: 639.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQE 338
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd01383 221 LKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd01383 301 VKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 499 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRq 578
Cdd:cd01383 381 RHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 579 lkDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVaelwkdeiqniqrACFYDNITGLHDPPVDRivg 658
Cdd:cd01383 457 --GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLP-------------QLFASKMLDASRKALPL--- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 659 ldqvtgiteTAFGSAYKTKkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd01383 518 ---------TKASGSDSQK----QSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEV 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 739 IRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd01383 585 VRISRSGYPTRMTHQEFARRYGFLLPEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
99-802 |
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: 603.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01381 222 DIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSK 572
Cdd:cd01381 382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 573 FQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIqniqracfydnitglhdpp 652
Cdd:cd01381 458 YLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDI------------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 653 vdrivgldqvtgitetAFGSAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd01381 518 ----------------SMGSETRKKS---PTLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRY 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd01381 579 SGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
99-802 |
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: 601.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIPPespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEGRS-----------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDN 335
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIK 412
Cdd:cd01384 225 YRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 413 VGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01384 304 VTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHS 571
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 572 KFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdeiqniqracfydnitglhdP 651
Cdd:cd01384 460 RFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF---------------------P 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 652 PVDRivgldqvtgiteTAFGSAYKtkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 731
Cdd:cd01384 517 PLPR------------EGTSSSSK-----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLR 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 732 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 802
Cdd:cd01384 580 CGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
99-802 |
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: 572.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQ 337
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRA 405
Cdd:cd01382 208 RMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 566 EQGTHSKFQKPRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNiq 637
Cdd:cd01382 440 KHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNN-- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 638 racfydnitglhdppvdrivgldqvtgitetAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:cd01382 518 -------------------------------NKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMT 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQS 797
Cdd:cd01382 567 SHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLT 644
|
....*
gi 45382679 798 KIFFR 802
Cdd:cd01382 645 KVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
99-802 |
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: 568.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV- 413
Cdd:cd14872 220 EVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 573
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 574 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdeiqniqracfydnitglhdPPV 653
Cdd:cd14872 457 VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF---------------------PPS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 DrivgLDQVTgitetafgsayktkkgMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14872 516 E----GDQKT----------------SKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYA 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14872 576 GVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-802 |
2.98e-176 |
|
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: 551.69 E-value: 2.98e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 254 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 334 DNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 412 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQEQG 568
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHASFG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 569 T-------------HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdkfvaelwkdeiqn 635
Cdd:cd14890 477 RksgsggtrrgssqHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR-------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 636 iqracfydnitglhdppvdrivgldqvTGITETafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 715
Cdd:cd14890 542 ---------------------------RSIREV--------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNET 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 716 KRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIG 795
Cdd:cd14890 581 KAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIG 655
|
....*..
gi 45382679 796 QSKIFFR 802
Cdd:cd14890 656 SSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
99-802 |
3.60e-171 |
|
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: 537.80 E-value: 3.60e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnipPESPKPVKhqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN------------QRRNNLVT------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01387 143 FFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQ 574
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 KPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNIQRAcfydnitglhdppvd 654
Cdd:cd01387 458 KPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKA--------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 655 rivgldqvtgiTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd01387 521 -----------PPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSG 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfMDGKQACERMIRALELDP-NLYRIGQSKIFFR 802
Cdd:cd01387 590 MLETIRIRKEGYPVRLPFQVFIDRYRCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
99-802 |
8.76e-170 |
|
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: 535.03 E-value: 8.76e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLahVASSHKGrkdhnippespkpvkHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---------------YGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHS 571
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 572 KFQKPrQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAEL----------WkdeiqNIQRAcF 641
Cdd:cd01385 460 YYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrW-----AVLRA-F 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 642 YDNITGLHDPPVDRIVGLDQVTGI----TETAFGSAYKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:cd01385 532 FRAMAAFREAGRRRAQRTAGHSLTlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKK 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQS 797
Cdd:cd01385 610 PLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKT 685
|
....*
gi 45382679 798 KIFFR 802
Cdd:cd01385 686 KVFLK 690
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
99-802 |
1.76e-166 |
|
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: 525.11 E-value: 1.76e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIppespkpvkhqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgeHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNF 336
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASP--DVEERLFLDSANECAYTgANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGTHSKFQ 574
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 K----PRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhd 650
Cdd:cd14903 453 DviefPRT--SRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKE------------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 651 ppvdrIVGLDQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 730
Cdd:cd14903 512 -----KVESPAAASTSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQL 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 731 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELD-PNLYRIGQSKIFFR 802
Cdd:cd14903 587 RCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
99-800 |
5.53e-164 |
|
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: 518.19 E-value: 5.53e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 171 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPPESpkpvkhqgeLERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------VRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYIP 326
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 327 IPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQL 484
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 485 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFV 560
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 561 EKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdeiqniqrac 640
Cdd:cd14901 464 NKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 641 fydnitglhdppvdrivgldqvtgitetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGK 720
Cdd:cd14901 531 ------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSE 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 721 LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrI 794
Cdd:cd14901 569 FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-V 647
|
....*.
gi 45382679 795 GQSKIF 800
Cdd:cd14901 648 GKTKVF 653
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
99-764 |
2.05e-162 |
|
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: 514.24 E-value: 2.05e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVT---------GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIP-- 326
Cdd:cd14888 145 LQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 327 ----------------------IPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPE 384
Cdd:cd14888 225 idmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 385 NTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG 461
Cdd:cd14888 305 ASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 462 ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGV 541
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 542 LALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS 621
Cdd:cd14888 462 FCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 622 DKFVAELWKdeiqniqracfydnitglhdPPVDRIVGLdqvtgitetafgsayKTKKGMFRTVGQLYKESLTKLMATLRN 701
Cdd:cd14888 540 NPFISNLFS--------------------AYLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDK 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 702 TNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 764
Cdd:cd14888 585 TEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
99-802 |
4.65e-161 |
|
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: 509.72 E-value: 4.65e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnippespkpVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSL----------KEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR- 415
Cdd:cd14873 231 REVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14873 307 EEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQ 574
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 KPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfydnitglHDPPVD 654
Cdd:cd14873 460 KPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE------------------HVSSRN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 655 RivgldqvtgitETAFGSAYKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14873 520 N-----------QDTLKCGSKHRRP---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSG 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKqaCERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14873 586 MLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
100-802 |
2.17e-160 |
|
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: 507.20 E-value: 2.17e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVAsshkgrKDHNippespkpvkhqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLG------KANN------------RTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD 332
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 333 --KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAi 406
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd01379 299 LTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd01379 379 LCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 563 LvqEQGTHSKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdeiqniqracfy 642
Cdd:cd01379 455 F--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 643 dnitglhdppvdrivgldqvtgitetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLD 722
Cdd:cd01379 517 ----------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFD 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 723 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDgKQACERMIRALELDPnlYRIGQSKIFFR 802
Cdd:cd01379 557 REKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
99-802 |
3.84e-156 |
|
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: 495.75 E-value: 3.84e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD----- 332
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 333 --KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14897 223 yyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 567 QGTHSKFQKPrqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKdeiqniqracfydnit 646
Cdd:cd14897 460 CGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 647 glhdppvdrivgldqvtgitetafgsayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLV 726
Cdd:cd14897 522 ---------------------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELV 562
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 727 LDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 802
Cdd:cd14897 563 RRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
99-802 |
4.59e-155 |
|
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: 493.51 E-value: 4.59e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQ 330
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 331 QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAI 406
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 407 LTPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIF 476
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 477 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 555
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 556 DKTFVEKLVQEQ-GTHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDkfvaelwkdeiq 634
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 635 niqracfydnitglhdppvdrivgldqvtgitetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNH 714
Cdd:cd14892 536 ----------------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNN 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 715 EKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELD 788
Cdd:cd14892 563 LKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALE 642
|
730
....*....|....
gi 45382679 789 PNLYRIGQSKIFFR 802
Cdd:cd14892 643 RENFQLGRTKVFLR 656
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
100-762 |
1.96e-145 |
|
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: 465.94 E-value: 1.96e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkDHNIPPESPKPVKHQGeLERQLLQANPILESFGNAKT 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSG-IAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 244 VKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEhlksdlllegfnnyrflsng 323
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 324 yipipGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLG 396
Cdd:cd14900 214 -----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAG 472
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 473 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 552
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 553 KATDKTFVEKLVQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDplndnvatLLHQSSdkfvaelwkde 632
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQEA----------- 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 633 iqniqracfydnitglhdppVDrivgldqvtgitetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIP 712
Cdd:cd14900 507 --------------------VD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKP 540
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 45382679 713 NHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 762
Cdd:cd14900 541 NDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-802 |
7.89e-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: 462.45 E-value: 7.89e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 177 TGESGAGKTENTKKVIQYLAHVAsshkgrkdhnippespkpvKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 257 RINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-- 332
Cdd:cd14889 144 QLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRev 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 333 ---KDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAi 406
Cdd:cd14889 217 qywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd14889 294 LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIerPANPPGVLALLDEECWFPKATDKTFVEKL 563
Cdd:cd14889 374 ACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLF--LNKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 564 VQEQGTHSKFQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNiqracfyd 643
Cdd:cd14889 451 NIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSR-------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 644 niTGLHDPPVDRIvgldqvtGITETAFGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDP 723
Cdd:cd14889 521 --TGTLMPRAKLP-------QAGSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDS 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 724 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFF 801
Cdd:cd14889 586 KYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFF 658
|
.
gi 45382679 802 R 802
Cdd:cd14889 659 K 659
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-765 |
9.16e-144 |
|
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: 462.58 E-value: 9.16e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKHQ-GELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKStKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 249 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLE----GFNNYRFLSNG 323
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 324 YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 401
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 402 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 474
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 552
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 553 KATDKTFVEKLVQEQGTHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDE 632
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 633 IQniqracfydnitglhdppvdrivgldqvtgiTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIP 712
Cdd:cd14907 557 DG-------------------------------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKP 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 45382679 713 NHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 765
Cdd:cd14907 606 NEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-802 |
7.41e-141 |
|
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: 453.73 E-value: 7.41e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 252 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 329
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 330 QQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 404
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 405 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 482
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 483 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 563 LVQEQGTHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqSSDKFvaelwkdeiqniqracf 641
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLA-SSAKF----------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 642 ydnitglhdppvdrivgLDQVTGITEtafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKL 721
Cdd:cd14891 531 -----------------SDQMQELVD------------------------------TLEATRCNFIRCIKPNAAMKVGVF 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 722 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIF 800
Cdd:cd14891 564 DNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVF 643
|
..
gi 45382679 801 FR 802
Cdd:cd14891 644 FR 645
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-802 |
1.24e-134 |
|
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: 436.68 E-value: 1.24e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPpespkpvkhqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA---------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDN 335
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14904 302 ESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGTHSK 572
Cdd:cd14904 382 KFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNES 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 573 FQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdeiqniqracfydnitglhdpp 652
Cdd:cd14904 458 IDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF----------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 653 vdrivglDQVTGITETAFGSAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14904 513 -------GSSEAPSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRS 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 802
Cdd:cd14904 585 AGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-802 |
3.52e-134 |
|
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: 434.98 E-value: 3.52e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIppespkpvkhqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------RQPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQ 337
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-G 414
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14896 301 YGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 494 QQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 573
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 574 QKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWkdeiqniQRAcfydnitglhdppv 653
Cdd:cd14896 458 AKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF-------QEA-------------- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 drivgldqvtgitetafGSAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14896 515 -----------------EPQYGLGQGK-PTLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQA 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14896 577 GILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-802 |
1.43e-132 |
|
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: 432.02 E-value: 1.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPPEspkpvkhQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-------KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGE--------HLKSDLLLEGFNNYRFL 320
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 321 SNGYIPIPGQ-QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLG 396
Cdd:cd14908 234 GQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFE 474
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 553
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 554 ATDKTFVEKLV--------QEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNmdplndnvatllhqssdkf 624
Cdd:cd14908 470 GSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 625 vaelwKDEIQNiqracfydnitglhdppvdrivgldqvtgitetafgsaykTKKGMFRTvGQLYKESLTKLMATLRNTNP 704
Cdd:cd14908 531 -----KDEIPL----------------------------------------TADSLFES-GQQFKAQLHSLIEMIEDTDP 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 705 NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK--------------- 769
Cdd:cd14908 565 HYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqkl 643
|
730 740 750
....*....|....*....|....*....|....*....
gi 45382679 770 --GFMDGKQACERMIRALELDPNL----YRIGQSKIFFR 802
Cdd:cd14908 644 cvKKMCKDLVKGVLSPAMVSMKNIpedtMQLGKSKVFMR 682
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
99-764 |
2.96e-131 |
|
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: 429.31 E-value: 2.96e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKgrkdhnippESPKPVKHQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQS---------STEQEGSDAVEIGKRILQTNPILESFGNAQTIRNDN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLsNGYIP-- 326
Cdd:cd14902 152 SSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPsf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 327 --IPGQQDKDN--FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNV 399
Cdd:cd14902 231 arKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 400 MEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDIA 471
Cdd:cd14902 311 DKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 472 GFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWF 551
Cdd:cd14902 391 GFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLM 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 552 PKATDKTFVEKLVQEQGTHSKFqkprqlkdkadfCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKD 631
Cdd:cd14902 468 PKGSNQALSTKFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGAD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 632 EiqniqracfydnitglhdppvdrivgldQVTGITETAfGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVRC 709
Cdd:cd14902 536 E----------------------------NRDSPGADN-GAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRC 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 710 IIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 764
Cdd:cd14902 587 LKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-763 |
2.21e-128 |
|
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: 420.90 E-value: 2.21e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 168 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvKHQGELERQLLQANPILESFGNAKTVK 245
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSK---------RRRAISGSELLSANPILESFGNARTLR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 246 NDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--NYR 318
Cdd:cd14895 146 NDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 319 FLSNG--YIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD---------------QAS 381
Cdd:cd14895 226 YISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSAS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 382 MPENTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTK 458
Cdd:cd14895 306 PSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 459 ----------RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPC 528
Cdd:cd14895 386 falnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVC 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 529 IDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWLMKNM 606
Cdd:cd14895 465 LEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 607 DPLNDNVATLLHQSSDKFVAELWKdeiqniqracFYD----NITGLHDPPVDRIVGLDQVTGItetafgsayktkkgmfr 682
Cdd:cd14895 541 DQPNAELFSVLGKTSDAHLRELFE----------FFKasesAELSLGQPKLRRRSSVLSSVGI----------------- 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 683 tvGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 762
Cdd:cd14895 594 --GSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL 671
|
.
gi 45382679 763 T 763
Cdd:cd14895 672 V 672
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-855 |
2.62e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.44 E-value: 2.62e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvkhqgelERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKI--------------QNAIMAANPVLEAFGNAKTIRNNNSSRFGRF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 256 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:PTZ00014 251 MQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:PTZ00014 331 FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTN 490
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITN 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 491 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTH 570
Cdd:PTZ00014 490 EMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNN 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 571 SKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiQNIQRAcfydnitglhd 650
Cdd:PTZ00014 567 PKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG--VEVEKG----------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 651 ppvdrivgldqvtgitetafgsayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 730
Cdd:PTZ00014 633 ------------------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQL 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 731 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLA 807
Cdd:PTZ00014 687 HSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELT 766
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 45382679 808 HLEEERDLKITDIIIFFQAVCRGYLARKAFAKKqqqlsaLKILQRNCA 855
Cdd:PTZ00014 767 QIQREKLAAWEPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-800 |
2.47e-123 |
|
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: 404.37 E-value: 2.47e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIppespkpvkhqgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI--------------QTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 338 ETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIK 412
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 413 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGTHS 571
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 572 KFqKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiQNIQRAcfydnitglhdp 651
Cdd:cd14876 459 KF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEG--VVVEKG------------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 652 pvdrivgldqvtgitetafgsayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 731
Cdd:cd14876 524 -----------------------KIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLH 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 732 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 800
Cdd:cd14876 579 ALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
99-802 |
2.41e-122 |
|
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: 403.23 E-value: 2.41e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnIPPESpkpvkhqgelerqlLQA-NPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV----LSVEK--------------LNAaLTVLEAFGNVRTALNGNATRFSQLFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:cd01386 143 LDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 336 FQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI--------- 406
Cdd:cd01386 223 FSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 407 ---LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN---- 479
Cdd:cd01386 303 qqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 480 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALL 545
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 546 DEECWFPKATDKTFVEKLVQEQG--THSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQ 619
Cdd:cd01386 462 DEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 620 SSDKFVAelwkdeiqniqracfydnitglhdppvdrivgldqvtgitetafgsayKTKKGMFRTVgqlyKESLTKLMATL 699
Cdd:cd01386 542 SQKETAA------------------------------------------------VKRKSPCLQI----KFQVDALIDTL 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 700 RNTNPNFVRCIIPNH--EKRAGK----------LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 767
Cdd:cd01386 570 RRTGLHFVHCLLPQHnaGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLT 649
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 45382679 768 PKGF-----MDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd01386 650 KKLGlnsevADERKAVEELLEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
99-764 |
2.24e-116 |
|
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: 384.97 E-value: 2.24e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 175 LCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipPESPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGK 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAAS----------PTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 255 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKD 334
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 335 NFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 412 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGT 569
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 570 HSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNIQRacfyDNITGLH 649
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQ----EEPSGQS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 650 DPPVdrivgldqvtgitetafgsayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 729
Cdd:cd14880 540 RAPV----------------------------LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQ 591
|
650 660 670
....*....|....*....|....*....|....*
gi 45382679 730 LRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 764
Cdd:cd14880 592 LEACGLVETIHISAAGFPIRVSHQNFVERYKLLRR 626
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
99-765 |
2.54e-115 |
|
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: 383.95 E-value: 2.54e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 177 TGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNN--------NNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 257 RINFDVTGYIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLAGAGehlKSDLLLEGFNN----YRFL---------- 320
Cdd:cd14906 153 KIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 321 ----SNGYIPIPGQQDKD-NFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---C 392
Cdd:cd14906 230 ksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 393 HLLGMNVMEFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQ 460
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 461 GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppG 540
Cdd:cd14906 390 NNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--G 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 541 VLALLDEECWFPKATDKTFVEKLVQE-QGTHSKFQkpRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQ 619
Cdd:cd14906 467 ILSLLDDECIMPKGSEQSLLEKYNKQyHNTNQYYQ--RTLA-KGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLA 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 620 SSDKFVAELWKDEIQNiqracfydnitglhdPPVDrivgldqvtgitetafgsayKTKKGMFRTVGQLYKESLTKLMATL 699
Cdd:cd14906 544 SSNFLKKSLFQQQITS---------------TTNT--------------------TKKQTQSNTVSGQFLEQLNQLIQTI 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 700 RNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 765
Cdd:cd14906 589 NSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-802 |
4.11e-110 |
|
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: 367.21 E-value: 4.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRkdhnippESPKPVKHQgeLERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN-------TSQRSIADK--IDENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 256 IRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPG 329
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 330 Q--QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAIL 407
Cdd:cd14875 232 KtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 408 tprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 567 QGTHSK-FQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNIQRAcfydni 645
Cdd:cd14875 465 WANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 646 tglhdppvdrivgldqvtgitetafgsayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 725
Cdd:cd14875 538 ------------------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 726 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSK 798
Cdd:cd14875 582 VGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTK 660
|
....
gi 45382679 799 IFFR 802
Cdd:cd14875 661 VFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
99-802 |
3.24e-109 |
|
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: 363.82 E-value: 3.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnippespkpvkhQGELERQLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 253 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQ 331
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 332 DKDNFQETMEAMHIMgFSHDEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILT 408
Cdd:cd14886 223 DQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIIT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 409 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd14886 302 KVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVeklvq 565
Cdd:cd14886 378 INYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFT----- 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 566 eQGTHSKFQKPRQLKDKA---DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfY 642
Cdd:cd14886 450 -SSCKSKIKNNSFIPGKGsqcNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD----------I 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 643 DNITGLhdppvdrivgldqvtgitetafgsayktKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLD 722
Cdd:cd14886 519 PNEDGN----------------------------MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYE 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 723 PHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIF 800
Cdd:cd14886 569 TKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVF 648
|
..
gi 45382679 801 FR 802
Cdd:cd14886 649 LR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-759 |
1.76e-108 |
|
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: 364.03 E-value: 1.76e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 168 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPPESPKPVKHQGELERQLLQANPILESFGNAKTVKND 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 248 NSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-----AGEHLKSDLLLEGFNNYRFLS 321
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 322 NGYIPI--PGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ-------- 389
Cdd:cd14899 240 QSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 390 --KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT---------- 457
Cdd:cd14899 320 ftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 458 ----KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE 533
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 534 RpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGTHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLN 610
Cdd:cd14899 479 H--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 611 DNVATLLHQSSDKFVAELwkdeiqniqracfydnITGLHDPPVDRIVGLDQVTGITETAFGSAYKTKkgmfrTVGQLYKE 690
Cdd:cd14899 557 ESAAQLLAGSSNPLIQAL----------------AAGSNDEDANGDSELDGFGGRTRRRAKSAIAAV-----SVGTQFKI 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 691 SLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRY 759
Cdd:cd14899 616 QLNELLSTVRATTPRYVRCIKPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
99-802 |
3.19e-95 |
|
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: 325.83 E-value: 3.19e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG--------------LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 251 RFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFlsngyipipgq 330
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 331 qDKDNFQETMEAMHIMGFSHDEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL------- 395
Cdd:cd14887 216 -DLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclss 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 396 GMNVMEFTRAILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 455
Cdd:cd14887 292 GLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 456 RTKR-------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 519
Cdd:cd14887 372 RSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 520 --DFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGTH 570
Cdd:cd14887 452 csAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 571 SKFQK--PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNdnvatllhqssdkfvaelwkDEIQNIQRACFYdnitgl 648
Cdd:cd14887 532 AKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATS--------------------DELERLFLACST------ 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 649 hdppVDRIVGLDQVTGItetafgSAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 728
Cdd:cd14887 586 ----YTRLVGSKKNSGV------RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHR 652
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 729 QLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIpKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14887 653 QLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
96-801 |
1.06e-94 |
|
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: 321.81 E-value: 1.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnippeSPKPVKhqgeLERQLLQANPILESFGNAKTVK 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTK----LSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 246 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFL--SNG 323
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 324 Y--IPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMN 398
Cdd:cd14879 223 HplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 399 VMEFtRAILTPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGF 473
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 474 EIF---ELNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALL 545
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGIL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 546 DEEC-WFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSS 621
Cdd:cd14879 449 DDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SP 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 622 DkFVAelwkdeiqniqracfydnitglhdppvdrivgldqvtgitetafgsayktkkgMFRTVGQLyKESLTKLMATLRN 701
Cdd:cd14879 519 D-FVN-----------------------------------------------------LLRGATQL-NAALSELLDTLDR 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 702 TNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERM 781
Cdd:cd14879 544 TRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCA 617
|
730 740
....*....|....*....|
gi 45382679 782 IRALELDPNLYRIGQSKIFF 801
Cdd:cd14879 618 RANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
100-766 |
2.58e-93 |
|
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: 315.30 E-value: 2.58e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDvtGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQET 339
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 340 MEAMHIMGFSHdeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14898 210 CSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 500 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgthSKFQKPRqL 579
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 580 KDKADFCII--HYAGKVDYKADEWLMKNMDplndnvatllhqssdkfvaelwkdeiqniqracfydnitglhdppvdriv 657
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNRE-------------------------------------------------- 459
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 658 gldqvtGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 737
Cdd:cd14898 460 ------KGQLLIFKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILE 533
|
650 660
....*....|....*....|....*....
gi 45382679 738 GIRICRQGFPNRIVFQEFRQRYEILTPNA 766
Cdd:cd14898 534 TIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
99-802 |
2.74e-90 |
|
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: 309.05 E-value: 2.74e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 176 CTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIppespkpvKHqgelerqllqANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTTFDSRF--------KH----------VNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 256 IRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQ 330
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 331 QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 487
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 488 YTNEKLQQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATD 556
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 557 KTFVEKL---VQEQGTHSKFQKPRQ------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVA 626
Cdd:cd14878 450 PNLPKKLqslLESSNTNAVYSPMKDgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 627 ELWKDEIQniqracfydnitglhdppvdrivgldqvtgitetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNF 706
Cdd:cd14878 530 HLFQSKLV------------------------------------------------TIASQLRKSLADIIGKLQKCTPHF 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 707 VRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALE 786
Cdd:cd14878 562 IHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVL 638
|
730
....*....|....*...
gi 45382679 787 LDPNL--YRIGQSKIFFR 802
Cdd:cd14878 639 QQCKLqgWQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
99-802 |
2.94e-87 |
|
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: 299.62 E-value: 2.94e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAhvasshkgrkdhnippespKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL-------------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 339 TMEAMHIMGFsHDEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14937 218 LMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 494 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF 573
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 574 QKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDeiqniqracfydnitglhdppV 653
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED---------------------V 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 654 DRIVGLDQVTGITetafgsaYKtkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14937 510 EVSESLGRKNLIT-------FK------------YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSL 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 734 GVLEGIRIcRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRAlELDPNLYRIGQSKIFFR 802
Cdd:cd14937 571 SIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
99-754 |
1.06e-77 |
|
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: 272.94 E-value: 1.06e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNippespkpvkhqgELERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT-------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 251 RFGKFIRINFD---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG-AGEHLKSDLLLEGFNNYRFL 320
Cdd:cd14884 144 RCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 321 --------------------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKkerntdqa 380
Cdd:cd14884 224 npdeshqkrsvkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 381 smpentvaqKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ 460
Cdd:cd14884 296 ---------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 461 GA-----------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCI 529
Cdd:cd14884 367 DEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 530 DLIERpanppgVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGTHSK-FQKPR--------QLKDKADFCIIHY 590
Cdd:cd14884 446 IFIAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 591 AGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAElwkdeiqniqracfydnitglhdppvdrivgldqvtgitetaf 670
Cdd:cd14884 520 AGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE------------------------------------------- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 671 gSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 750
Cdd:cd14884 557 -ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
....
gi 45382679 751 VFQE 754
Cdd:cd14884 636 PKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
100-789 |
3.65e-76 |
|
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: 266.98 E-value: 3.65e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipPESpKPVKHqgelerqLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGGG---------PET-DAFKH-------LAAAFTVLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 253 GKFIRINFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQ 330
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 331 QDKDNFQETMEAMHIMGFshdEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiL 407
Cdd:cd14881 212 EDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 408 TPRIK-VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFEL 478
Cdd:cd14881 284 TTRTHnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 479 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDK 557
Cdd:cd14881 360 SQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 558 TFVEKLVQEQGTHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHqssdkfvaelwkdeiqniQ 637
Cdd:cd14881 436 SYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY------------------K 496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 638 RACFYDNITGLHDppvdrivgldqvtgitetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:cd14881 497 QNCNFGFATHTQD------------------------------FHT-------RLDNLLRTLVHARPHFVRCIRSNTTET 539
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 789
Cdd:cd14881 540 PNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-767 |
4.72e-72 |
|
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: 254.80 E-value: 4.72e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 178 GESGAGKTENTKKVIQYLAHvasshkgrkdhniPPESPKPVKHQGELERqllqanpILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTS-------------QPKSKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDvTGYIVGANIE-TYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14874 131 LLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14874 210 KHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 414 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 494 QQLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSK 572
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 573 FQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNIQracfydnitglhdpp 652
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 653 vDRIVgldqvtgitetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14874 505 -DMIV-------------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKN 558
|
650 660 670
....*....|....*....|....*....|....*
gi 45382679 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 767
Cdd:cd14874 559 LLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-802 |
1.43e-70 |
|
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: 251.55 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnippespkpvkhqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNF 336
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 337 QETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 417 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 497 FNHTMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGTHSKF-Q 574
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 575 KPRQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVaeLWKDEIQNIQRAC-----FYDNITGLH 649
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL--FSRDGVFNINATVaelnqMFDAKNTAK 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 650 DPPVDRIVGL--------DQVTGITETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAG 719
Cdd:cd14905 512 KSPLSIVKVLlscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHL 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 720 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSK 798
Cdd:cd14905 592 TFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTK 669
|
....
gi 45382679 799 IFFR 802
Cdd:cd14905 670 IFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-801 |
7.77e-68 |
|
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: 245.27 E-value: 7.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDhnipPESPKPVKHqgELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD----SEGASGVLH--PIGQQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAgEH---LKSDLLL-EGFNNYRFLSNGyIPI 327
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 328 PGQ--QDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------L 395
Cdd:cd14893 236 ATNfaLDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 396 GMNVMEFTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG- 461
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 462 ---ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCI 529
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 530 DLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGTHSKFQKPRQLKDKAD------------FCIIHYAGKVDYK 597
Cdd:cd14893 476 QLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 598 ADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNIQRAcfydnitglhdppvdriVGLDQVT--GITETAFG---- 671
Cdd:cd14893 554 GKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSE-----------------KAAKQTEerGSTSSKFRksas 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 672 SAYKTKKGMFRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIV 751
Cdd:cd14893 617 SARESKNITDSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLT 695
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 45382679 752 FQEFRQRYeiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 801
Cdd:cd14893 696 YGHFFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-762 |
2.44e-60 |
|
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: 220.77 E-value: 2.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnippespkpvkhqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRG-------------------ATGRVESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG------ 329
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 330 ----QQDKDNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14882 219 rddpEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNS 480
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 481 FEQLCINYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDK 557
Cdd:cd14882 374 LEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 558 TFVEKLVQEQgtHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKDEIQNIQ 637
Cdd:cd14882 446 NYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNM 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 638 RACfydnitglhdppvdrivgldqvtgitetafgsayktkKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNH 714
Cdd:cd14882 521 RTL-------------------------------------AATFRAT------SLELLKMLSIGANSggtHFVRCIRSDL 557
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 45382679 715 EKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 762
Cdd:cd14882 558 EYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFL 605
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
121-265 |
6.27e-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: 6.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 200 SSHKGRKDHNIppeSPKPVKHQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 265
Cdd:cd01363 81 FNGINKGETEG---WVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
100-800 |
6.65e-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: 220.86 E-value: 6.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 179 ESGAGKTENTKKVIQYLAHVA--SSHKGRKDHNIPPESPKPV---KHQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgSRRLPTNLNDQEEDNIHNEentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 254 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLAGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 334 DNFQETMEAMHIMGFSHDEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 387
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 388 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 464
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 465 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 544
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 545 LDEECWFPKATDKTFVEKL-VQEQGTHSKF-QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 622
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSiIRKFSRNSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 623 KFVAELwkdeiqniqrACFYD-NITGlhdppvdRIVGLDQVTGITET--AFGSAYKTKKGMFRTvgqLYKESLTKLMATL 699
Cdd:cd14938 558 EYMRQF----------CMFYNyDNSG-------NIVEEKRRYSIQSAlkLFKRRYDTKNQMAVS---LLRNNLTELEKLQ 617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 700 RNTNPNFVRCIIPNHEKRA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQAC 778
Cdd:cd14938 618 ETTFCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKV 689
|
730 740
....*....|....*....|..
gi 45382679 779 ERMIRALELDPNLYRIGQSKIF 800
Cdd:cd14938 690 EALIKSYQISNYEWMIGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
882-1714 |
6.60e-39 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 159.49 E-value: 6.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFA----EAEEMRARLAAKKQELEEILHD 957
Cdd:COG1196 178 ERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLaklkELRKELEELEEELSRLEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 958 LESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1037
Cdd:COG1196 258 LQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1038 RIAECTSQLAEEEEKAKNLAKLKNKQEmmiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA 1117
Cdd:COG1196 338 ELEERETLLEELEQLLAELEEAKEELE---EKLSALLEELEELFEALREELAELEAELAEIRNELEELKREIESLEERLE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1118 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED---TLDTTA 1194
Cdd:COG1196 415 RLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSleaRLDRLE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1195 AQQElRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEE---------LSEQLEQAKRFKANLEKNKQGLESdnk 1265
Cdd:COG1196 495 AEQR-ASQGVRAVLEALESGLPGVYGPVAELIKVKEKYETALEAalgnrlqavVVENEEVAKKAIEFLKENKAGRAT--- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1266 elaceVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLR------------VELAEKANKLQNELDN----VSSLLEE 1329
Cdd:COG1196 571 -----FLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEpavrfvlgdtlvVDDLEQARRLARKLRIkyriVTLDGDL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1330 AEKKGI-----KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQL 1404
Cdd:COG1196 646 VEPSGSitggsRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKREL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1405 AEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqrqivsnlekkqkkf 1484
Cdd:COG1196 726 AALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEEL--------------------- 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1485 dqmlaeeKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKS 1564
Cdd:COG1196 785 -------EEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1565 KRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQnEEKKRMLVKQVRELEAELED--ERKQ 1642
Cdd:COG1196 858 LEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKL-RERLEELEAKLERLEVELPEleEELE 936
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1643 RALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLK 1714
Cdd:COG1196 937 EEYEDTLETELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKR 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1049-1889 |
2.69e-38 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 157.57 E-value: 2.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1049 EEEKAKNLAKLKNKQE------MMITDLEERLKKEEKTRQELEKAKrKLDGETTDLQDQIA-----ELQAQIEELKIQLA 1117
Cdd:COG1196 171 KERKEEAERKLERTEEnlerleDLLEELEKQLEKLERQAEKAERYQ-ELKAELRELELALLlaklkELRKELEELEEELS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1118 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQ 1197
Cdd:COG1196 250 RLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1198 ELRTKREQEVAELKKAIEEETKNhEAQIQEIRQRHATALEELSEQLEQAKrfkANLEKNKQGLESDNKELACEVKVLQQV 1277
Cdd:COG1196 330 EKIEALKEELEERETLLEELEQL-LAELEEAKEELEEKLSALLEELEELF---EALREELAELEAELAEIRNELEELKRE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1278 KAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQE 1357
Cdd:COG1196 406 IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSS 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1358 ETRQKLNLSSRIRQLEEEKNnlqeqqeeEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEG------LEENKKKLLKD 1431
Cdd:COG1196 486 LEARLDRLEAEQRASQGVRA--------VLEALESGLPGVYGPVAELIKVKEKYETALEAALGnrlqavVVENEEVAKKA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1432 MESLSQRLEEKAMaYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKnisarYAEERDRAEAEARE 1511
Cdd:COG1196 558 IEFLKENKAGRAT-FLPLDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVLGDTL-----VVDDLEQARRLARK 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1512 KETKALSLARA------------LEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQL 1579
Cdd:COG1196 632 LRIKYRIVTLDgdlvepsgsitgGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1580 EELEDELQATEDAKLRLEvnmqamkaQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKD 1659
Cdd:COG1196 712 EELERQLEELKRELAALE--------EELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1660 LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQ 1739
Cdd:COG1196 784 LEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1740 ERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQK--SENA 1817
Cdd:COG1196 864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEeyEDTL 943
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1818 RQQLERQNKELKAKLQELeGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQV 1889
Cdd:COG1196 944 ETELEREIERLEEEIEAL-GPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELDKEKRERFKET 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1075-1912 |
3.48e-38 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 157.18 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1075 KKEEKTRQELEKAKRKLDGettdLQDQIAELQAQIEELKIQLAKKEE--ELQAALargdeEAVQKNNALKVIRELQAQIA 1152
Cdd:COG1196 172 ERKEEAERKLERTEENLER----LEDLLEELEKQLEKLERQAEKAERyqELKAEL-----RELELALLLAKLKELRKELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1153 ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRH 1232
Cdd:COG1196 243 ELEEELSRLEEELEELQEELEEAEKEIEELKSELEEL----REELEELQEELLELKEEIEELEGEISLLRERLEELENEL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1233 ATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEK 1312
Cdd:COG1196 319 EELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1313 ANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKN 1392
Cdd:COG1196 399 LEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQR 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1393 LEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAM--------------------------AY 1446
Cdd:COG1196 479 LEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIKVKEKyetaleaalgnrlqavvveneevakkAI 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1447 DKLEKTK---------NRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLaeeKNISARY--AEERDRAEAEAREKETK 1515
Cdd:COG1196 559 EFLKENKagratflplDRIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAV---RFVLGDTlvVDDLEQARRLARKLRIK 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1516 ALSLARaleealeakeeferqnKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR 1595
Cdd:COG1196 636 YRIVTL----------------DGDLVEPSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRS 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1596 LEVNmqamkaqfERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRalavaakKKMEMDLKDLEGQIEAANKARDEAI 1675
Cdd:COG1196 700 LEDL--------LEELRRQLEELERQLEELKRELAALEEELEQLQSRL-------EELEEELEELEEELEELQERLEELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1676 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGK 1755
Cdd:COG1196 765 EELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKL 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1756 SALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQEL 1835
Cdd:COG1196 845 DELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERL 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1836 EG-------SVKSKFKATIST-LEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKAN 1907
Cdd:COG1196 925 EVelpeleeELEEEYEDTLETeLEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEVIEELD 1004
|
....*
gi 45382679 1908 ARMKQ 1912
Cdd:COG1196 1005 KEKRE 1009
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1047-1892 |
1.81e-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: 148.28 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1047 AEEEEKAKNL-AKLKNKQ-EMMITDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQ 1124
Cdd:TIGR02168 209 AEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1125 AALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKRE 1204
Cdd:TIGR02168 285 ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1205 QEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDNkelacevkvlqqvkaeSEHK 1284
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI----------------EELL 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1285 RKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEetrqKLN 1364
Cdd:TIGR02168 428 KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1365 LSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVdddlgtiegLEENKKKLLKDMESLSQRLEEKAM 1444
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV---------VVENLNAAKKAIAFLKQNELGRVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1445 AYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAeekNISARYAEERDRAEAEAREKETKAL------- 1517
Cdd:TIGR02168 575 FLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNALELAKKLRPGyrivtld 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1518 --------SLARALEEALEAKEEFERQNKQLRADMEdlmsskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDELQAT 1589
Cdd:TIGR02168 652 gdlvrpggVITGGSAKTNSSILERRREIEELEEKIE--------------ELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1590 EDAKLRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANK 1669
Cdd:TIGR02168 718 RKELEELSRQISALRKDLAR-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1670 ARDEAIKQLRKLQAQ--------------MKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARR 1735
Cdd:TIGR02168 797 ELKALREALDELRAEltllneeaanlrerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1736 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSA----- 1810
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtleea 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1811 ---AQKSENARQQLERQNKELKAKLQELeGSVK----SKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLK 1883
Cdd:TIGR02168 957 ealENKIEDDEEEARRRLKRLENKIKEL-GPVNlaaiEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERFK 1035
|
....*....
gi 45382679 1884 EVFMQVEDE 1892
Cdd:TIGR02168 1036 DTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1151-1866 |
2.32e-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: 144.81 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1151 IAELQEDLESEKASRNKAEKQKrDLSEELEALKTELEdTLDTTAAQQELRTKREQEvaelkkaieeetknheAQIQEIRQ 1230
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAERYK-ELKAELRELELALL-VLRLEELREELEELQEEL----------------KEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1231 RHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELA 1310
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1311 EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR 1390
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1391 KNLEKQMLALQAQLAEAKKK-VDDDLGTIEGLEENKKKLLKDM----ESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMV 1465
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKeLQAELEELEEELEELQEELERLeealEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1466 DLDHQRQI---VSNLEKKQKKF--------DQMLAEEKNISARYAEERDRAEAEAREKETKAL----SLARALEEALEAK 1530
Cdd:TIGR02168 497 LQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaiaFLKQNELGRVTFL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1531 EEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKL---------------- 1594
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgdlvr 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1595 --------RLEVNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE 1665
Cdd:TIGR02168 657 pggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1666 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1745
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1746 DEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGE--------------RSAA 1811
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnerasleealallRSEL 896
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1812 QKSENARQQLERQNKELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAK 1866
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYS 950
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1008-1889 |
5.04e-33 |
|
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: 140.20 E-value: 5.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1008 EAKIKKMEEEIllleDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEmmitDLEERLKKEEKtrQELEKA 1087
Cdd:TIGR02169 169 DRKKEKALEEL----EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKR----EYEGYELLKEK--EALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1088 KRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV-IRELQAQIAELQEDLESEKASRN 1166
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1167 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtknhEAQIQEIRQRHATALEELS---EQL 1243
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1244 EQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNV 1323
Cdd:TIGR02169 395 EKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1324 SSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRI-------RQLEEEKNNLQEQQEEEEEARKN---L 1393
Cdd:TIGR02169 475 KEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvAQLGSVGERYATAIEVAAGNRLNnvvV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1394 EKQMLALQA-QLAEAKKkvdddLGTIEGLEENKkklLKDMESLSQRLEEKA---MAYDKLE---KTKNRLQQELDDLMV- 1465
Cdd:TIGR02169 555 EDDAVAKEAiELLKRRK-----AGRATFLPLNK---MRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVv 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1466 -DLDHQRQIVSN----------LEKKQKKFDQMLAEEKNISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFE 1534
Cdd:TIGR02169 627 eDIEAARRLMGKyrmvtlegelFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1535 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQAR 1614
Cdd:TIGR02169 702 NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1615 DEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEE 1694
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1695 ARASRDEIFAQSKESEKKLKGLEAEILQLQEEfaaserarrhaeqeRDELADEIansasgkSALLDEKRRLEARIAQLEE 1774
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKE--------------RDELEAQL-------RELERKIEELEAQIEKKRK 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1775 ELEEEQSNMELLNERfrkttlqvdtlNSELAGERSAAQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATISTLEA 1852
Cdd:TIGR02169 918 RLSELKAKLEALEEE-----------LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLK 986
|
890 900 910
....*....|....*....|....*....|....*..
gi 45382679 1853 KIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQV 1889
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1177-1965 |
8.69e-32 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 136.38 E-value: 8.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1177 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIE--EETKNHEAQIQEIRqrHATALEELSEQLEQAKRFKANLE 1254
Cdd:COG1196 172 ERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEkaERYQELKAELRELE--LALLLAKLKELRKELEELEEELS 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1255 KNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKvtegERLRVELAEKANKLQNELDNVSSLLEEAEKKG 1334
Cdd:COG1196 250 RLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLEL----KEEIEELEGEISLLRERLEELENELEELEERL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1335 IKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLqeqqeeeeeaRKNLEKQMLALQAQLAEAKKKVDDD 1414
Cdd:COG1196 326 EELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSAL----------LEELEELFEALREELAELEAELAEI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1415 LGTIEGLEENkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNI 1494
Cdd:COG1196 396 RNELEELKRE-------IESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1495 SARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQL---RADMEDLMSSKDDVGKNV---------HELE 1562
Cdd:COG1196 469 LAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLpgvYGPVAELIKVKEKYETALeaalgnrlqAVVV 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1563 KSKRTLEQQVEEMRTQ------------LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQAR---------DEQNEEK 1621
Cdd:COG1196 549 ENEEVAKKAIEFLKENkagratflpldrIKPLRSLKSDAAPGFLGLASDLIDFDPKYEPAVRFVlgdtlvvddLEQARRL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1622 KRMLVKQVRELEAELEDERKQRALAVAAKKK-----MEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEAR 1696
Cdd:COG1196 629 ARKLRIKYRIVTLDGDLVEPSGSITGGSRNKrsslaQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELR 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1697 ASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1776
Cdd:COG1196 709 RQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKR 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1777 EEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgsvkskfkATISTLEAKIAQ 1856
Cdd:COG1196 789 QALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELE--------EELEELEKELEE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1857 LEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaEEEATRANASRRKLQR 1936
Cdd:COG1196 861 LKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKL---ERLEVELPELEEELEE 937
|
810 820
....*....|....*....|....*....
gi 45382679 1937 ELDDATEanEGLSREVSTLKNRLRRGGPI 1965
Cdd:COG1196 938 EYEDTLE--TELEREIERLEEEIEALGPV 964
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1216-1965 |
8.99e-31 |
|
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: 132.87 E-value: 8.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1216 EETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LESDNKELACEVKVLQQVKAESEHKRKKLDAQ 1291
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1292 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1371
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1372 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEkamaydkLEK 1451
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER-------LED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1452 TKNRLQQElddlmvdldhQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKE 1531
Cdd:TIGR02168 415 RRERLQQE----------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1532 EFERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRTLEQQV----------EEMRTQLEE-LEDELQA-----TEDAKLR 1595
Cdd:TIGR02168 485 AQLQARL---DSLERLQENLEGFSEGVKALLKNQSGLSGILgvlselisvdEGYEAAIEAaLGGRLQAvvvenLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1596 LE---------VNMQAMKAQFERDLQARDEQNEEKKRM-------LVKQVRELEAELED--------ERKQRALAVAAKK 1651
Cdd:TIGR02168 562 IAflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGflgvakdLVKFDPKLRKALSYllggvlvvDDLDNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1652 KMEMDLKDLEGQ-------------------------IEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1706
Cdd:TIGR02168 642 RPGYRIVTLDGDlvrpggvitggsaktnssilerrreIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1707 KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1786
Cdd:TIGR02168 722 EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1787 NERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkFKATISTLEAKIAQLEEQLEQEAK 1866
Cdd:TIGR02168 802 REALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLN 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1867 ERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA---- 1941
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAeale 960
|
810 820
....*....|....*....|....*..
gi 45382679 1942 ---TEANEGLSREVSTLKNRLRRGGPI 1965
Cdd:TIGR02168 961 nkiEDDEEEARRRLKRLENKIKELGPV 987
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
880-1654 |
1.43e-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: 129.02 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 880 RQEEELQakdeeLMKVKEKQTKVEAELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKK-QELEEILHDL 958
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLRlEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 959 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDR 1038
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1039 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAK 1118
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1119 KEEELQAALARGDE-----EAVQKNNALKVIRELQAQIAELQ---EDLESEKASRNKAEKQKRDLSEELEALKTELEDTL 1190
Cdd:TIGR02168 405 LEARLERLEDRRERlqqeiEELLKKLEEAELKELQAELEELEeelEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1191 DTTAAQQELRTKREQEVAELKKAIEEETKNHE---------AQIQEIRQRHATALEE---------LSEQLEQAKRFKAN 1252
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEGFSEGVKALLKNQSglsgilgvlSELISVDEGYEAAIEAalggrlqavVVENLNAAKKAIAF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1253 LEKNKQG--------------LESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKV------TEGERLRVELAE- 1311
Cdd:TIGR02168 565 LKQNELGrvtflpldsikgteIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVlvvddlDNALELAKKLRPg 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1312 -------------------KANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1372
Cdd:TIGR02168 645 yrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1373 EEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKT 1452
Cdd:TIGR02168 725 SRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1453 KNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEE 1532
Cdd:TIGR02168 805 LDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1533 FERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ-----ATEDAKLRLEVNMQAMKAQF 1607
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDnlqerLSEEYSLTLEEAEALENKIE 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1608 ERDLQARDEQNEEKKR---------MLVKQVRELEAELEDERKQRALAVAAKKKME 1654
Cdd:TIGR02168 965 DDEEEARRRLKRLENKikelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
875-1750 |
1.82e-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: 125.55 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 875 LLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFaeaeemrarlaakkQELEEI 954
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL--------------YALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 955 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQldeeegaRQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKL 1034
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESK-------LDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1035 MEDRIAECtsqlaeeeekaknlaklknkqemmitdleerlkkeektRQELEKAKRKLDgettDLQDQIAELQAQIEELKI 1114
Cdd:TIGR02168 370 LESRLEEL--------------------------------------EEQLETLRSKVA----QLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1115 QLakkeEELQAALARGDEEAVQKNNALKvirelQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttA 1194
Cdd:TIGR02168 408 RL----ERLEDRRERLQQEIEELLKKLE-----EAELKELQAELEELEEELEELQEELERLEEALEELREELE------E 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1195 AQQELRTKREQevaelkkaiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNK-ELACE--- 1270
Cdd:TIGR02168 473 AEQALDAAERE---------LAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaal 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1271 --------VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK--KGIKFAKD 1340
Cdd:TIGR02168 544 ggrlqavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1341 AASLESQLQDTQELlqeetRQKLNLSSRIRQLEEEK-----------NNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1409
Cdd:TIGR02168 624 GVLVVDDLDNALEL-----AKKLRPGYRIVTLDGDLvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1410 KVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL-DHQRQIVSNLEKKQKKFDQML 1488
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1489 AEEKNIsaryaeERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadMEDLMSSKDDVGKNVHELEKSKRTL 1568
Cdd:TIGR02168 779 EAEAEI------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER--LESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1569 EQQVEEMRTQLEELEDELQATEDAklrLEVNMQAMKAQFERDLQARDEQNEekkrmLVKQVRELEAELEDERKQRALAVA 1648
Cdd:TIGR02168 851 SEDIESLAAEIEELEELIEELESE---LEALLNERASLEEALALLRSELEE-----LSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1649 AKKKMEMDLKDLEGQIEaankardeaikqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQL----- 1723
Cdd:TIGR02168 923 KLAQLELRLEGLEVRID-------------NLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvnl 989
|
890 900
....*....|....*....|....*....
gi 45382679 1724 --QEEFAASERARRHAEQERDELADEIAN 1750
Cdd:TIGR02168 990 aaIEEYEELKERYDFLTAQKEDLTEAKET 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
877-1575 |
2.30e-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: 121.70 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 956
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 957 DLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKK------------MEEEILLLEDQ 1024
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkelqaeleeLEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1025 NSKFLKEKKLMEDRIAECTSQLAEEEEKaknLAKLKNKQEMMiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI-- 1102
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERE---LAQLQARLDSL-ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsv 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1103 -AELQAQIEelkiqlAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE----DLESEKASRNKAEKQKRDLSE 1177
Cdd:TIGR02168 532 dEGYEAAIE------AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAK 605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1178 ELEALKTELEDTLD------------TTAAQQELRTKREQEVAELKK-------AIEEETKNHEAQIQEIRQRhataLEE 1238
Cdd:TIGR02168 606 DLVKFDPKLRKALSyllggvlvvddlDNALELAKKLRPGYRIVTLDGdlvrpggVITGGSAKTNSSILERRRE----IEE 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1239 LSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQN 1318
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1319 ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQML 1398
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1399 ALQAQLAEAKKKVDDDLGTIEGLEENK-------KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQR 1471
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIeeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1472 QIVSNLEKKQKKFDQMLAE-EKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSS 1550
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKER 1001
|
730 740
....*....|....*....|....*
gi 45382679 1551 KDDVGKNVHELEKSKRTLEQQVEEM 1575
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
890-1771 |
4.67e-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: 120.94 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 890 EELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 969
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 970 QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIllledqnskflkeKKLMEDRIAECTSQLAEE 1049
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI-------------KDLGEEEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1050 EEKAKNLaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALAR 1129
Cdd:TIGR02169 300 EAEIASL-------ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1130 GDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1209
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1210 LKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLqqvkaesEHKRKKLD 1289
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEE-YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVH 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1290 AQVQELtAKVTEGERLRVELAekankLQNELDNVSSLLEEAEKKGIKFAKdaaslESQLQDTQELLQEETRQKLNLSSRI 1369
Cdd:TIGR02169 525 GTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1370 R------------QLEEEKNNLQEQQEEEEEARKNLEK--------QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLL 1429
Cdd:TIGR02169 594 SedgvigfavdlvEFDPKYEPAFKYVFGDTLVVEDIEAarrlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1430 KDMESLSQRLEEkamaydkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNISARYAEERDRA 1505
Cdd:TIGR02169 674 AELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDL 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1506 EAEAREKETKALSLARaleeALEAKEEFERQNKQLRADMEDLMSSKDDVGknVHELEKSKRTLEQQVEEMRTQLEELEDE 1585
Cdd:TIGR02169 747 SSLEQEIENVKSELKE----LEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQK 820
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1586 LQATEDAKLRLEVNMQAMKAQfERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE 1665
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1666 AANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKGLEAEILQLQEEFAASERARRHAEQ 1739
Cdd:TIGR02169 900 ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
890 900 910
....*....|....*....|....*....|..
gi 45382679 1740 ERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1128-1948 |
3.37e-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: 117.86 E-value: 3.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1128 ARGDEEAVQKNnalkvIRELQAQIAELQEDLESEKASRNKAEKQKrDLSEELEalktELEDTLdTTAAQQELRTKREQEV 1207
Cdd:TIGR02169 175 ALEELEEVEEN-----IERLDLIIDEKRQQLERLRREREKAERYQ-ALLKEKR----EYEGYE-LLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1208 AELKkAIEEETKNHEAQIQEIRQRHATALEELSEQleqAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKK 1287
Cdd:TIGR02169 244 RQLA-SLEEELEKLTEEISELEKRLEEIEQLLEEL---NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1288 LDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSS 1367
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1368 RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYD 1447
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1448 KLEKTKNRLQQELDdlmvDLDHQRQIVSNLEKKQKKFDQMLaeEKNISARYAEERDRAEAEarEKETKALSLAraleeal 1527
Cdd:TIGR02169 480 RVEKELSKLQRELA----EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA------- 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1528 eakeeferqnkqLRADMEDLMSSKDDVGKNVHELEKSK---RTLEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMK 1604
Cdd:TIGR02169 545 ------------AGNRLNNVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1605 AQFERDLQ--ARDE---QNEEKKRMLVKQVR--ELEAELEDE--------RKQRALAVAAKKKMEmDLKDLEGQIEAANK 1669
Cdd:TIGR02169 610 PKYEPAFKyvFGDTlvvEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1670 ARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIA 1749
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1750 NSASGKSALLDEKRRLEARIAQLEEELEEEQsnMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELK 1829
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1830 AKLQELEGSV------KSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQM 1903
Cdd:TIGR02169 847 EQIKSIEKEIenlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 45382679 1904 EKANARMKQLKRqLEEAEEEATRANASRRKLQRELDDATEANEGL 1948
Cdd:TIGR02169 927 EALEEELSEIED-PKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
880-1609 |
4.94e-26 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 117.51 E-value: 4.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 880 RQEEELQAKDEELM-----KVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 954
Cdd:COG1196 217 ELKAELRELELALLlaklkELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 955 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKkl 1034
Cdd:COG1196 297 IEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEEL-- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1035 mEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKI 1114
Cdd:COG1196 375 -EELFEALREELAELEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1115 QLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL-------- 1186
Cdd:COG1196 454 QLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPGVYGPVAELIkvkekyet 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1187 ---------------EDTLDTTAAQQELRTKREQEVA---------------------------------ELKKAIE--- 1215
Cdd:COG1196 534 aleaalgnrlqavvvENEEVAKKAIEFLKENKAGRATflpldrikplrslksdaapgflglasdlidfdpKYEPAVRfvl 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1216 --------EETKNHEAQIQEIRQR--------------------HATALEELSEQLEQAKRFKANLEKNKQGLESDNKEL 1267
Cdd:COG1196 614 gdtlvvddLEQARRLARKLRIKYRivtldgdlvepsgsitggsrNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSL 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1268 ACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQ 1347
Cdd:COG1196 694 KNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1348 LQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvdddlgtIEGLEENKKK 1427
Cdd:COG1196 774 LAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEE-------IEELEEKLDE 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1428 LLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEA 1507
Cdd:COG1196 847 LEEELEELEKELEELKEELEELEAEKEELEDELKEL-------EEEKEELEEELRELESELAELKEEIEKLRERLEELEA 919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1508 EAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1585
Cdd:COG1196 920 KLERLEVELPELEEELEEEYEDTLETELEREieRLEEEIEALGPVNLRAIEEYEEVEERYEELKSQREDLEEAKEKLLEV 999
|
810 820
....*....|....*....|....*
gi 45382679 1586 LQA-TEDAKLRLEVNMQAMKAQFER 1609
Cdd:COG1196 1000 IEElDKEKRERFKETFDKINENFSE 1024
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
875-1737 |
7.79e-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: 116.71 E-value: 7.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 875 LLQVTRQEEELQAKDEElmkVKEKQTKVEAELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 952
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 953 EILHDLESRVEEEEERNQILQNEKKKMqghiqdleEQLDEEEGARQKLQLEKVTAEakIKKMEEEILLLEDQNSKFLKEK 1032
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI--------KDLGEEEQLRVKEKIGELEAE--IASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1033 KLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEEL 1112
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1113 KIQLAKKEEELQaalaRGDEEAVQKNNALKVIRE-----------LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1181
Cdd:TIGR02169 405 KRELDRLQEELQ----RLSEELADLNAAIAGIEAkineleeekedKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1182 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE------AQIQEIRQRHATALEELS--------------- 1240
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvAQLGSVGERYATAIEVAAgnrlnnvvveddava 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1241 -EQLEQAKRFKAN----LEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELtakvteGERLRVELAEKANK 1315
Cdd:TIGR02169 561 kEAIELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1316 LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNNLQEQqeeeeeaRKNLEK 1395
Cdd:TIGR02169 635 LMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1396 QMLALQAQLAEAKKKvdddlgtIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1475
Cdd:TIGR02169 703 RLDELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1476 NLEKKQKKFDQMLAEEKNISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1555
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1556 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQARDEQNEEKKRMLVKQVRELEAE 1635
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1636 LEDERKQRALAVAAKKKMEMDLKDLEGQIeAANKARDEAIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKE 1708
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDE 990
|
890 900
....*....|....*....|....*....
gi 45382679 1709 SEKKLKGLEAEILQLQEEFAASERARRHA 1737
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1281-1961 |
1.65e-24 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 112.50 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1281 SEHKRKKLDAQvQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETR 1360
Cdd:COG1196 168 SKYKERKEEAE-RKLERTEENLERLEDLLEELEKQLEKLERQAEKAERYQELKAELRELELALLLAKLKELRKELEELEE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1361 QKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLE 1440
Cdd:COG1196 247 ELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1441 EKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQmlaEEKNISARYAEERDRAEAEAREKETKALSLA 1520
Cdd:COG1196 327 ELKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLE---ELEELFEALREELAELEAELAEIRNELEELK 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1521 RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNM 1600
Cdd:COG1196 404 REIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKEL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1601 QAMKAQFERdLQARDEQNEEKKRMLVKQVRELE------AEL--EDERKQRALAVAAKKKME----MDLKDLEGQIEAAN 1668
Cdd:COG1196 484 SSLEARLDR-LEAEQRASQGVRAVLEALESGLPgvygpvAELikVKEKYETALEAALGNRLQavvvENEEVAKKAIEFLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1669 KAR--------DEAIKQLRKLQAQMK-----------DYQRELEEA--RASRDEIFAQSKESEKKL---KGLEAEILQLQ 1724
Cdd:COG1196 563 ENKagratflpLDRIKPLRSLKSDAApgflglasdliDFDPKYEPAvrFVLGDTLVVDDLEQARRLarkLRIKYRIVTLD 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1725 EEF----------AASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeleeeqsnmelLNERFRKTT 1794
Cdd:COG1196 643 GDLvepsgsitggSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRS--------------LEDLLEELR 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1795 LQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKL 1874
Cdd:COG1196 709 RQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEE-LEELQERLEELEEELESLEEALAKLKEEIEELEEK 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1875 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVST 1954
Cdd:COG1196 788 RQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEE 867
|
....*..
gi 45382679 1955 LKNRLRR 1961
Cdd:COG1196 868 LEAEKEE 874
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
228-743 |
2.62e-24 |
|
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: 111.37 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 228 LLQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHIFYQ 296
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 297 LLAGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHDEILSMLKVVS 361
Cdd:cd14894 329 MVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 362 SVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVEALA 435
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 436 KATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLqqlfnh 499
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 500 tmfileqeeYQREGiewNFIDFGLDLQPCI-------DLIERPANPPGVLALLDEECWFPKAT----------DKTFVEK 562
Cdd:cd14894 563 ---------YAREE---QVIAVAYSSRPHLtardsekDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 563 LVQEQGthSKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDKFVAELWKD 631
Cdd:cd14894 631 IYDRNS--SRLPEPPRVLSNAKrhtpvllnvlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 632 EIQniqracfydnitglhdppvdrivgLDQVTGITETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCII 711
Cdd:cd14894 709 SSQ------------------------LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIR 763
|
570 580 590
....*....|....*....|....*....|..
gi 45382679 712 PNHEKRAGKLDPHLVLDQLRCNGVLEGIRICR 743
Cdd:cd14894 764 PNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1137-1912 |
1.55e-23 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 109.04 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1137 KNNALKVIRELQAQIAELQEDLESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1216
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1217 ETKNHEAQiqeiRQRHATALEELSEQLEQAKRFKANLEKNKQGLESD--NKELACEVKVLQQVKAESEHKR--------- 1285
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLNDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTIHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1286 -KKLDAQVQELTAKVTEGE-RLRVELAEKANK----LQNELDNVSSLLEEAEKKGIKFAKDAASLESQ---LQDTQELLQ 1356
Cdd:pfam15921 226 lRELDTEISYLKGRIFPVEdQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1357 EETRQKLnlSSRIRQLEEeknnlqeqqeeeeearknLEKQMLALQAQLAEAKKKVDDdlgTIEGLEenKKKLLKDMESLS 1436
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYED---KIEELE--KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1437 QRLEEkamayDKLEKTKNRLQQELDDLMVDLdHQRQIVSNLEKKQKK--FDQMLAEEKNISARYAEERDR-AEAEAREKE 1513
Cdd:pfam15921 361 ARTER-----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNKrlWDRDTGNSITIDHLRRELDDRnMEVQRLEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1514 TKALSlARALEEALEAKEEFERQNKQLR---ADMEDLMSSKDDVGKNVHELEKSKRTLE---QQVEEMRTQLEELEDELQ 1587
Cdd:pfam15921 435 LKAMK-SECQGQMERQMAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLEsseRTVSDLTASLQEKERAIE 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1588 AT--EDAKLRLEVNMQAMKAQFERdlqardeqNEEKkrmlvkQVRELEAELEDERKQRAlavAAKKKMEMDLKDLEGQIE 1665
Cdd:pfam15921 514 ATnaEITKLRSRVDLKLQELQHLK--------NEGD------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1666 -AANKARDEAIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERD 1742
Cdd:pfam15921 577 lVGQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1743 ELADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNERFRKTTLQVDTLNSELAGERSAAQ----KSENAR 1818
Cdd:pfam15921 657 QLLNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETTTNKLKMQLKSAQseleQTRNTL 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1819 QQLERQNKELKAKLQELEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERaaanKLVRRTEKKLKEVFMQVEDERRHADQ 1898
Cdd:pfam15921 716 KSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAG 790
|
810
....*....|....
gi 45382679 1899 YKEQMEKANARMKQ 1912
Cdd:pfam15921 791 ELEVLRSQERRLKE 804
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
997-1586 |
4.34e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 107.46 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 997 RQKLQLEKV-TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLK 1075
Cdd:PRK03918 152 RQILGLDDYeNAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1076 KEEKTRQELEKAKR---KLDGETTDLQDQIAELQAQIEELKiqlaKKEEELQAALARgdeeavqknnaLKVIRELQAQIA 1152
Cdd:PRK03918 232 ELEELKEEIEELEKeleSLEGSKRKLEEKIRELEERIEELK----KEIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1153 ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ---EVAELKKAIE--EETKNHEAQIQE 1227
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1228 IRQRHA-TALEELSEQLEQAKRFKANLEKN-------KQGLESDNKELACEVKVLQQVKAE--------SEHKRKKLdaq 1291
Cdd:PRK03918 377 LKKRLTgLTPEKLEKELEELEKAKEEIEEEiskitarIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKEL--- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1292 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK--KGIKFAKDAASLESQLQD-TQELLQEETRQKLNLSSR 1368
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1369 IRQLEEEKNNLQEQQEEEeearKNLEKQMLALQAQLAEAKKKVDDDLGTiegLEENKKKLLKDMESLSQRLEEKAMAYDK 1448
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKE---LEELGFESVEELEERLKELEPFYNEYLE 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1449 LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEErdraeaEAREKETKALSLARALEEALE 1528
Cdd:PRK03918 607 LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEYLELSRELAGLRA 680
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1529 AKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEqQVEEMRTQLEELEDEL 1586
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 ... |
1345-1961 |
1.07e-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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 103.32 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1345 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEeeeeARKNLEKQMLALQAQLAEAKKKVDDDLGTIE----- 1419
Cdd:pfam01576 11 EEELQKVKEKQQKAESELKELEKKHQQLCEEKNILAEQLQ----AETELFAEAEEMRARLAARKQELEEILHELEarlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1420 ------GLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEL----DDLMVDLDHQrqivSNLEKKQKKFDQMLA 1489
Cdd:pfam01576 87 eeersqQLQNEKKKMQQHIQDLEEQLEEEEAARQKLQLEKVTTEAKIkkmeEDILLLEDQN----NKLQKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1490 EeknISARYAEErdraeaearekETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRTLE 1569
Cdd:pfam01576 163 E---FTSNLAEE-----------EEKSKSLNKLKN-----------KHEAMISDLEDRLKKEE---KGRQELEKAKRKLE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1570 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAA 1649
Cdd:pfam01576 215 GESSDLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNAALKKLRELEAQLSELQEDLESERAARAKAEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1650 KKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKGLEAEILQLQEEFA 1728
Cdd:pfam01576 294 RRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1729 ASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGER 1808
Cdd:pfam01576 374 SLEKAKQALESENAELQAELRSLQQAKQDSEHKRKKLEGQLQELQSRLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1809 SAAQKSENARQQLERQNKELKAKLQElEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQ 1888
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSSRLRQLEDEKNSLQEQLEEEEEAKRNVERQLQTLQAQLSDLKKK 532
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1889 VEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:pfam01576 533 LEEDAGAVEALEEGRKRLQRELEALTQRLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
878-1765 |
4.44e-21 |
|
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: 101.20 E-value: 4.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 878 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 957
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 958 LESRVEEEEERNQILQNEKKKMQGHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1037
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1038 RIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLdgettdLQDQIAELQAQiEELKIQLA 1117
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEL------EKLQEKLEQLE-EELLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1118 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqQ 1197
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK----Q 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1198 ELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQV 1277
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGV 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1278 KAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQE 1357
Cdd:pfam02463 537 AVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1358 ETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQ 1437
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILR 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1438 RLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKnisaryaeerdrAEAEAREKETKAL 1517
Cdd:pfam02463 697 RQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1518 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE 1597
Cdd:pfam02463 765 EKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1598 VNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIK 1676
Cdd:pfam02463 845 EQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1677 QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERD-----ELADEIANS 1751
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYnkdelEKERLEEEK 1004
|
890
....*....|....
gi 45382679 1752 ASGKSALLDEKRRL 1765
Cdd:pfam02463 1005 KKLIRAIIEETCQR 1018
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
876-1451 |
5.49e-21 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 100.61 E-value: 5.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 876 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIL 955
Cdd:COG0419 218 LEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 956 HDLEsrveeeeeRNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1035
Cdd:COG0419 298 REIE--------ELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEER 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 EDRIaectsqLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLdgetTDLQDQIAELQAQIEELKIQ 1115
Cdd:COG0419 370 LEEL------EKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKEL----EELERELEELEEEIKKLEEQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1116 LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEdtldttaA 1195
Cdd:COG0419 440 INQLESKELMIAELAGAGEKCPVCGQELPEEHEKELLELYELELEELEEELSREKEEAELREEIEELEKELR-------E 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1196 QQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQrhatalEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ 1275
Cdd:COG0419 513 LEEELIELLELEEALKEELEEKLEKLENLLEELEE------LKEKLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1276 QVKA--ESEHKRKKLDAQVQELTAKVtEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLEsQLQDTQE 1353
Cdd:COG0419 587 ELEElrERLKELKKKLKELEERLSQL-EELLQSLELSEAENELEEAEEELESELEKLNLQAELEELLQAALE-ELEEKVE 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1354 LLQEETRQKLNLSSRIRQLEEEKNNLqeqqeeeeearKNLEKQMLALQAQLAEAKKKvdddLGTIEGLEENKKKLLKDME 1433
Cdd:COG0419 665 ELEAEIRRELQRIENEEQLEEKLEEL-----------EQLEEELEQLREELEELLKK----LGEIEQLIEELESRKAELE 729
|
570
....*....|....*...
gi 45382679 1434 SLSQRLEEKAMAYDKLEK 1451
Cdd:COG0419 730 ELKKELEKLEKALELLEE 747
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
877-1219 |
6.35e-21 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 100.56 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 956
Cdd:COG1196 675 ELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 957 DLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLME 1036
Cdd:COG1196 755 ELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1037 DRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQL 1116
Cdd:COG1196 835 EEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERL 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1117 AKKEEELQAALARGDEEAVQKNNALKVIR--ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldtta 1194
Cdd:COG1196 915 EELEAKLERLEVELPELEEELEEEYEDTLetELEREIERLEEEIEALGPVNLRAIEEYEEVEERYEELKSQRED------ 988
|
330 340
....*....|....*....|....*
gi 45382679 1195 aQQELRTKREQEVAELKKAIEEETK 1219
Cdd:COG1196 989 -LEEAKEKLLEVIEELDKEKRERFK 1012
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1751 |
2.56e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 880 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMR----ARLAAKKQELEEIL 955
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKkaeaARKAEEVRKAEELR 1194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 956 HDLESRVEEEEERnqiLQNEKKkmqghiqdleeqLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1035
Cdd:PTZ00121 1195 KAEDARKAEAARK---AEEERK------------AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 EDRIAECTSQLAEEEEKAKNLAKLKNKQEmmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK-- 1113
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEE--KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkk 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1114 IQLAKKEEELQAALARGDEEAVQKNnalkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTT 1193
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAA-------EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1194 AAQQELRTKREqevaELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKelACEVKV 1273
Cdd:PTZ00121 1411 KKAAAAKKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKK 1484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1274 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNEldnvssllEEAEKKGIKFAKDAASLESQLQDTQE 1353
Cdd:PTZ00121 1485 ADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEE 1556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1354 LLQEETRQKLNLSSRirqlEEEKNNLQEQQEEEEearKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDME 1433
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKK----AEEDKNMALRKAEEA---KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAE 1629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1434 SLSQRLEEKAMAYDKLEKTKNRLQQElddlmvdlDHQRQIVSNLEKKQKKFDQMLAEEknisARYAEERDRAEAEAREKE 1513
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKA--------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKE 1697
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1514 TKAlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAK 1593
Cdd:PTZ00121 1698 AEE---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1594 LRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmdlkdlegqieaankarDE 1673
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DS 1830
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1674 AIKQLRKLQAQMKDYQRELEEARASRDEIfaqSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANS 1751
Cdd:PTZ00121 1831 AIKEVADSKNMQLEEADAFEKHKFNKNNE---NGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
881-1457 |
4.42e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.83 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 881 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 960
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 961 RVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEILLLEDQNSkflkEKKLMEDRIA 1040
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1041 ECTSQLAEEEEKAKNLAKLKNKQEMM-----------ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQI 1109
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEELerlkkrltgltPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1110 EELKiqLAKKEEELQAALARGDEEAvqknnalKVIRELQAQIAELQEDLEsekasrnKAEKQKRDLSEELEALKTELEdt 1189
Cdd:PRK03918 429 EELK--KAKGKCPVCGRELTEEHRK-------ELLEEYTAELKRIEKELK-------EIEEKERKLRKELRELEKVLK-- 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1190 ldttaaqQELRTKREQEVAELKKAIEEETKNHEAQiqeirqrhatALEELSEQLEQAKRFKANLEKNKQGLESD---NKE 1266
Cdd:PRK03918 491 -------KESELIKLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1267 LACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgikfakdAASLES 1346
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE-------LKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1347 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARknLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKK 1426
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELEKRREEIKKTLEKLKEELE 704
|
570 580 590
....*....|....*....|....*....|.
gi 45382679 1427 KllkdmeslsqrLEEKAMAYDKLEKTKNRLQ 1457
Cdd:PRK03918 705 E-----------REKAKKELEKLEKALERVE 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
895-1512 |
5.28e-20 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 97.44 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 895 VKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLESRVEEEEERNQI 971
Cdd:PRK03918 146 SREKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 972 LQNEKKKMQGHiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEIllledqnskflkekKLMEDRIAECTSQLAEEEE 1051
Cdd:PRK03918 226 LEKEVKELEEL-----------KEEIEELEKELESLEGSKRKLEEKI--------------RELEERIEELKKEIEELEE 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1052 KAKNLAKLKNKQEMMITdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGD 1131
Cdd:PRK03918 281 KVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELE 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1132 EEAvqknNALKVIRELQAQIaelqEDLESEKASRNKaEKQKRDLsEELEALKTELEDTLDTTAAQqelRTKREQEVAELK 1211
Cdd:PRK03918 359 ERH----ELYEEAKAKKEEL----ERLKKRLTGLTP-EKLEKEL-EELEKAKEEIEEEISKITAR---IGELKKEIKELK 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1212 KAIEEETKNH-----------EAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLE---SDNKELACEVKVLQQV 1277
Cdd:PRK03918 426 KAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlKKESELIKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1278 KaESEHKRKKLDaqVQELTAKVTEGERLRvelaEKANKLQNELDNVSSLLEEAEkkgiKFAKDAASLESQLQDTQELLQE 1357
Cdd:PRK03918 506 K-ELEEKLKKYN--LEELEKKAEEYEKLK----EKLIKLKGEIKSLKKELEKLE----ELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1358 ETRQKLN--------LSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLaLQAQLAEAKKKVDDDLGTIEGLEENKKKLL 1429
Cdd:PRK03918 575 LLKELEElgfesveeLEERLKELEPFYNEYLELKDAEKELEREEKELKK-LEEELDKAFEELAETEKRLEELRKELEELE 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1430 K-----DMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK---KFDQMLAEEKNISARYAEE 1501
Cdd:PRK03918 654 KkyseeEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKeleKLEKALERVEELREKVKKY 733
|
650
....*....|.
gi 45382679 1502 RDRAEAEAREK 1512
Cdd:PRK03918 734 KALLKERALSK 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1202-1959 |
7.12e-20 |
|
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: 97.45 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1202 KREQEVAELKkAIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKAnLEKNKQGLESdnKELACEVKVLqqvkaes 1281
Cdd:TIGR02169 171 KKEKALEELE-EVEENIERLDLIIDEKRQQ----LERLRREREKAERYQA-LLKEKREYEG--YELLKEKEAL------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1282 EHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEE-AEKKGIKFAKDAASLESQLQDTQELLQEETR 1360
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1361 QKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLE 1440
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1441 EKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDqmlaeeknisaryaEERDRAEAEAREKETKALSLA 1520
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1521 raleealEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT----------- 1589
Cdd:TIGR02169 462 -------ADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvg 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1590 EDAKLRLEV----NMQAMKAQFERDLQARDEQNEEKK--RMLVKQVRELEAEledERKQRALAVAAKKKMEMDLKDLEGQ 1663
Cdd:TIGR02169 535 ERYATAIEVaagnRLNNVVVEDDAVAKEAIELLKRRKagRATFLPLNKMRDE---RRDLSILSEDGVIGFAVDLVEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1664 IEAANK--ARD----EAIKQLRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKGLEAEILQLQEEF 1727
Cdd:TIGR02169 612 YEPAFKyvFGDtlvvEDIEAARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1728 AASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGE 1807
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1808 RSAAQKSENARQQLER-----QNKELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKL 1882
Cdd:TIGR02169 771 EEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEV-SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1883 KEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1051-1432 |
7.54e-20 |
|
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: 97.05 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1051 EKAKNLAKLKNKQEMM---ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1127
Cdd:TIGR02168 674 ERRREIEELEEKIEELeekIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1128 ARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEV 1207
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1208 AELKKAIEEETKNHEaQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKK 1287
Cdd:TIGR02168 834 AATERRLEDLEEQIE-ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1288 LDAQVQELTAKV----TEGERLRVELAEKANKLQNEldnVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKL 1363
Cdd:TIGR02168 913 LRRELEELREKLaqleLRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNL 989
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1364 NLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQaqlAEAKKKVDDdlgTIEGLEENKKKLLKDM 1432
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID---REARERFKD---TFDQVNENFQRVFPKL 1052
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1011-1829 |
9.67e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1011 IKKMEEeiLLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAK-- 1088
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEea 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1089 RKLDGETTDLQDQIAELQAQIEELKiqlaKKEEELQAALARGDEEAVQKNNALKVIRELQAQIA-ELQEDLESEKASRNK 1167
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDAR----KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDArKAEEARKAEDAKKAE 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1168 AEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAK 1247
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1248 RFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRvELAEKANKLQNELDNVSSLL 1327
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKKA 1338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1328 EEAEKKGIKFAKDAASLESQLQDTQEllqEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEA 1407
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEE---KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAA 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1408 KKKVDDDLgtiegleENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEldDLMVDLDHQRQIVSNLEKKQKKFDQM 1487
Cdd:PTZ00121 1416 AKKKADEA-------KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKAD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1488 LAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlmSSKDDVGKNVHELEKSKRT 1567
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE---KKKADELKKAEELKKAEEK 1563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1568 leQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQ--NEEKKRMLVKQVRELEAELEDERKQRAL 1645
Cdd:PTZ00121 1564 --KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEakKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1646 AVAAKKKMEMDLKDlegqiEAANKARDEAIKQlrklqaQMKDYQRELEEARASRDEifaqSKESEKKLKGLEAEILQLQE 1725
Cdd:PTZ00121 1642 EAEEKKKAEELKKA-----EEENKIKAAEEAK------KAEEDKKKAEEAKKAEED----EKKAAEALKKEAEEAKKAEE 1706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1726 EFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELa 1805
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL- 1785
|
810 820
....*....|....*....|....
gi 45382679 1806 gersaAQKSENARQQLERQNKELK 1829
Cdd:PTZ00121 1786 -----DEEDEKRRMEVDKKIKDIF 1804
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1142-1738 |
1.04e-19 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 96.37 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1142 KVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSE-----ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1216
Cdd:COG0419 185 AKIEELEGQLSELLEDIEDLLEALEEELKELKKLEEiqeeqEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1217 ETKNHEAQIQEIRQ--RHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQE 1294
Cdd:COG0419 265 ELEALKIREEELREleRLLEELEEKIERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1295 LTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAK-------DAASLESQLQDTQELLQEETRQKLNLS- 1366
Cdd:COG0419 345 LEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEaiqelkeELAELSAALEEIQEELEELEKELEELEr 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1367 ------SRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTieGLEENKKKLLKDMESLSQRLE 1440
Cdd:COG0419 425 eleeleEEIKKLEEQINQLESKELMIAELAGAGEKCPVCGQELPEEHEKELLELYEL--ELEELEEELSREKEEAELREE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1441 ekamaYDKLEKTKNRLQQELDDLMVDldhQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLA 1520
Cdd:COG0419 503 -----IEELEKELRELEEELIELLEL---EEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRLQELKEL 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1521 RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSkRTLEQQVEEMRTQLEELEDELQATEdAKLRLEVNM 1600
Cdd:COG0419 575 LEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQS-LELSEAENELEEAEEELESELEKLN-LQAELEELL 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1601 QAMKAQFERDLQARDEQnEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmDLKDLEGQIEAANKARDEAIKQLRK 1680
Cdd:COG0419 653 QAALEELEEKVEELEAE-IRRELQRIENEEQLEEKLEELEQLEEELEQLREELE-ELLKKLGEIEQLIEELESRKAELEE 730
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1681 LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1738
Cdd:COG0419 731 LKKELEKLEKALELLEELREKLGKAGLRADILRNLLAQIEAEANEILSKLSLNRYDLR 788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
876-1515 |
1.88e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 96.36 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 876 LQVTRQEEELQaKDEELMKVKEKQTKVEAELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 954
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 955 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-----ARQKLQLEKVTAEAK----IKKMEEEILLLEDQN 1025
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkaeeKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1026 SKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1103
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1104 ELQAQIEEL--KIQLAKKEEEL--QAALARGDEEAVQKNNALKVIREL--QAQIAELQEDLESEKASRNKAEKQKRDlSE 1177
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAkkKAEEAKKADEAKKKAEEAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1178 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhataleelSEQLEQAKRFKANLEKNK 1257
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1258 qgleSDNKELACEVKVLQQVKAESEHKRKKldAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSllEEAEKKGIKF 1337
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1338 AKDAAslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNlekqmlalqaqlAEAKKKVDDDLGT 1417
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA------------AEALKKEAEEAKK 1703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1418 IEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISAR 1497
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 45382679 1498 YAEERDRAEAEAREKETK 1515
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 ... |
876-1687 |
2.93e-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: 95.42 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 876 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIL 955
Cdd:pfam02463 188 LIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 956 HDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLM 1035
Cdd:pfam02463 268 AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKtRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1115
Cdd:pfam02463 348 EIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK-LKEEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1116 LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT--- 1192
Cdd:pfam02463 427 EELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESkar 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1193 ------TAAQQELRTKREQEVAELKKAIEEETKNHEAQI--QEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESD- 1263
Cdd:pfam02463 507 sglkvlLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIstAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPk 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1264 -------------NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA 1330
Cdd:pfam02463 587 lklplksiavleiDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1331 EKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKK 1410
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKID 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1411 VDDDlgtiEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1490
Cdd:pfam02463 747 EEEE----EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1491 EKNISArYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQ 1570
Cdd:pfam02463 823 LIEQEE-KIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1571 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQN--EEKKRMLVKQVRELEAELEDERKQRALAVA 1648
Cdd:pfam02463 902 LEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEkeENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
810 820 830
....*....|....*....|....*....|....*....
gi 45382679 1649 AKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKD 1687
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning]; |
1324-1959 |
5.77e-19 |
|
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 224117 [Multi-domain] Cd Length: 1163 Bit Score: 94.40 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1324 SSLLEEAEkkGI-KFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEqqeeeeeaRKNLEKQMLALQA 1402
Cdd:COG1196 158 RKLIEEAA--GVsKYKERKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAER--------YQELKAELRELEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1403 QLAEAKkkvdddlgtIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQK 1482
Cdd:COG1196 228 ALLLAK---------LKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1483 KFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlmsskddvgknvhELE 1562
Cdd:COG1196 299 ELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKE--------------ELE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1563 KSKRTLEQQVEEMrtqLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVKQVRELEAELEDERKQ 1642
Cdd:COG1196 365 EKLSALLEELEEL---FEALREELAELEAELAEIRNELEELKREIE-SLEERLERLSERLEDLKEELKELEAELEELQTE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1643 RALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLE----- 1717
Cdd:COG1196 441 LEELNEELEELEEQLEELRDRLKELERELAELQEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLEALESGLPgvygp 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1718 -AEILQLQEEF-AASERARRHAEQ----ERDELADEI------ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMEL 1785
Cdd:COG1196 521 vAELIKVKEKYeTALEAALGNRLQavvvENEEVAKKAieflkeNKAGRATFLPLDRIKPLRSLKSDAAPGFLGLASDLID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1786 LNERFRK-------TTLQVDTLNS--ELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKatISTLEAKIAQ 1856
Cdd:COG1196 601 FDPKYEPavrfvlgDTLVVDDLEQarRLARKLRIKYRIVTLDGDLVEPSGSITGGSRNKRSSLAQKRE--LKELEEELAE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1857 LEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQR 1936
Cdd:COG1196 679 LEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQE 758
|
650 660
....*....|....*....|...
gi 45382679 1937 ELDDATEANEGLSREVSTLKNRL 1959
Cdd:COG1196 759 RLEELEEELESLEEALAKLKEEI 781
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1167-1748 |
6.12e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.98 E-value: 6.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1167 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR--QRHATALEELSEQLE 1244
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEklEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1245 QAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDaQVQELTAKVTEGERLRVELAEKANKLQNELDNVS 1324
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1325 SLLEEAEKKGIKFAKDAASLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEEKNNLQEQQ------------EEEEEAR 1390
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEELKKKLKELEKrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekelEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1391 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGL---------------EENKKKLLKD-MESLSQRLEEKAMAYDKLEKTKN 1454
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEyTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1455 RLqqelddlmVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFE 1534
Cdd:PRK03918 481 EL--------RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1535 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQAR 1614
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1615 DEQNEEKKR--MLVKQVRELEAELEDERKQRAlaVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQ---MKDYQ 1689
Cdd:PRK03918 633 EELAETEKRleELRKELEELEKKYSEEEYEEL--REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEleeREKAK 710
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1690 RELEEARASRDEIfaqsKESEKKLKGLEAEilqlqeefaaserARRHAEQERDELADEI 1748
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 ... |
973-1792 |
9.98e-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: 93.50 E-value: 9.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 973 QNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLA-EEEE 1051
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRdEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1052 KAKNLAKLKNKQEMMITDLEER------LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQA 1125
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENkeeekeKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1126 ALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLdTTAAQQELRTKREQ 1205
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL-ELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1206 EVAELKKAIEEETKNHEAQIQEIRQRHATALEE-LSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHK 1284
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1285 RKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAE-----KKGIKFAKDAASLESQLQDTQELLQEET 1359
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVenykvAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1360 RQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLAlqAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL 1439
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA--TLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1440 EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSL 1519
Cdd:pfam02463 650 KGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1520 AraleEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLR-LEV 1598
Cdd:pfam02463 730 A----QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEeLRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1599 NMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQL 1678
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1679 RKLQaQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASErarrhaEQERDELADEIANSASGKSAL 1758
Cdd:pfam02463 886 DELE-SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEP------EELLLEEADEKEKEENNKEEE 958
|
810 820 830
....*....|....*....|....*....|....
gi 45382679 1759 LDEKRRLEARIAQLEEELEEEQSNMELLNERFRK 1792
Cdd:pfam02463 959 EERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
878-1485 |
1.61e-18 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 92.52 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 878 VTRQEEELQAKDEELMKVKEK---------QTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKK 948
Cdd:COG0419 112 IADGKKDVNEKIEELLGLDKDtftrsvylpQGEFDAFLKSKPKERKEILDELFGLEKYEKLSELLKEVIKEAKAKIEELE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 949 QELEEILHDLESRVEEEEERnqiLQNEKKKMQghiQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKF 1028
Cdd:COG0419 192 GQLSELLEDIEDLLEALEEE---LKELKKLEE---IQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLE 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1029 LKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKN------KQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI 1102
Cdd:COG0419 266 LEALKIREEELRELERLLEELEEKIERLEELEReieeleEELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLESEL 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1103 AELQAQIEELKIQLAKKEEELQAALARGDEEAV----QKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEE 1178
Cdd:COG0419 346 EELAEEKNELAKLLEERLKELEERLEELEKELEkaleRLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERE 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1179 LEALKTELEDTLDTTAAQQELRTKREQEVAELKK-----------AIEEETKNHEAQIQEIRQR------HATALEELSE 1241
Cdd:COG0419 426 LEELEEEIKKLEEQINQLESKELMIAELAGAGEKcpvcgqelpeeHEKELLELYELELEELEEElsrekeEAELREEIEE 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1242 QLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLdaQVQELTAKVTEGERLRVELaEKANKLQNELD 1321
Cdd:COG0419 506 LEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKL--QLQQLKEELRQLEDRLQEL-KELLEELRLLR 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1322 NVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEetRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQ 1401
Cdd:COG0419 583 TRKEELEELRERLKELKKKLKELEERLSQLEELLQS--LELSEAENELEEAEEELESELEKLNLQAELEELLQAALEELE 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1402 AQLAEAKKKVDDDLGTIEGLEENKKKlLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1481
Cdd:COG0419 661 EKVEELEAEIRRELQRIENEEQLEEK-LEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLE 739
|
....
gi 45382679 1482 KKFD 1485
Cdd:COG0419 740 KALE 743
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
881-1460 |
2.49e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.03 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 881 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 960
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 961 RveeeeernqilqnekkkmqghiqdleeqldeEEGARQKLQLEKVTAEAkikkmeeeillLEDQNSKFLKEKKLMEDRIA 1040
Cdd:PRK02224 294 E-------------------------------RDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1041 ECTSQLAEEEEKAKNLAKlknkqemMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1120
Cdd:PRK02224 332 ECRVAAQAHNEEAESLRE-------DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1121 EELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLES-----------------EKASRNKAEKQKRDLSEELEALK 1183
Cdd:PRK02224 405 VDLGNAEDFLEELREERDELREREAELEATLRTARERVEEaealleagkcpecgqpvEGSPHVETIEEDRERVEELEAEL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1184 TELEDTLDTTAAqqelRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQakrfkanLEKNKQGLEsd 1263
Cdd:PRK02224 485 EDLEEEVEEVEE----RLERAEDLVEAEDRIERLEERREDLEELIAERRET-IEEKRERAEE-------LRERAAELE-- 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1264 nkelacevkvlqqvkAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNeLDNVSSLLEEAEKKGikfaKDAAS 1343
Cdd:PRK02224 551 ---------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE----DEIER 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1344 LESQLQDTQElLQEETRQKL-NLSSRIRQLEEE--KNNLQEQQEEEEEARKNLEKQMLALQaQLAEAKKKVDDDLGTIEG 1420
Cdd:PRK02224 611 LREKREALAE-LNDERRERLaEKRERKRELEAEfdEARIEEAREDKERAEEYLEQVEEKLD-ELREERDDLQAEIGAVEN 688
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 45382679 1421 LEENKKKLLKDMESLSQRLEEKAMAYDK---LEKTKNRLQQEL 1460
Cdd:PRK02224 689 ELEELEELRERREALENRVEALEALYDEaeeLESMYGDLRAEL 731
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1104-1725 |
2.63e-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: 91.62 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1104 ELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKasrNKAEKQKRDLSEELEALK 1183
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNK---DKINKLNSDLSKINSEIK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1184 TEledtldttaaqQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHaTALEELSEQLEQAKRFKANLEKNKQGLESD 1263
Cdd:TIGR04523 114 ND-----------KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKE-KELEKLNNKYNDLKKQKEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1264 NKELACEVKVLQQVKAESEHKRKKLDAQVQ---ELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKD 1340
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLKKKIQknkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1341 AASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR-----KNLEKQMLALQAQLAEAKKKVDDDL 1415
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLN 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1416 GTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDdlmvdldhqrqivsNLEKKQKKFDQMLAEEKNIS 1495
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK--------------NLESQINDLESKIQNQEKLN 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1496 ARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1575
Cdd:TIGR04523 408 QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1576 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRmLVKQVRELEAELE--DERKQRALAVAAKKKM 1653
Cdd:TIGR04523 488 QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNkdDFELKKENLEKEIDEK 566
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1654 EMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQE 1725
Cdd:TIGR04523 567 NKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1394-1961 |
3.50e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 91.64 E-value: 3.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1394 EKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAmaydklEKtknrlQQELDDLMVDLDHQRQI 1473
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE------ER-----REELETLEAEIEDLRET 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1474 VSNLEKKQKKFDQMLAEEKNISARYAEERD--RAEAEAREKETKALSLARALEEaleakeefeRQNKQLRADMEDLMSSK 1551
Cdd:PRK02224 267 IAETEREREELAEEVRDLRERLEELEEERDdlLAEAGLDDADAEAVEARREELE---------DRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1552 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAklrlevnmqamkaqferdlqaRDEQNEEkkrmlvkqVRE 1631
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREA---------------------VEDRREE--------IEE 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1632 LEAELEDERKQRALAvaakkkmEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDE---------- 1701
Cdd:PRK02224 389 LEEEIEELRERFGDA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpv 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1702 ----IFAQSKESEKKLKGLEAEILQLQEEFAASErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELE 1777
Cdd:PRK02224 462 egspHVETIEEDRERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1778 EEQSNMELLNERfrkttlqVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkfKATISTLEAKIAQL 1857
Cdd:PRK02224 534 EKRERAEELRER-------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES--LERIRTLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1858 EEQLEqeakeraaanklvRRTEKklKEVFMQVEDERRhadqykEQMEKANARMKQLKRQLEEAEEEATRANASR-----R 1932
Cdd:PRK02224 605 EDEIE-------------RLREK--REALAELNDERR------ERLAEKRERKRELEAEFDEARIEEAREDKERaeeylE 663
|
570 580
....*....|....*....|....*....
gi 45382679 1933 KLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEIGAVENELEE 692
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1301-1884 |
4.41e-18 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 90.98 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1301 EGERLRVELAEKANKLQNELDNVSSLLEEAEKKgikFAKDAASLESqlqdtqELLQEETRQKLNLSSRIRQLEEEKNNLQ 1380
Cdd:COG0419 168 KYEKLSELLKEVIKEAKAKIEELEGQLSELLED---IEDLLEALEE------ELKELKKLEEIQEEQEEEELEQEIEALE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1381 EQQEEEEEARKNLEKqmlaLQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEL 1460
Cdd:COG0419 239 ERLAELEEEKERLEE----LKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1461 DDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQL 1540
Cdd:COG0419 315 EELEELLEKLKSLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQEL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1541 RADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQAMKAQFERDLQARDEQNEE 1620
Cdd:COG0419 395 KEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKELMIA---ELAGAGEKCPVCGQELPEEH 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1621 KKRMLVKQVRELEaELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRD 1700
Cdd:COG0419 472 EKELLELYELELE-ELEEELSREKEEAELREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1701 EIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQ 1780
Cdd:COG0419 551 KLQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELEELRERLKELKKKLKELEERLSQLEELLQSLELSEAENELEE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1781 SNMELLNERfrkttlqvDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKA-TISTLEAKIAQLEE 1859
Cdd:COG0419 631 AEEELESEL--------EKLNLQAELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLeELEQLEEELEQLRE 702
|
570 580
....*....|....*....|....*
gi 45382679 1860 QLEQEAKERAAANKLVRRTEKKLKE 1884
Cdd:COG0419 703 ELEELLKKLGEIEQLIEELESRKAE 727
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1513 |
5.98e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 859 KLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAElEEMERKHQQLLEEKNILAEQLQAETELFAEAE 938
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 939 EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAK-----IKK 1013
Cdd:PTZ00121 1326 EAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaeeDKK 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1014 MEEEILLLEDQNSKFLKEKKLMED-RIAECTSQLAEEEEKAKnlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLD 1092
Cdd:PTZ00121 1406 KADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKAD---EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1093 GETTDLQDQIAELQAQIEELKiqlAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1172
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAK---KAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1173 RDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATAleelsEQLEQAKRFKAN 1252
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-----EELKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1253 LEKNKQGLESDNKElACEVKVLQQ---VKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEE 1329
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEenkIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1330 AEKKGIKFAKDAASLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALqaqlaeAKK 1409
Cdd:PTZ00121 1714 EKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV------IEE 1783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1410 KVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYdkLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1489
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLV--INDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENG 1861
|
650 660
....*....|....*....|....
gi 45382679 1490 EEKNISARYAEERDRAEAEAREKE 1513
Cdd:PTZ00121 1862 EDGNKEADFNKEKDLKEDDEEEIE 1885
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
930-1768 |
8.59e-18 |
|
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: 90.28 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 930 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKkmqghiQDLEEQLDEEEGARQKLQLEKVTAEA 1009
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELN------QLLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1010 KIKKMEEEILLLEDQNSKFLKEkklmedriaectsqlaeeeekakNLAKLKNKQEMmitdleerlkkEEKTRQELEKAKR 1089
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDA-----------------------DIETAAADQEQ-----------LPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1090 KLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKviRELQAQIAELQEDLESEKASRNKAE 1169
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAE--DDLQALESELREQLEAGKLEFNEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1170 KQkrdLSEELEALKTEledtLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQ--IQEIRQRHATALEELSEQLEQAK 1247
Cdd:pfam12128 440 YR---LKSRLGELKLR----LNQATATPELLLQLENFDERIERAREEQEAANAEVerLQSELRQARKRRDQASEALRQAS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1248 RFkanLEKNKQGLEsdnkelacEVKVLQQVKAESEHKRKKLDAQV-QELTAKVTEGERL-RVELAEKANKlqneldnvSS 1325
Cdd:pfam12128 513 RR---LEERQSALD--------ELELQLFPQAGTLLHFLRKEAPDwEQSIGKVISPELLhRTDLDPEVWD--------GS 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1326 LLEEAEKKGIKFAKDAASLESQLQDTQELlqeetRQKLNLSSRIRQLEEEKnnlqeqqeeeeeaRKNLEKQMLALQAQLA 1405
Cdd:pfam12128 574 VGGELNLYGVKLDLKRIDVPEWAASEEEL-----RERLDKAEEALQSAREK-------------QAAAEEQLVQANGELE 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1406 EAKKKVDDDLGTIEGLEENKKKLLKDMESLSqrleekamayDKLEKTKNRLQQELDDLMVDLDHQRQIvsnLEKKQKKFD 1485
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ---LDKKHQAWL 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1486 QMLAEEKnISARYAEERDRAEAEarekETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1565
Cdd:pfam12128 703 EEQKEQK-REARTEKQAYWQVVE----GALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1566 RTLEQQVEemrtqleeledelqatedaklRLEVNMQAMkAQFERDLQardEQNEEKKRMLVKQVRELEAELEDERKQRAL 1645
Cdd:pfam12128 778 RTLERKIE---------------------RIAVRRQEV-LRYFDWYQ---ETWLQRRPRLATQLSNIERAISELQQQLAR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1646 AVAAKKkmeMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQR-----ELEEARASRDEIFAQSKESEKKLKGLEAEI 1720
Cdd:pfam12128 833 LIADTK---LRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedaNSEQAQGSIGERLAQLEDLKLKRDYLSESV 909
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 45382679 1721 LQLQEEFAASERARRHAEQER--DELADEIANSASGKSALLDEKRRLEAR 1768
Cdd:pfam12128 910 KKYVEHFKNVIADHSGSGLAEtwESLREEDHYQNDKGIRLLDYRKLVPYL 959
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
1393-1961 |
9.32e-18 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 90.20 E-value: 9.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1393 LEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESlsQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQ 1472
Cdd:COG0419 169 YEKLSELLKEVIKEAKAKIEELEGQLSELLEDIEDLLEALEE--ELKELKKLEEIQEEQEEEELEQEIEALEERLAELEE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1473 IVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLrADMEDLMSSKD 1552
Cdd:COG0419 247 EKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEREIEELEEELEGLRALL-EELEELLEKLK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1553 DVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEE---KKRMLVKQV 1629
Cdd:COG0419 326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQElkeELAELSAAL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1630 RELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARdEAIKQLRKLQAQMKDYQRELEEArasrdeifaqskES 1709
Cdd:COG0419 406 EEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKE-LMIAELAGAGEKCPVCGQELPEE------------HE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1710 EKKLKGLEAEILQLQEEFAASERARRhAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNER 1789
Cdd:COG0419 473 KELLELYELELEELEEELSREKEEAE-LREEIEELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEK 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1790 frKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKaKLQELEGSVKSKFKAtISTLEAKIAQLEEQLEQEAKERA 1869
Cdd:COG0419 552 --LQLQQLKEELRQLEDRLQELKELLEELRLLRTRKEELE-ELRERLKELKKKLKE-LEERLSQLEELLQSLELSEAENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1870 AANKLVRRTEK--KLKEVFMQVEDERRHADQYKEQMEKANARMKQLK------RQLEEAEEEATRANASRRKLQRELDDA 1941
Cdd:COG0419 628 LEEAEEELESEleKLNLQAELEELLQAALEELEEKVEELEAEIRRELqrieneEQLEEKLEELEQLEEELEQLREELEEL 707
|
570 580
....*....|....*....|
gi 45382679 1942 TEANEGLSREVSTLKNRLRR 1961
Cdd:COG0419 708 LKKLGEIEQLIEELESRKAE 727
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1144-1769 |
2.74e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.56 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1144 IRELQAQIAELQEDLESEKAsrnkaEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEVAELKKAieeetknhea 1223
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIE-----EKEEKDLHERLNGLESELAEL---DEEIERYEEQREQARETRDEA---------- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1224 qiQEIRQRHATALEELSEqleqakrfkanleknkqglesdnkeLACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGE 1303
Cdd:PRK02224 240 --DEVLEEHEERREELET-------------------------LEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1304 RLRVELAEKANKLQNELDNVSSLLEEaekkgikFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqq 1383
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREE-------LEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA------- 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1384 eeeeearKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEEnkkkllkDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1463
Cdd:PRK02224 359 -------EELREEAAELESELEEAREAVEDRREEIEELEE-------EIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1464 MVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS-ARYAEERDRAEAEAREKETKAlslaraleealeakeeferqnkQLRA 1542
Cdd:PRK02224 425 REREAELEATLRTARERVEEAEALLEAGKCPEcGQPVEGSPHVETIEEDRERVE----------------------ELEA 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1543 DMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELqatedaklrlevnmqamkAQFERDLQARDEQNEEKK 1622
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELI------------------AERRETIEEKRERAEELR 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1623 rmlvKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIeAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1702
Cdd:PRK02224 544 ----ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL-AELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1703 FAQSKESEKKLKGLEAEILQLQEEFaasERARRHAEQERDELADEIANSASGKSALLDEKR-RLEARI 1769
Cdd:PRK02224 619 AELNDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEI 683
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1008-1597 |
4.76e-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: 87.38 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1008 EAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKA 1087
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1088 KRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEEL---QAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKAS 1164
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1165 RNKAEKQKRDLSEELEALKTELEDTldttaAQQELRTKREQEvaELKKAIEEETKnheaqiqeirqrhataleelseQLE 1244
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNT-----QTQLNQLKDEQN--KIKKQLSEKQK----------------------ELE 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1245 QAKRFKANLEKNKQGLESdnkelacEVKVLQQVKAESEHKR-----KKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1319
Cdd:TIGR04523 278 QNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKElkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1320 LDNVSSlleEAEKKGIKFAKDAASLESQLQDTQELLQEetrqKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1399
Cdd:TIGR04523 351 LTNSES---ENSEKQRELEEKQNEIEKLKKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1400 LQAQLAEAKKKVDDDLGTIEGLEENK-------KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQ 1472
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDsvkeliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1473 IVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSS 1550
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieELKQTQKSLKKK 583
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 45382679 1551 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE 1597
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS 630
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1021-1833 |
7.63e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 87.46 E-value: 7.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1021 LEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLkkeEKTRQELEKAKrkldgetTDLQD 1100
Cdd:pfam15921 94 LNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQL---QNTVHELEAAK-------CLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1101 QIAELQAQIEELKIQLAKKE---EELQAALARGDEEAVQK---NNALKVI--RELQAQIAELQEDLESEKASrnkAEKQK 1172
Cdd:pfam15921 164 MLNDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyeHDSMSTIhfRSLGSAISKILRELDTEISY---LKGRI 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1173 RDLSEELEALKTELEDTLDTTAAQQELRtkreqevaelkkaIEEETKNHEAQIQEIRQRHATALEE---LSEQL----EQ 1245
Cdd:pfam15921 241 FPVEDQLEALKSESQNKIELLLQQHQDR-------------IEQLISEHEVEITGLTEKASSARSQansIQSQLeiiqEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1246 AKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSS 1325
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSE---LREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1326 LLEEAEKKgikfakdaasLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARK----NLEKQMLALQ 1401
Cdd:pfam15921 385 DLHKREKE----------LSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSecqgQMERQMAAIQ 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1402 AQlAEAKKKVDDDLGTIEGLEENKKKLLKDmeslsqrLEEKAMAYDKLEKTknrlqqeLDDLMVDLDHQRQIV----SNL 1477
Cdd:pfam15921 455 GK-NESLEKVSSLTAQLESTKEMLRKVVEE-------LTAKKMTLESSERT-------VSDLTASLQEKERAIeatnAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1478 EKKQKKFDQMLAEEKNISaryaEERDRAEAEAREKETKALSLARALEEALEakeeferqnkqLRADMEDLMSSKDDVGKN 1557
Cdd:pfam15921 520 TKLRSRVDLKLQELQHLK----NEGDHLRNVQTECEALKLQMAEKDKVIEI-----------LRQQIENMTQLVGQHGRT 584
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1558 VHELEKSKRTLEQQVEEMRTQLEELEdELQATEDAKLrlevnmqamkaqfeRDLQARDEQNEEKKRMLVKQVRELEAELE 1637
Cdd:pfam15921 585 AGAMQVEKAQLEKEINDRRLELQEFK-ILKDKKDAKI--------------RELEARVSDLELEKVKLVNAGSERLRAVK 649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1638 DERKQRALAVAAKKKMEMDLKDLEGQIEAANK----ARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1713
Cdd:pfam15921 650 DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA 729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1714 KGLEAEIlqlqeefaASERARRHAEQERDELADE-IANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRK 1792
Cdd:pfam15921 730 MGMQKQI--------TAKRGQIDALQSKIQFLEEaMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERR 801
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 45382679 1793 ttLQVDTLNSELAGERSAAQKSEnARQQLERQNKE-LKAKLQ 1833
Cdd:pfam15921 802 --LKEKVANMEVALDKASLQFAE-CQDIIQRQEQEsVRLKLQ 840
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1030-1625 |
2.29e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 85.48 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1030 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL-----------------EKAKRKLD 1092
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELetleaeiedlretiaetEREREELA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1093 GETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1172
Cdd:PRK02224 279 EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1173 RDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKAIEEETKnheaqiqeirqrhatALEELSEQLEQAKRFKAN 1252
Cdd:PRK02224 359 EELREEAAELESELEEA-------REAVEDRREEIEELEEEIEELRE---------------RFGDAPVDLGNAEDFLEE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1253 LEKNKQGLESDNKELACEVKVLQQVKAESEhkrKKLDA-QVQELTAKVTEGERLRV--ELAEKANKLQNELDNVSSLLEE 1329
Cdd:PRK02224 417 LREERDELREREAELEATLRTARERVEEAE---ALLEAgKCPECGQPVEGSPHVETieEDRERVEELEAELEDLEEEVEE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1330 AEKKgIKFAKDAASLESQLQDTQEllqeetrQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1409
Cdd:PRK02224 494 VEER-LERAEDLVEAEDRIERLEE-------RREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1410 KVDDDLGTIEGLEenkkkllkdmeslsQRLEEKAMAYDKLEKtknrlqqeLDDLMVDLDHQRQIVSNLEKKQKKFDQMLA 1489
Cdd:PRK02224 566 EAEEAREEVAELN--------------SKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1490 EEKNisaRYAEERDRAEAEAREKETKALSlaraleealeakeeferqnkQLRADMEDLMSSKDDVGKNVHELEKSKRTLE 1569
Cdd:PRK02224 624 ERRE---RLAEKRERKRELEAEFDEARIE--------------------EAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1570 QQ---VEEMRTQLEELEDELQATEDAKLRLEV------NMQAMKAQFERDLQARDEqnEEKKRML 1625
Cdd:PRK02224 681 AEigaVENELEELEELRERREALENRVEALEAlydeaeELESMYGDLRAELRQRNV--ETLERML 743
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1016-1747 |
2.60e-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: 85.41 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1016 EEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEeeKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKaKRKLDGET 1095
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQ-KREAQEEQ 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1096 TDLQDQIAELQAQIEELKIQLAKKEE-----ELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEK 1170
Cdd:TIGR00618 256 LKKQQLLKQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVK 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1171 QKRDLSEELEALKTELedtldttaaQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEEL---SEQLEQAK 1247
Cdd:TIGR00618 336 QQSSIEEQRRLLQTLH---------SQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLqslCKELDILQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1248 RFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNeLDNVSSLL 1327
Cdd:TIGR00618 407 REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1328 EEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnLQEQQEEEEEARKNLEKQMLALQAQLAEA 1407
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR----GEQTYAQLETSEEDVYHQLTSERKQRASL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1408 KKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQrQIVSNLEKKQKKFDQM 1487
Cdd:TIGR00618 562 KEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE-QDLQDVRLHLQQCSQE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1488 LAEEKNISARYAEERdraeaeAREKETKALSLARALEEaleakeeferQNKQLRADMEDLMSSKddvgknVHELEKSKRT 1567
Cdd:TIGR00618 641 LALKLTALHALQLTL------TQERVREHALSIRVLPK----------ELLASRQLALQKMQSE------KEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1568 LEQQVEEMRTQLEELEdelqatEDAKLRLEVNMQAMKAQfeRDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1647
Cdd:TIGR00618 699 LAQCQTLLRELETHIE------EYDREFNEIENASSSLG--SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1648 AAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKGLEAEILQL 1723
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQ 850
|
730 740
....*....|....*....|....
gi 45382679 1724 QEEFAASERARRHAEQERDELADE 1747
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQL 874
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
890-1546 |
7.09e-16 |
|
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: 84.00 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 890 EELMKVKEKQTKVEAELEEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD----------LE 959
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQ---ENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 960 SRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLE----KVTAEAKIKKMEEEILLLEDQNSKFLKEKklm 1035
Cdd:pfam05483 162 ETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQaenaRLEMHFKLKEDHEKIQHLEEEYKKEINDK--- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQIEE 1111
Cdd:pfam05483 239 EKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEED 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1112 LKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:pfam05483 319 LQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1192 TTAAQ----QELRT-----------------------KREQEVAELKKAIEEETKNHEAQIQEIR---QRHATALEELSE 1241
Cdd:pfam05483 399 FKNNKevelEELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQLTAIKtseEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1242 QLEQAKRFKANLEKNKQGLESDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerLRVELAEKAN 1314
Cdd:pfam05483 479 ELEKEKLKNIELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1315 KLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1394
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1395 KQMLALQAQLAEAKKKVDDDLGTIEGLEENKK----KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQ 1470
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1471 rqivsnLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1546
Cdd:pfam05483 716 ------YDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1087-1462 |
1.54e-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: 83.19 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1087 AKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1166
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1167 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIE----EETKNHEAQIQEIRQRHATALEELSEQ 1242
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1243 LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDN 1322
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1323 VSSLLEEAEKKgikfAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK----QML 1398
Cdd:TIGR02169 901 LERKIEELEAQ----IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvNML 976
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1399 ALQaQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAM-AYDKLEKTKNRLQQELDD 1462
Cdd:TIGR02169 977 AIQ-EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMeAFEAINENFNEIFAELSG 1040
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
878-1308 |
1.63e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 878 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQELEE 953
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLtgltPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 954 ILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEILLLEDQNSKFLKEKK 1033
Cdd:PRK03918 406 EISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAE--LKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1034 LMEDRIAEcTSQLAEEEEKAKNLAKLKNK-QEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQdQIAELQAQIEEL 1112
Cdd:PRK03918 484 ELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAEL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1113 KIQLAKKEEELQAALARGDEEavqknnALKVIRELQAQIAELqEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT 1192
Cdd:PRK03918 562 EKKLDELEEELAELLKELEEL------GFESVEELEERLKEL-EPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1193 TA-AQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLEsDNKELACEV 1271
Cdd:PRK03918 635 LAeTEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKEL 713
|
410 420 430
....*....|....*....|....*....|....*..
gi 45382679 1272 KVLQQVKAESEHKRKKldaqVQELTAKVTEGERLRVE 1308
Cdd:PRK03918 714 EKLEKALERVEELREK----VKKYKALLKERALSKVG 746
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
882-1468 |
2.03e-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: 82.38 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKnilaEQLQAETELFaeaeemrarlaakKQELEEILHDLESR 961
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQK----EELENELNLL-------------EKEKLNIQKNIDKI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 962 VEEEEERNQILQNEKKKMQGH------IQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEkklm 1035
Cdd:TIGR04523 193 KNKLLKLELLLSNLKKKIQKNkslesqISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ---- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 edrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEErlKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQ 1115
Cdd:TIGR04523 269 ---LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN--QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1116 LAKKEEELQAALARG---DEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN----KAEKQKRDLSEELEALKTELED 1188
Cdd:TIGR04523 344 ISQLKKELTNSESENsekQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLEskiqNQEKLNQQKDEQIKKLQQEKEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1189 TLDTTAAQQELRTKREQEVAELKKAI---EEETKNHEAQIQEIRQrhataleELSEQLEQAKRFKANLEKNKQGLESDNK 1265
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDsvkELIIKNLDNTRESLET-------QLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1266 ELacevKVLQQVKAESEHKRKKLDAQVQELTAKVtegERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLE 1345
Cdd:TIGR04523 497 EL----KKLNEEKKELEEKVKDLTKKISSLKEKI---EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKE 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1346 -SQLQDTQELLQEETRQKLNLssrIRQLEEEKNNLQEQQEeeeearkNLEKQMLALQAQLAEAKKKVdddlgtiEGLEEN 1424
Cdd:TIGR04523 570 iEELKQTQKSLKKKQEEKQEL---IDQKEKEKKDLIKEIE-------EKEKKISSLEKELEKAKKEN-------EKLSSI 632
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 45382679 1425 KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLD 1468
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKID 676
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1274-1960 |
2.36e-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: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1274 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVEL--AEKANKLQNELDNV-----SSLLEEAEKKGIKFAKDAASLES 1346
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRRERekAERYQALLKEKREYegyelLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1347 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR-KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENK 1425
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1426 KKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqrqiVSNLEKKQKKFDQMLAEEKnisaryaEERDRA 1505
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL----------RAELEEVDKEFAETRDELK-------DYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1506 EAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDE 1585
Cdd:TIGR02169 395 EKLKREIN----ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1586 LQATEDAKLRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELEAELE------------DERKQRALAVAAKKKM 1653
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRL 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1654 EMDLKDLEGQIEaankardEAIKQLRKLQA---------QMKDYQRELEEAR------------------------ASRD 1700
Cdd:TIGR02169 550 NNVVVEDDAVAK-------EAIELLKRRKAgratflplnKMRDERRDLSILSedgvigfavdlvefdpkyepafkyVFGD 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1701 EIFAQSKESEKKLKG------LEAEILQ---------LQEEFAASERARRHAEQERdeLADEIANSASGKSALLDEKRRL 1765
Cdd:TIGR02169 623 TLVVEDIEAARRLMGkyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQR--LRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1766 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgSVKSKFKA 1845
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE-EDLHKLEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1846 TISTLEAKIA-----QLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEA 1920
Cdd:TIGR02169 780 ALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL 859
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 45382679 1921 EEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1960
Cdd:TIGR02169 860 NGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1001-1598 |
3.29e-15 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 82.07 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1001 QLEKVTAEAKiKKMEeeiLLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLA--------KLKNKQEMMITDLEE 1072
Cdd:pfam15921 246 QLEALKSESQ-NKIE---LLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQsqleiiqeQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1073 RLKKEEKTRQELEKAKRKLDGettdlqdqiaelqaQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIA 1152
Cdd:pfam15921 322 LESTVSQLRSELREAKRMYED--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLH 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1153 ELQEDLESEKASRNKAEKQKRDLSEELEALKTELED------TLDT--TAAQQELRTKREQEVAELKKAIE--EETKNHE 1222
Cdd:pfam15921 388 KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDrnmevqRLEAllKAMKSECQGQMERQMAAIQGKNEslEKVSSLT 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1223 AQIQEIRQRHATALEELSEQ---LEQAKR----FKANLEKNKQGLESDNKELA-------CEVKVLQQVKAESEHKRkkl 1288
Cdd:pfam15921 468 AQLESTKEMLRKVVEELTAKkmtLESSERtvsdLTASLQEKERAIEATNAEITklrsrvdLKLQELQHLKNEGDHLR--- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1289 daQVQeltakvTEGERLRVELAEKANK---LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNL 1365
Cdd:pfam15921 545 --NVQ------TECEALKLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1366 SSRIRQLEEEKNNLQEQQEEEEEARknlEKQMLALQaqlaEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAma 1445
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAG---SERLRAVK----DIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS-- 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1446 yDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ-KKFDQMLAEEKNISARyaeerdRAEAEAREKETKALSLAraLE 1524
Cdd:pfam15921 688 -EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDgHAMKVAMGMQKQITAK------RGQIDALQSKIQFLEEA--MT 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1525 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRT-------QLEELEDELQATEDAKLRLE 1597
Cdd:pfam15921 759 NANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQESVRLK 838
|
.
gi 45382679 1598 V 1598
Cdd:pfam15921 839 L 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1311-1885 |
6.61e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 80.88 E-value: 6.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1311 EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEAR 1390
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1391 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKL--LKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLD 1468
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1469 HQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAeaREKETKALSLARALEEaleakeeferQNKQLRADMEDLm 1548
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKE----------ELERLKKRLTGL- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1549 sSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQARDEQNEEKKRMLvkq 1628
Cdd:PRK03918 385 -TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHRKELL--- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1629 vRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKAR--DEAIKQLRKLQAQMKDYQRE-LEEARASRDEIFAQ 1705
Cdd:PRK03918 455 -EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1706 SKESEKKLKGLEAEILQLQE---EFAASERARRHAEQERDELADEIANSASGKSALLDEK-------------------- 1762
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkelepfyneylelkdaeke 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1763 -RRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGErsaaqKSENARQQLERQNKELKAKLQELEGsVKS 1841
Cdd:PRK03918 614 lEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE-----EYEELREEYLELSRELAGLRAELEE-LEK 687
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 45382679 1842 KFKATISTLeakiaqleEQLEQEAKERAAANKLVRRTEKKLKEV 1885
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 ... |
1161-1906 |
6.98e-15 |
|
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: 80.79 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1161 EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1240
Cdd:pfam02463 170 KKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1241 EQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKAN-KLQNE 1319
Cdd:pfam02463 250 QEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKkKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1320 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDtQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLA 1399
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEE-LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1400 LQAQLAEAKKKVDDDLGTIEglEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1479
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEE--LEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1480 KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEferqnKQLRADMEDLMSSKDDVGKNVH 1559
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE-----NYKVAISTAVIVEVSATADEVE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRTQLEELEDELqateDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1639
Cdd:pfam02463 562 ERQKLVRALTELPLGARKLRLLIPKLK----LPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFA---QSKESEKKLKGL 1716
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKkkeQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1717 EAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTL- 1795
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLk 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1796 -QVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAAnKL 1874
Cdd:pfam02463 798 aQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLL-KE 876
|
730 740 750
....*....|....*....|....*....|..
gi 45382679 1875 VRRTEKKLKEVFMQVEDERRHADQYKEQMEKA 1906
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
834-1480 |
1.91e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 834 RKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEaeleemERKH 913
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 914 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqghiqdleeqldee 993
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 994 egARQKLQLEKVTAEAkiKKMEEEILLLEDQNSKFLKEKKLMEDRIAEcTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1073
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1074 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQIEELKIQ----LAKKEEELQAALARGDEEAVQKNNALKVIRELQA 1149
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1150 QIAELQEDLESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKAIEEETKNHEAQIQEir 1229
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1230 qrhatalEELSEQLEQAKRFKAnlEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKvtEGERLRVEL 1309
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK--KIAHLKKEE 1766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1310 AEKANKLQNELDNV--SSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKN---NLQ 1380
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNmqlEEA 1846
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1381 EQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESlsqRLEEKAMAYDKLEKTKNRLQQEl 1460
Cdd:PTZ00121 1847 DAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIER---EIPNNNMAGKNNDIIDDKLDKD- 1922
|
650 660
....*....|....*....|
gi 45382679 1461 DDLMVDLDHQRQIVSNLEKK 1480
Cdd:PTZ00121 1923 EYIKRDAEETREEIIKISKK 1942
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
845-1395 |
2.46e-14 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 223496 [Multi-domain] Cd Length: 908 Bit Score: 79.03 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 845 SALKILQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVK---EKQTKVEAELEEMERKHQQLLEEKN 921
Cdd:COG0419 246 EEKERLEELKARLLEIESLELEALKIREEELRELERLLEELEEKIERLEELEreiEELEEELEGLRALLEELEELLEKLK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 922 ILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESrveeeeernqilqnekkkmqghiqdleeqldeeegarqKLQ 1001
Cdd:COG0419 326 SLEERLEKLEEKLEKLESELEELAEEKNELAKLLEERLK--------------------------------------ELE 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1002 LEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTR 1081
Cdd:COG0419 368 ERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELEEEIKKLEEQINQLESKE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1082 QELEKAKRKLDGETTDLQDQIAELQAQIEELkiqLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESE 1161
Cdd:COG0419 448 LMIAELAGAGEKCPVCGQELPEEHEKELLEL---YELELEELEEELSREKEEAELREEIEELEKELRELEEELIELLELE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1162 KASRNKAEKQKRDLSEELEALKTELEDTLdtTAAQQELRTKREQEVAELKKAIEEETKN--HEAQIQEIRQRhataLEEL 1239
Cdd:COG0419 525 EALKEELEEKLEKLENLLEELEELKEKLQ--LQQLKEELRQLEDRLQELKELLEELRLLrtRKEELEELRER----LKEL 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1240 SEQLEQAKRFKANLEKNKQGLESDNKELAcevkvLQQVKAESEHKRKKLDAQVQELTAKvtegERLRVELAEKANKLQNE 1319
Cdd:COG0419 599 KKKLKELEERLSQLEELLQSLELSEAENE-----LEEAEEELESELEKLNLQAELEELL----QAALEELEEKVEELEAE 669
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1320 LDNVSSLLEEaEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK 1395
Cdd:COG0419 670 IRRELQRIEN-EEQLEEKLEELEQLEEELEQLREELEELLKKLGEIEQLIEELESRKAELEELKKELEKLEKALEL 744
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
871-1332 |
2.75e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 871 KVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 950
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 951 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEdqnsKFLK 1030
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1031 EKKLMEDRIAECTSQLAEEEEKaknlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIA--ELQAQ 1108
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1109 IEELKIQLAKKEEELQAALARGDEEAVQKnnalkvIRELQAQIAELQEDLESEKASRNKA---EKQKRDLSEELEALKTE 1185
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKAEEYEKLKEK------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELLKE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1186 LEDTLDTTAAQQELRTKreqevaELKKAIEE--ETKNHEAQIQEIRQRhataLEELSEQLEQAkrfkanlEKNKQGLESD 1263
Cdd:PRK03918 579 LEELGFESVEELEERLK------ELEPFYNEylELKDAEKELEREEKE----LKKLEEELDKA-------FEELAETEKR 641
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1264 NKELACEVKVLQQVKAESEHKRK-----KLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1332
Cdd:PRK03918 642 LEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1010-1836 |
2.99e-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: 78.94 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1010 KIKKMEEEILLLEDQNSKFLKEKKLMEDRiaecTSQLAEEEEKA-----KNLAKLKNKQEMMITDLEERLKKEEKTRQEL 1084
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKD----NSELELKMEKVfqgtdEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1085 EKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQA--------ALARGDEEAVQKNNALKVIRELQAQIAELQE 1156
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1157 DLESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKAIEEETKNHEAQIQEIRQR 1231
Cdd:TIGR00606 412 QLCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1232 HATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESehkRKKLDAQVQELTAKVTEGERLRVELAE 1311
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGY 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1312 KANK--LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRI------RQLEEEKNNLQEQQ 1383
Cdd:TIGR00606 569 FPNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEI 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1384 EEEEEARKNLEKQMLALQAQLAEAKKK-------VDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRL 1456
Cdd:TIGR00606 649 EKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEM 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1457 QQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQ 1536
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKI 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1537 NKQL-RADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNmqamKAQFERDLQARd 1615
Cdd:TIGR00606 809 AQQAaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE----KLQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1616 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKardeaikqlrKLQAQMKDYQRELEEA 1695
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1696 RASRDEIFAQSKES-EKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1774
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1775 ELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELE 1836
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1132-1950 |
3.24e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1132 EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK 1211
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1212 KaIEEETKNHEA--QIQEIRQRHATALEELSEQLEQAKRfkanleknkqglESDNKELACEVKVLQQVKAESehKRKKLD 1289
Cdd:PTZ00121 1110 K-AEEARKAEEAkkKAEDARKAEEARKAEDARKAEEARK------------AEDAKRVEIARKAEDARKAEE--ARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1290 AQVQELTAKVTEGER-LRVELAEKANKLQ--NELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqKLNLS 1366
Cdd:PTZ00121 1175 AKKAEAARKAEEVRKaEELRKAEDARKAEaaRKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAE---EERNN 1251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1367 SRIRQLEEEKNNLQEQQEEEEEArknlEKQMLALQAQLAEAKKKVDddlgtieglEENKKKLLKDMESLSQRLEEKAMAy 1446
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKA----EEARKADELKKAEEKKKAD---------EAKKAEEKKKADEAKKKAEEAKKA- 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1447 DKLEKTKNRLQQELDDLMvdldhqrqivSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETkalslARALEEA 1526
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAK----------KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE-----AKKKADA 1382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1527 LEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRtLEQQVEEMRT--QLEELEDELQATEDAKLRLEvnmqamk 1604
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEKKKadEAKKKAEEAKKADEAKKKAE------- 1454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1605 aqferdlQARDEQNEEKKRMLVKQVRELEAELEDERKqralAVAAKKKMEMDLKDLEgQIEAANKARDEAIKQLRKLQAQ 1684
Cdd:PTZ00121 1455 -------EAKKAEEAKKKAEEAKKADEAKKKAEEAKK----ADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKAEEAK 1522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1685 MKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAASERARRhAEQERDELADEIANSASGKSALLDEKRR 1764
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELK--KAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1765 LEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQlERQNKELKAKLQELEGSVKSKFK 1844
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAEEAKKAEEDKKKAE 1678
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1845 ATISTLEAKiAQLEEQLEQEAKERAAANKLVRRTEKKLK----------EVFMQVEDERRHADQYKEQMEKANARMKQLK 1914
Cdd:PTZ00121 1679 EAKKAEEDE-KKAAEALKKEAEEAKKAEELKKKEAEEKKkaeelkkaeeENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
810 820 830
....*....|....*....|....*....|....*.
gi 45382679 1915 RQLEEAEEEATRANASRRKLQRELDDATEANEGLSR 1950
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRR 1793
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
881-1724 |
3.51e-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: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 881 QEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNIlAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 960
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI-VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKS 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 961 RVEEEEERN-QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK---KLME 1036
Cdd:TIGR00606 277 RKKQMEKDNsELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQgrlQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1037 DRIAE-------------CTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIA 1103
Cdd:TIGR00606 357 DRHQEhirardsliqslaTRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1104 ELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELqedlesEKASRNKAEKQKRDLSEELEALK 1183
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEK 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1184 TELEDTLDTTAAQQElRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA---NLEKNKQGL 1260
Cdd:TIGR00606 511 ADLDRKLRKLDQEME-QLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQT 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1261 ESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerlrvelAEKANKLQNELDNVSSLLEEAEKKGIKFAKD 1340
Cdd:TIGR00606 590 RDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1341 AASLESQLQDTQE-------LLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1413
Cdd:TIGR00606 662 TAVYSQFITQLTDenqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1414 DLGTIEGLEENKKKLLKDMESLSQRLEEKamayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKN 1493
Cdd:TIGR00606 742 KEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1494 ISARYAEERDRAEAEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRTLEQQVE 1573
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLV 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1574 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQN---EEKKRMLVKQVRELEAELED-ERKQRALAVAA 1649
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDY 971
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1650 KKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQ 1724
Cdd:TIGR00606 972 LKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
875-1623 |
4.05e-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: 78.47 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 875 LLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 950
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 951 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFL 1029
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1030 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQI 1109
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1110 EELKIQLAKKEEELQAALARGDE-EAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELED 1188
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVEnYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1189 TLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1268
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1269 CEVKVLQQVKAESEHKRKKLDAQVQELTA--KVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLES 1346
Cdd:pfam02463 677 EIQELQEKAESELAKEEILRRQLEIKKKEqrEKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1347 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKK 1426
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1427 KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAE 1506
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1507 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRTLEQQVEEMRTQLEELEDEL 1586
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 45382679 1587 QATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR 1623
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1236-1890 |
5.90e-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: 77.37 E-value: 5.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1236 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1315
Cdd:TIGR04523 42 LKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1316 LQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK 1395
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1396 QMLALQAQLAEAKKKVDDdlgtIEGLEENKKKLLKDMESLSQRLEEKAmayDKLEKTKNRLQQELDDlmvdldhQRQIVS 1475
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQEINEKT---TEISNTQTQLNQLKDE-------QNKIKK 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1476 NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKE---TKAL-SLARALEEALEAKEEFERQNKQLRADMEDLMSsk 1551
Cdd:TIGR04523 268 QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwNKELkSELKNQEKKLEEIQNQISQNNKIISQLNEQIS-- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1552 dDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlqardeQNEEKKRMLVKQVRE 1631
Cdd:TIGR04523 346 -QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ--------NQEKLNQQKDEQIKK 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1632 LEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1711
Cdd:TIGR04523 417 LQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1712 KLKGLEAEILQLqeefaaserarrhaEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR 1791
Cdd:TIGR04523 497 ELKKLNEEKKEL--------------EEKVKDLTKKI-------SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1792 KTTL--QVDTLNSELagersaaQKSENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERA 1869
Cdd:TIGR04523 556 KENLekEIDEKNKEI-------EELKQTQKSLKKKQEEKQELIDQKE-KEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660
....*....|....*....|.
gi 45382679 1870 AANKLVRRTEKKLKEVFMQVE 1890
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVK 648
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
838-1463 |
2.85e-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: 75.39 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 838 AKKQQQLSALKILqRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELmkvkekqTKVEAELEEMERKHQQLL 917
Cdd:TIGR00618 219 ERKQVLEKELKHL-REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-------RAQEAVLEETQERINRAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 918 EEKNILAEQlQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGAR 997
Cdd:TIGR00618 291 KAAPLAAHI-KAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIRE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 998 QKLQleKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE 1077
Cdd:TIGR00618 370 ISCQ--QHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1078 EKTRQ-------ELEKAKRKLDGETTDLQDQ-----------------IAELQAQIEELKIQLAKKEEELQAA------- 1126
Cdd:TIGR00618 448 TCTAQceklekiHLQESAQSLKEREQQLQTKeqihlqetrkkavvlarLLELQEEPCPLCGSCIHPNPARQDIdnpgplt 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1127 --LARGDEEAVQKNNALKVIR----ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1200
Cdd:TIGR00618 528 rrMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1201 TKREQEVAELKKAIEEETKN-----HEAQIQEIRQRHATALEELSEQLEQAKRFKANL---EKNKQGLESDNKELACEVK 1272
Cdd:TIGR00618 608 DMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLTQERVREHALsirVLPKELLASRQLALQKMQS 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1273 VLQQVKAESEHKRKKLDAqVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDA--ASLESQLQD 1350
Cdd:TIGR00618 688 EKEQLTYWKEMLAQCQTL-LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVlkARTEAHFNN 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1351 TQELL------QEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLgtiegleEN 1424
Cdd:TIGR00618 767 NEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL-------EE 839
|
650 660 670
....*....|....*....|....*....|....*....
gi 45382679 1425 KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL 1463
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
948-1724 |
3.01e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 435022 [Multi-domain] Cd Length: 1112 Bit Score: 75.52 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 948 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQGHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEILL 1020
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1021 LEDQNS--KFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL------------EK 1086
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLNDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstihfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1087 AKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlargdeeavQKNNALKVIRELQAQIAELqedleSEKASrn 1166
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1167 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQA 1246
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1247 KRF---KANLEKNKQGLESD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNE 1319
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1320 LDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQqeeeeearknlEKQMLA 1399
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1400 LQAQLAEAKKKVDDDLGTIEGLeENKKKLLKDMESLSQRLEEKAMAYDKLEKTknrLQQELDDLMVDLDHQRQIVSNLEK 1479
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHL-KNEGDHLRNVQTECEALKLQMAEKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1480 KQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKDDVG 1555
Cdd:pfam15921 591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELN 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1556 KNVHELEKSKRTLEQQVEEMRTQLEELEDELQAtedAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVK--QVRELE 1633
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKS---AQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKrgQIDALQ 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1634 AELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1713
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDII 827
|
810
....*....|.
gi 45382679 1714 KGLEAEILQLQ 1724
Cdd:pfam15921 828 QRQEQESVRLK 838
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1007-1517 |
3.09e-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: 75.24 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1007 AEAKIKKMEeeiLLLEDQNSKFLKEKKLMEDRiaectSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEktrQELEK 1086
Cdd:pfam10174 190 AEMQLGHLE---VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQM 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1087 AKRKLDGETTDLQDQIAELQA----------QIEELKIQLAKKEEELQAALARGDEEAVQKNNA---LKVIRE------- 1146
Cdd:pfam10174 259 LKTNGLLHTEDREEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTKLETLTNQNSDCkqhIEVLKEsltakeq 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1147 ----LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKAIE---EETK 1219
Cdd:pfam10174 339 raaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLR 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1220 NHEAQIQEIRQRHA----------TALEELSEQLEQAKRFKANLEKNKqglESDNKELACEVKVLQQvkaesehKRKKLD 1289
Cdd:pfam10174 412 DKDKQLAGLKERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLK 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1290 AQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELlQEETRQKLNLSSRI 1369
Cdd:pfam10174 482 EKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNA-EEAVRTNPEINDRI 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1370 RQLEEEknnLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvDDDLGTIEGL------EENKKKL-LKDMESLSQR---- 1438
Cdd:pfam10174 561 RLLEQE---VARYKEESGKAQAEVERLLGILREVENEKNDK-DKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKkgaq 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1439 -LEEKAMAYDklEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKAL 1517
Cdd:pfam10174 637 lLEEARRRED--NLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1417-1960 |
4.97e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1417 TIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNI-- 1494
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLeg 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1495 SARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQV-- 1572
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIke 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1573 -EEMRTQLEELEDELQATEDAKLRLEVNMQAmkaqFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKqralavaAKK 1651
Cdd:PRK03918 333 lEEKEERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK-------AKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1652 KMEMDLKDLE---GQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASR--DEIFAQSKESEKKLKGLEAEILQLQEE 1726
Cdd:PRK03918 402 EIEEEISKITariGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1727 FAASERARRHAEQER--DELADEIANSASGKSALLDEKRRLEARiaqleeeleeeqsNMELLNERFRKTTLQVDTLNSEL 1804
Cdd:PRK03918 482 LRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAE-------------EYEKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1805 agerSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEqLEQEAKERAAANKLVRRTEKKLKE 1884
Cdd:PRK03918 549 ----EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKK 623
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1885 VFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRANASRRKLQRELDDATEANEGLSREVSTLKNRLR 1960
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
879-1493 |
3.07e-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: 71.98 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 879 TRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 958
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 959 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ-----------------LEKVTAEAKIKKMEEEILLL 1021
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQknidkiknkllklelllSNLKKKIQKNKSLESQISEL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1022 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNlakLKNKQEMMITDLEERlkkeektRQELEKAKRKLDgettDLQDQ 1101
Cdd:TIGR04523 224 KKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ---LKDEQNKIKKQLSEK-------QKELEQNNKKIK----ELEKQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELKIQlakKEEELqaalargdeeavqknnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1181
Cdd:TIGR04523 290 LNQLKSEISDLNNQ---KEQDW--------------------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1182 LKTELEDTLDTTAAQQELRTKREQEVAELKKAIE---EETKNHEAQIQEIRQrhataleelseQLEQAKRFKANLEKNKQ 1258
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1259 GLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFA 1338
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1339 KDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQeeeeearKNLEKQMLALQAQL--AEAKKKVDDDLG 1416
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNK 568
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1417 TIEGLEENKKKLLKDMESLSQRLeekamayDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKN 1493
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
891-1463 |
3.65e-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: 72.18 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 891 ELMKVKEKQTKVEAELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAA---KKQELEEILHDLESRVE 963
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKAltgKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 964 EEEERNQILQNEKKKMQghiqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEI-LLLEDQNSKFLKEKKLMEDRIAEC 1042
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI----------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGEL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1043 TSQLAE---EEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQIEELKIQL 1116
Cdd:pfam12128 450 KLRLNQataTPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQL 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1117 AKKEEELQAALA------------------------------------------RGDEEAVQKNNALKVIRELQAQIAEL 1154
Cdd:pfam12128 530 FPQAGTLLHFLRkeapdweqsigkvispellhrtdldpevwdgsvggelnlygvKLDLKRIDVPEWAASEEELRERLDKA 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1155 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKAIEEETKNHEA 1223
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1224 QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGlESDNKelacevkvLQQVKAESEHKRKKLDAQVQEL-TAKVTEG 1302
Cdd:pfam12128 690 QLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEG-ALDAQ--------LALLKAAIAARRSGAKAELKALeTWYKRDL 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1303 ERLRVElAEKANKLQNELDNVSSLLEEAEKKGikfaKDAASLESQLQDTqeLLQEETRQKLNLSSRIRQLEEEKNNLQEQ 1382
Cdd:pfam12128 761 ASLGVD-PDVIAKLKREIRTLERKIERIAVRR----QEVLRYFDWYQET--WLQRRPRLATQLSNIERAISELQQQLARL 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1383 QEEEEEARKNLEKQMLALQAQLAEAK---KKVDDDLGTIEGLEENKKKLLKDMeSLSQRLEEKAMAYDKLEKTKNRLQQE 1459
Cdd:pfam12128 834 IADTKLRRAKLEMERKASEKQQVRLSenlRGLRCEMSKLATLKEDANSEQAQG-SIGERLAQLEDLKLKRDYLSESVKKY 912
|
....
gi 45382679 1460 LDDL 1463
Cdd:pfam12128 913 VEHF 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
795-1182 |
5.36e-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: 71.63 E-value: 5.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 795 GQSKIFFRAGVLAHLEEERDLKITDIIIFFQAVCRgylARKAFAKKQQQLSALKILQRNCAAYLKLRHWQWWRVFTKVKP 874
Cdd:TIGR02168 668 TNSSILERRREIEELEEKIEELEEKIAELEKALAE---LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQ 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 875 LLQ-VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETElfaeaeemrarlaaKKQELEE 953
Cdd:TIGR02168 745 LEErIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE--------------ALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 954 ILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEeqldeeegarqklqlekvtaeAKIKKMEEEILLLEDQnskflkekk 1033
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLE---------------------EQIEELSEDIESLAAE--------- 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1034 lmedrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK 1113
Cdd:TIGR02168 861 -----IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1114 IQLAKKEEELQAALARGDEEAVQKNNALKV--------IRELQAQIAEL-------QEDLESEKASRNKAEKQKRDLSEE 1178
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEEAEALENKIEDdeeearrrLKRLENKIKELgpvnlaaIEEYEELKERYDFLTAQKEDLTEA 1015
|
....
gi 45382679 1179 LEAL 1182
Cdd:TIGR02168 1016 KETL 1019
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
9.16e-12 |
|
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: 426949 Cd Length: 45 Bit Score: 61.29 E-value: 9.16e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 45382679 31 TAKKLVWIPSERHGFEAASIKEERGDEVLVELaENGKKALVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
877-1462 |
9.58e-12 |
|
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: 426331 [Multi-domain] Cd Length: 1081 Bit Score: 70.57 E-value: 9.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILH 956
Cdd:pfam01576 514 NVERQLQTLQAQLSDLKKKLEEDAGAVEALEEGRKRLQRELEALT---QRLEEKAAAYDKLEKTKNRL---QQELDDLLV 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 957 DLESrveeeeeRNQILQNEKKKMQG-----------HIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------ 1015
Cdd:pfam01576 588 DLDH-------QRQLVSNLEKKQKKfdqmlaeekaiSARYAEERDRAEAEAREKetkaLSLARALEEALDAKEElerqnk 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1016 ------EEILLLEDQNSKFLKE----KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELE 1085
Cdd:pfam01576 661 qlraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQG 740
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1086 KAKRKLdgettdLQDQIAELQAQIEELKIQLA-------KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDL 1158
Cdd:pfam01576 741 EEKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIEAANKGRDEAVKQLKKLQAQMKDLQREL 814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1159 ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQ---RHATA 1235
Cdd:pfam01576 815 DEARASRDEIFAQSKESEKKLKSLEAELLQLQEDLAAAERARRQAQQERDELAEEIASGNSGKSALLDEKRRleaRIAQL 894
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1236 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELTAKVTEgerlrvelaekank 1315
Cdd:pfam01576 895 EEELEEEQSNTELLNDRLRKLTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE-------------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1316 lqneldnvsslLEEAEKKgiKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnlqeqqeeeeearknlek 1395
Cdd:pfam01576 957 -----------MEGTVKS--KYKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK--------------------- 1002
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1396 qmlalqaQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDD 1462
Cdd:pfam01576 1003 -------KLKEVLLQVEDERRNADQYKDQAEKGNSRLKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
925-1298 |
2.19e-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: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 925 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQGHIQDLEEQLDEEEG 995
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 996 ARQKLQLEKVTAEAKIKKmeEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAE--EEEKAKNLAKLKNKQEMMItdleER 1073
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1074 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQIEELK--------IQLAKKEEELQAALARGDEEAVQKNNALKVIR 1145
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1146 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQI 1225
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1226 QEIRQRHATALEELSEQLEQAKRFKANLEKNKQglesdnkelacEVKVLQQVKaESEHKRKKLDAQVQELTAK 1298
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----------EREMMRQIV-ESEKARAEYEATTPITTIK 601
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1235-1958 |
2.25e-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: 69.31 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1235 ALEELSEQLEQAKRFKANLEKNKQGLESDNKELA---CEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAE 1311
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQehqMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1312 KANKLQNELDNVSSLLEeaekkgikfakdaaslesqLQDTQELLQEETRQKLNLSSRIRQLEEEKnnLQEQQEEEEEARK 1391
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMK-------------------LDNEIKALKSRKKQMEKDNSELELKMEKV--FQGTDEQLNDLYH 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1392 NLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLS---QRLEEKAMAYDkLEKTKNRLQQELDDLMVDLD 1468
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlqaDRHQEHIRARD-SLIQSLATRLELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1469 HQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1548
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1549 SSKDDVGKNVHELEKSKRTLEQQveemrtqleeledELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKR----- 1623
Cdd:TIGR00606 468 GSSDRILELDQELRKAERELSKA-------------EKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHhtttr 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1624 ----MLVKQVRELEAELEDERKQRALAVAA---------------------KKKMEMDLKDLEGQIEAANKARDEAIKQL 1678
Cdd:TIGR00606 535 tqmeMLTKDKMDKDEQIRKIKSRHSDELTSllgyfpnkkqledwlhskskeINQTRDRLAKLNKELASLEQNKNHINNEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1679 RKLQAQMKDYQRELEEARASRDE------IFAQSKESEKKLKGLEAE-------ILQLQEEFAASERARRHAEQERDELA 1745
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFDVCGSQDEesdlerLKEEIEKSSKQRAMLAGAtavysqfITQLTDENQSCCPVCQRVFQTEAELQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1746 DEIANSASGKSALLDEKRRLEARIAQLEEELEE-------EQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSEnar 1818
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQE--- 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1819 QQLERQNKELK-AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAA--NKLVRRTEKKLKEVFMQVEDERRH 1895
Cdd:TIGR00606 772 TLLGTIMPEEEsAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQqvNQEKQEKQHELDTVVSKIELNRKL 851
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1896 ADQYKEQMEKANARMKQLKRQleeaEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1958
Cdd:TIGR00606 852 IQDQQEQIQHLKSKTNELKSE----KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQ 910
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
883-1301 |
2.36e-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: 68.89 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 883 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 957
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 958 LESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED 1037
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1038 RIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA 1117
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1118 KKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTAA 1195
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQEE 586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1196 QQELRTKREQEVAELKKAIEEETKnheaqiqeirqrhatALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ 1275
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
410 420
....*....|....*....|....*.
gi 45382679 1276 QVKAESEHKRKKLDAQVQELTAKVTE 1301
Cdd:TIGR04523 652 ETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
877-1262 |
2.67e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.91 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 956
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 957 DLESRVEEEEERNQILQNEKKKMQGHIQDLE--EQLDEEEGARQKLQLEKvtAEAKIKKMEEEILLLEDQNSKFLKEKKL 1034
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAGKcpECGQPVEGSPHVETIEE--DRERVEELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1035 MEDrIAECTSQLAEEEEKAKNLAKLknkqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKI 1114
Cdd:PRK02224 501 AED-LVEAEDRIERLEERREDLEEL-------IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEARE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1115 QLAKKEEELQAALARGDeeavqknnALKVIRELQAQIAELQEDLES---EKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:PRK02224 573 EVAELNSKLAELKERIE--------SLERIRTLLAAIADAEDEIERlreKREALAELNDERRERLAEKRERKRELEAEFD 644
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1192 tTAAQQELRTKREQEVAELKKaIEEETKNHEAQIQEIRQRHATALEELsEQLEQAKRFKANLEKNKQGLES 1262
Cdd:PRK02224 645 -EARIEEAREDKERAEEYLEQ-VEEKLDELREERDDLQAEIGAVENEL-EELEELRERREALENRVEALEA 712
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
883-1301 |
6.20e-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: 67.82 E-value: 6.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 883 EELQAKDEELMKVKEKQTKVEAE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 951
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 952 EEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLK- 1030
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1031 ----EKKLMEDR--IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1104
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1105 LQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKT 1184
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1185 ELEDTLDTTAAQQELRTKREQ--------------EVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK 1250
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEklleevekakaiadEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLY 730
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1251 ANLEKN----KQGLESDNKELACE-VKVLQQVKAESEHKrKKLDAQVQELTAKVTE 1301
Cdd:pfam05483 731 KNKEQEqssaKAALEIELSNIKAElLSLKKQLEIEKEEK-EKLKMEAKENTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1040-1769 |
1.01e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 67.29 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1040 AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERL-----------------KKEEKTRQELEKAKRKL----------D 1092
Cdd:PRK04863 296 YTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYqaasdhlnlvqtalrqqEKIERYQADLEELEERLeeqnevveeaD 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1093 GETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgdeeAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQK 1172
Cdd:PRK04863 376 EQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTR----AIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1173 RDLSEELEALKTELEDTLDT----TAAQQELRT-------KREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSE 1241
Cdd:PRK04863 452 QEATEELLSLEQKLSVAQAAhsqfEQAYQLVRKiagevsrSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQ 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1242 Q------LEQA-KRFKANLEKNKQgLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEgerlrveLAEKAN 1314
Cdd:PRK04863 532 QqraerlLAEFcKRLGKNLDDEDE-LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQR-------LAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1315 KLQNELDNVSSLLEEAekkGIKFAkDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1394
Cdd:PRK04863 604 AWLAAQDALARLREQS---GEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALA 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1395 KQM--------------------LALQAQLAEAkkKVDDDLGTIEGLEENKKKLLKDM---------------------E 1433
Cdd:PRK04863 680 ERFggvllseiyddvsledapyfSALYGPARHA--IVVPDLSDAAEQLAGLEDCPEDLyliegdpdsfddsvfsveeleK 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1434 SLSQRLEEKAMAYDKL-----------EKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEER 1502
Cdd:PRK04863 758 AVVVKIADRQWRYSRFpevplfgraarEKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEA 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1503 DRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRTLEQQVEEMRTQLEE 1581
Cdd:PRK04863 838 ELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQLDE 905
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1582 LEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELeaeleDERKQRALAVAAKKKMEM 1655
Cdd:PRK04863 906 AEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAAEM 979
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1656 DLKD------LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLkgleaEILQLQEEFAA 1729
Cdd:PRK04863 980 LAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQEL-----QDLGVPADSGA 1054
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 45382679 1730 SERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1769
Cdd:PRK04863 1055 EERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
998-1743 |
2.29e-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: 65.90 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 998 QKLQLEKVTAEAKIK----KMEEEILLLEDQNsKFLKEKKLMEDRIaecTSQLAEEEEKAKNLAKLKNKQEMMITDLEER 1073
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1074 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALaRGDEEAVQKnnalkVIRELQAQIAE 1153
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKL-KEDHEKIQH-----LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1154 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEetknheaqIQEIRQRHA 1233
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1234 TALEELSEQLEQAKRFKANLEKNKQG-LESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEK 1312
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1313 anklqneldnvSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEEtrqklnlssriRQLEEEKNNLQEQQEEEEEARKN 1392
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1393 LEKQMLALQAQLAEAKKKVDDDLGTIEGLE-ENKKKLLKDMESLSQRleekamayDKLEKTKNRLQQELDDLMVDLDHQR 1471
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1472 QIVSNLEKKQKKfdqMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSK 1551
Cdd:pfam05483 520 EDIINCKKQEER---MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1552 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRE 1631
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1632 LEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRdeifaqskesEK 1711
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAAL----------EI 746
|
730 740 750
....*....|....*....|....*....|..
gi 45382679 1712 KLKGLEAEILQLQEEFAASERARRHAEQERDE 1743
Cdd:pfam05483 747 ELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1667-1966 |
3.85e-10 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 64.66 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1667 ANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELAD 1746
Cdd:COG4372 65 LNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1747 EIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQvdtlNSELAGERSAAQKSENARQQLERQNK 1826
Cdd:COG4372 145 QAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLR----SAQIEQEAQNLATRANAAQARTEELA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1827 ELKAKLQElegsvkskfkatistLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEvfmqVEDERRHADQYKEQMEKA 1906
Cdd:COG4372 221 RRAAAAQQ---------------TAQAIQQRDAQISQKAQQIAARAEQIRERERQLQR----LETAQARLEQEVAQLEAY 281
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1907 NARMKQLKRQLEEAEEEATRANASRRKLQRELDDA------TEANEGLSREVSTLKNRLRRGGPIT 1966
Cdd:COG4372 282 YQAYVRLRQQAAATQRGQVLAGAAQRVAQAQAQAQaqaqllSSANRPAALRLRRSPRRGRRQRPVT 347
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1168-1917 |
4.82e-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: 64.99 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1168 AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKREQEVAELKKAIEEEtknheaqiQEIRQRHATALEELSEQLEQA 1246
Cdd:TIGR00618 185 EFAKKKSLHGKAELLTLRSQlLTLCTPCMPDTYHERKQVLEKELKHLREAL--------QQTQQSHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1247 KRFKANleknkqglesdnKELACEVKVLQQVKAESEHKRKKLDAQVQelTAKVTEGERLRVELAEKANKLQNELDNVSSL 1326
Cdd:TIGR00618 257 KKQQLL------------KQLRARIEELRAQEAVLEETQERINRARK--AAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1327 LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQklnlssrirqleEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAE 1406
Cdd:TIGR00618 323 RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHI------------RDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1407 AKKKVDDDLGTIEGLEENKKKLlkDMESLSQRLEEKAMAydKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQ 1486
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLA--HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1487 MLAEEKNisaryaEERDRAEAEAREKETKALSLARALEEALEAKEEFER-----QNKQLRADMEDLMSSKDDVGKNVHEL 1561
Cdd:TIGR00618 467 SLKEREQ------QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGScihpnPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1562 EKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkrmlvkqvreLEAELEDERK 1641
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-----------TEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1642 QRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES-EKKLKGLEAEI 1720
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEK 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1721 LQL---QEEFAASERARRHAEQ---ERDELADEIANSASGKSALLDekrrleariAQLEEELEEEQSNMELLNERFRKTT 1794
Cdd:TIGR00618 690 EQLtywKEMLAQCQTLLRELEThieEYDREFNEIENASSSLGSDLA---------AREDALNQSLKELMHQARTVLKART 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1795 LQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELegsvkskfkatistleakiAQLEEQLEQEAKEraaankl 1874
Cdd:TIGR00618 761 EAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLL-------------------KTLEAEIGQEIPS------- 814
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 45382679 1875 vrrtekKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1917
Cdd:TIGR00618 815 ------DEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQL 851
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1146-1937 |
7.52e-10 |
|
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: 64.30 E-value: 7.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1146 ELQAQIAELQEDLESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE 1222
Cdd:TIGR00606 221 EIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1223 AQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELTAkvte 1301
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT---- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1302 geRLRVELAEKANKLQNELDNVSSLLEEAEKKGikfAKDAASLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEKnn 1378
Cdd:TIGR00606 376 --RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI-- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1379 lqeqqeeeeearknLEKQmlalQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSqRLEEKAMAYDKLEKTKNRLQQ 1458
Cdd:TIGR00606 449 --------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQNE 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1459 ELDdlmvdldhqrqivsnLEKKQKKFDQMLAEEKnisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQNK 1538
Cdd:TIGR00606 510 KAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQIR 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1539 QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQARDEQn 1618
Cdd:TIGR00606 553 KIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEEQ- 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1619 eekkrmlvkqvrelEAELEDerkqRALAVAAKKKMEMDLKDLEGQIEAANKardeaikQLRKLQAQMKDYQRELEEARAS 1698
Cdd:TIGR00606 621 --------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSK-------QRAMLAGATAVYSQFITQLTDE 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1699 R-------DEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:TIGR00606 676 NqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQK 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1772 LEEELEEEQSNMELlNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVK----SKFKATI 1847
Cdd:TIGR00606 756 VNRDIQRLKNDIEE-QETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEK 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1848 STLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRA 1927
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPL 914
|
810
....*....|
gi 45382679 1928 NASRRKLQRE 1937
Cdd:TIGR00606 915 ETFLEKDQQE 924
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1659-1961 |
1.39e-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: 63.55 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1659 DLEGQIEAANKARDEAIKQLrklqAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1738
Cdd:TIGR02169 143 DVTDFISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1739 QERDELADEIANSasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERfrkttlqvdtlnselagersaaqkSENAR 1818
Cdd:TIGR02169 219 EKREYEGYELLKE---KEALERQKEAIERQLASLEEELEKLTEEISELEKR------------------------LEEIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1819 QQLERQNKELKAKLQELEGSVKSK---FKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRH 1895
Cdd:TIGR02169 272 QLLEELNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1896 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1539-1871 |
1.52e-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 characteristic 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: 62.39 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1539 QLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQARDEQN 1618
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1619 EEKK---RMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEA 1695
Cdd:pfam19220 107 EELRielRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1696 RASRDEIFAQSKESEKKLKGLEAEILQLQ----EEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1772 LEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQ-----------NKELKAKLQELEGSVK 1840
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAraeleeraemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 45382679 1841 S-------------KFKATISTLEAKIAQLEEQLEQEAKERAAA 1871
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1649-1884 |
1.71e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 62.05 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1649 AKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEfa 1728
Cdd:COG4942 32 SAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQ-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1729 ASERARRHAEQ----ERDELADEIANSASGKSALLDEK-----RRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDT 1799
Cdd:COG4942 110 EREQRRRLAEQlaalQRSGRNPPPALLVSPEDAQRSVRlaiyyGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTT 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1800 LNSELAGERSAAQKSENARQQLERQ-NKELKAKLQELEgsvksKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRT 1878
Cdd:COG4942 190 LLSEQRAQQAKLAQLLEERKKTLAQlNSELSADQKKLE-----ELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARA 264
|
....*.
gi 45382679 1879 EKKLKE 1884
Cdd:COG4942 265 RAAEAK 270
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
871-1513 |
3.05e-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: 62.37 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 871 KVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERK---HQQLLEEKNILAEQLQAETELFAEAEEMRAR---- 943
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNsltETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnhht 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 944 --------LAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME 1015
Cdd:TIGR00606 532 ttrtqmemLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1016 EEILLLEDQNSKFlkekklmEDRIAECTSQLAEE----------EEKAKNLAKLKNKQEMMITDLEERLKKEEK---TRQ 1082
Cdd:TIGR00606 612 NELESKEEQLSSY-------EDKLFDVCGSQDEEsdlerlkeeiEKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQ 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1083 ELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEK 1162
Cdd:TIGR00606 685 RVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1163 ASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR---TKREQEVAELKKAIEEETKNheaQIQEIRQRHATALEEL 1239
Cdd:TIGR00606 765 NDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKdveRKIAQQAAKLQGSDLDRTVQ---QVNQEKQEKQHELDTV 841
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1240 SEQLEQAKRFKANLEKNKQGLESDNKELACE---VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKL 1316
Cdd:TIGR00606 842 VSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1317 QNELDNVSSLLEEAEKKGikfakdaaslESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlqeqqeeeeeaRKNLEKQ 1396
Cdd:TIGR00606 922 QQEKEELISSKETSNKKA----------QDKVNDIKEKVKNIHGYMKDIENKIQDGKDDY-------------LKQKETE 978
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1397 MLALQAQLAEA---KKKVDDDLGTIEG---LEENKKKLLKDMESLSQRleekamaYDKLEKTKNRLQQELDDLmvDLDHQ 1470
Cdd:TIGR00606 979 LNTVNAQLEECekhQEKINEDMRLMRQdidTQKIQERWLQDNLTLRKR-------ENELKEVEEELKQHLKEM--GQMQV 1049
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 45382679 1471 RQIVSNLEKKQKKFDQMLAEEKNISAR---YAEERDRAEAEAREKE 1513
Cdd:TIGR00606 1050 LQMKQEHQKLEENIDLIKRNHVLALGRqkgYEKEIKHFKKELREPQ 1095
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
877-1408 |
3.30e-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: 62.05 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 952
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 953 EILHDLESRVEEEEernQILQNEKKKMQGHIQDLEEQLDEEEgaRQKLQLEKVTAEAKIKKME-EEILLLEDQNSKFLKE 1031
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1032 KKLMEdRIAEctsqlaEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEE 1111
Cdd:pfam05483 424 KKQFE-KIAE------ELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1112 LKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQedlESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1192 TTAAQQELRTKREQEVAELKKA---IEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1268
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1269 CEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKlqneldNVSSLLEEAEKKGIKFAKDAASLESQL 1348
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQH------KIAEMVALMEKHKHQYDKIIEERDSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1349 QDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAK 1408
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1099-1793 |
1.20e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 60.67 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1099 QDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEK----------ASRNKA 1168
Cdd:COG3096 347 QEKIERYQADLEELTIRLEEQNEVVEEANERQEENEARAEAAELEVDELKSQLADYQQALDVQQtraiqyqqaiAALERA 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1169 EK--QKRDLSEElealktELEDTLDTTAAQQELRTKREQEVaELKKAIEEETKNHEAQIQEIRQRHATALEElSEQLEQA 1246
Cdd:COG3096 427 KElcHLPDLTAD------SAEEWLETFQAKEEEATEKLLSL-EQKMSMAQAAHSQFEQAYQLVVAIAGELAR-SEAWDVA 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1247 K------RFKANLEKNKQGLESDNKELacEVKVLQQVKAE----SEHKRKKLDAQVQELTAkvtEGERLRVELAEKANKL 1316
Cdd:COG3096 499 RellregPDQRHLAEQVQPLRMRLSEL--EQRLRQQQSAErllaDFCKRQGKNLDAEELEA---LHQELEALIESLSDSV 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1317 QNELDNVSSLLEEAEKKGIKFAKDAASLESQL--QDTQELLQEETRQKLNLSsriRQLEEEKNNLQEQQEEEEEARKNLE 1394
Cdd:COG3096 574 SNAREQRMALRQEQEQLQSRIQSLMQRAPVWLaaQNALEQLSEQSGEEFTDS---QDVTEYMQQLLEREREATVERDELG 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1395 KQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLL----------KDMESLSQRL--EEKAMAYDKLEKTKNRLQQeLDD 1462
Cdd:COG3096 651 ARKNALDEEIERLSQPGGSEDQRLNALAERFGGVLlseiyddvtiEDAPYFSALYgpSRHAIVVPDLSQVKEHLEG-LTD 729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1463 LMVDL------------------DHQRQIVSNLEKKQKKFDQM--------LAEEKNISARYAEERDRAEAEAR-----E 1511
Cdd:COG3096 730 CPEDLyliegdpqsfddsvfsvdELEKAVVVKIADRQWRYSRFpeiplfgrAAREQRLESLHAERDVLSERHATlsfdvQ 809
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1512 KETKA-----------LSLARALEEALEAKEEFERQNKQLRA------DMEDLMSSKDDVGKNVHELEK--------SKR 1566
Cdd:COG3096 810 KTQRLhqafsrfigshLAVAFEADPEAEIRQLNSRRNELERAlsnhenDNQQQRIQFDQAKEGVTALNRlipqlnllADE 889
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1567 TLEQQVEEMRTQLEELEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQARDEQNEEKKRMLVKQVRELeAELEDER 1640
Cdd:COG3096 890 SLADRVEEIRERLDEAQEAarfIQQHGNTLSKLEpiaSVLQSDPEQFEQ-LKEDYAQAQQMQRQARQQAFAL-TEVVQRR 967
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1641 KQRALAVAAKKKME-MDLKD-LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDeifaQSKESEKKLKGlEA 1718
Cdd:COG3096 968 AHFSYSDSAEMLSEnSDLNEkLRQRLEQAEAERTRAREQLRQHQAQLSQYNQVLASLKSSYD----TKKELLNELQQ-EL 1042
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1719 EILQLQEEFAASERARRhaeqERDELADEIANSASGKSalldekrrleariaQLEEELEEEQSNMELLNERFRKT 1793
Cdd:COG3096 1043 QDIGVRADSGAEERARI----RRDELHAQLSTNRSRRN--------------QLEKQLTFCEAEMDNLTRKLRKL 1099
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1042-1246 |
2.59e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 58.58 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1042 CTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEE 1121
Cdd:COG4942 29 AAFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1122 E-----------LQAALARGDEEAVqknnALKVIRE-------LQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1183
Cdd:COG4942 109 QereqrrrlaeqLAALQRSGRNPPP----ALLVSPEdaqrsvrLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQ 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1184 TELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhATALEELSEQLEQA 1246
Cdd:COG4942 185 AELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRAN-ESRLKNEIASAEAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1098-1884 |
3.43e-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: 58.58 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1098 LQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL----KVIRELQAQIAELQEDLESEKASRNKAEKQKR 1173
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLqenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1174 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIqeirqrhaTALEELSEQLEQAK-RFKAN 1252
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1253 LEKNKQGLESDNKELACEVKvlqqvkaESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1332
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1333 KGIKFAKDAASLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKK 1409
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1410 KVDddlgtiEGLEENKKKLlkdmESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqrqivsnleKKQKKFDQMLA 1489
Cdd:pfam05483 367 TEQ------QRLEKNEDQL----KIITMELQKKSSELEEMTKFKNNKEVELEEL---------------KKILAEDEKLL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1490 EEKNISARYAEERDRAEAE------AREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEK 1563
Cdd:pfam05483 422 DEKKQFEKIAEELKGKEQElifllqAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1564 SKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQARDEQnEEKKRMLVKQVRELEAELEderkqr 1643
Cdd:pfam05483 500 ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDEL-ESVREEFIQKGDEVKCKLD------ 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1644 alavaakkKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQL 1723
Cdd:pfam05483 570 --------KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKL 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1724 QEEFAAserARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLeeeleeeqsnMELLNERFRKTTLQVDTLNSE 1803
Cdd:pfam05483 642 ELELAS---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA----------VKLQKEIDKRCQHKIAEMVAL 708
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1804 LAGERSAAQKSenarqqLERQNKEL---KAKLQElEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1880
Cdd:pfam05483 709 MEKHKHQYDKI------IEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTA 781
|
....
gi 45382679 1881 KLKE 1884
Cdd:pfam05483 782 ILKD 785
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1098-1880 |
4.03e-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: 58.68 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1098 LQDQIAELQAQIEELKIQLAKKEEELQAALargdeeavqknNALKVIrelqaqiaeLQEDLESEKASRNKAEKQKRDLSE 1177
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSM-----------NSIKTF---------WSPELKKERALRKEEAARISVLKE 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1178 ELEALKTELED-TLDTTAAQQELRTKRE------------QEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLE 1244
Cdd:pfam10174 61 QYRVTQEENQHlQLTIQALQDELRAQRDlnqllqqdfttsPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1245 QakrFKANLEKNKQGLESDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQELTA----KVTEGERLRVELAE 1311
Cdd:pfam10174 141 E---MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHLEVlldqKEKENIHLREELHR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1312 KaNKLQNELDNVSSLLEEAEKKGIKFakdaASLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNNLQEQQEEEE 1387
Cdd:pfam10174 218 R-NQLQPDPAKTKALQTVIEMKDTKI----SSLERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKID 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1388 EARKNLEK---QMLALQAQLAEAKKKVDDDLGTIEGLEEN-------KKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQ 1457
Cdd:pfam10174 293 QLKQELSKkesELLALQTKLETLTNQNSDCKQHIEVLKESltakeqrAAILQTEVDALRLRLEEKESFLNKKTKQLQDLT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1458 QELDDLMVDLDHQRQIVSNLEKK----QKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLaraleealeakeef 1533
Cdd:pfam10174 373 EEKSTLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL-------------- 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1534 erqnkqlrADMEDLMSSKDDVGKNV-HELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQ 1612
Cdd:pfam10174 439 --------TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----A 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1613 ARDEQNEEKKRMLVKQvreLEAELEDERKQRALAVAAKKKMEmdlkdlegQIEAANKARDEAIKQLRKLQAQMKDYQREL 1692
Cdd:pfam10174 506 SSLASSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEES 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1693 EEARASRDEIFAQSKESE-------KKLKGLEAEILQLQEEFAASERARRHAEQERDEladeiansasgKSALLDEkrrl 1765
Cdd:pfam10174 575 GKAQAEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE---- 639
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1766 EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAgerSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKA 1845
Cdd:pfam10174 640 EARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS---STQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLA 716
|
810 820 830
....*....|....*....|....*....|....*
gi 45382679 1846 TISTLEAKIAQLEeqLEQEAKERAAANKLVRRTEK 1880
Cdd:pfam10174 717 AISEKDANIALLE--LSSSKKKKTQEEVMALKREK 749
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1416-1961 |
4.59e-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: 58.70 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1416 GTIEGLEENKKKLlkdmESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLdhqRQIVSNLEKKQKKFDQMLAEEKNiS 1495
Cdd:pfam12128 241 PEFTKLQQEFNTL----ESAELRLSHLHFGYKSDETLIASRQEERQETSAEL---NQLLRTLDDQWKEKRDELNGELS-A 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1496 ARYAEERDRAEAEAREKETKALSLARALEEALEAKeeferQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQV-EE 1574
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDADIETAAADQE-----QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkEQ 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1575 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQardEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAkkkmE 1654
Cdd:pfam12128 388 NNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELR---EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAT----P 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1655 MDLKDLEGQIEAANKARDEaikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEE-FAAS--- 1730
Cdd:pfam12128 461 ELLLQLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlFPQAgtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1731 -ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR-----------RLEARIAQLEEELEEE 1779
Cdd:pfam12128 537 lHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpewaaseeELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1780 QSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEE 1859
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDK 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1860 QLeQEAKERAAANKLVRRTEK--KLKEVfmqVEDERRHADQYKEQMEkanARMKQLKRQLEEAEEEATRANASRrklqre 1937
Cdd:pfam12128 697 KH-QAWLEEQKEQKREARTEKqaYWQVV---EGALDAQLALLKAAIA---ARRSGAKAELKALETWYKRDLASL------ 763
|
570 580
....*....|....*....|....
gi 45382679 1938 lDDATEANEGLSREVSTLKNRLRR 1961
Cdd:pfam12128 764 -GVDPDVIAKLKREIRTLERKIER 786
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
920-1590 |
5.63e-08 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 58.32 E-value: 5.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 920 KNILAEQLQAETELFAEAEEMRARLAAKKQELEEilHDLESRveeeeeRNQILQNEKKKMQGHIQDLEEQLDEEEGARQK 999
Cdd:COG4717 180 NPQINQLLEKLKQERNEIDEAEKEYATYHKLLES--RRAEHA------RLAELRSELRADRDHIRALRDAVELWPRLQEW 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1000 LQLEKVTAEakikKMEEEILLLED---QNSKFLKEKKLMEDRIAECTSQLAEeeekaknlakLKNKQEMMITDLEERLKK 1076
Cdd:COG4717 252 KQLEQELTR----RREELATFPRDgvlRLEKREAHLQKTEAEIDALLVRLAE----------LKDLASQLIPAKEAVLQA 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1077 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALargDEEAVQKNNALKVIRELQAQIAELQE 1156
Cdd:COG4717 318 LVRLHQQLSEIKASAFELTETLAGIEADLRDKEEAAGNGFEAERVHDLRSL---ECMLRYQSSQRELKQTEAAYCKRLDE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1157 DLESEKASRNKAEKQKRDlseELEALKTELEDTLDTTAAQQELRTKreqevaelkkaieEETKNHEAQIQEIRQRHATAL 1236
Cdd:COG4717 395 KRLFEDEAEEEARQRLAD---DEEEVRAGDEAREEKIAANSQVIDK-------------EEVCNLYDRRDTAWQKQRFLR 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1237 EELSEQLEQAKRFKANLEKNKQGLesdnkELACEVKVLQQVKAesehkrkkldaqvqELTAKVTEGERLRVELAEKANKL 1316
Cdd:COG4717 459 EKQTAFERQKTEHTKIIALRLAGM-----LLVALSRLLTSLIF--------------QIIFAVAQIVFLSAEIKSSSRAV 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1317 QNELDNVSSLLEEAekkgikfAKDAASLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEK 1395
Cdd:COG4717 520 REEKAAVTDIPEEL-------ARLLITDELPELAVDLLVQSRIRQhWQQLRKALDQLEAAYEALEGRFAAAEAAMAEWQS 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1396 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL----EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQR 1471
Cdd:COG4717 593 EWEEALDELGLSRELSPEQQLDILSTMKDLKKLMQKKAELTHQVarlrEEQAAFEERVEGLLAVLEAQFIDLSTLFCVQR 672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1472 QIVS--NLEKKQKKFDQML---AEEKNISARYAEERDRAEAE------AREKETKALSLARALEEALEAKEEFERQNKQL 1540
Cdd:COG4717 673 LRVAaeLQKEEARLALEGNierTKELNDELRAELELHRKEILdlfdcgTADTEDAFREAAREEQQLTQRESRLESLEAQL 752
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1541 RA------DMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATE 1590
Cdd:COG4717 753 EGvaaeayELSASLDQRELKEEELALLEEAIDALDEEVEELHAQVAALSRQIAQLE 808
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1171-1379 |
8.90e-08 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 56.96 E-value: 8.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1171 QKRDLSEELEALKTELEDTldtTAAQQELRTKREQEVAELKKAiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK 1250
Cdd:COG4372 75 QLDDIRPQLRALRTELGTA---QGEKRAAETEREAARSELQKA-RQEREAVRQELAAARQNLAKAQQELARLTKQAQDLQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1251 ---ANLEKNKQGLESDNKELACEVKVLQQVKAEsehkrkkLDAQVQELTAKVTEGERLRVELAEKANKLQN---ELDNVS 1324
Cdd:COG4372 151 trlKTLAEQRRQLEAQAQSLQASQKQLQASATQ-------LKSQVLDLKLRSAQIEQEAQNLATRANAAQArteELARRA 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1325 SLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1379
Cdd:COG4372 224 AAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQL 278
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1308-1917 |
9.63e-08 |
|
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: 57.34 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1308 ELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEE 1387
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1388 EARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL 1467
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1468 DHQRQIVSNLEKKQKKFDQMLAEeknisaryaeerdraeaeareketkalslaraleealeakeeferqnkqlradmedl 1547
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQ--------------------------------------------------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1548 msskddvgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQARDEQNEEKKRMLVK 1627
Cdd:TIGR04523 220 ----------ISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS-EKQKELEQNNKKIKELEK 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1628 QVRELEAELEDERKQRALAVAakKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1707
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKEQDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1708 ESEKKLKGLEAEilqlqeefaaserarrhaeqerdeladeiansasgKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1787
Cdd:TIGR04523 367 EKQNEIEKLKKE-----------------------------------NQSYKQEIKNLESQINDLESKIQNQEKLNQQKD 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1788 ERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKE 1867
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD-NTRESLETQLKVLSRSINKIKQNLEQKQKE 490
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 45382679 1868 RAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1917
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1103-1403 |
9.77e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.61 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1103 AELQAQIEELKiqlakKEEELQAalargDEEAVQKN--NALKVIrelqAQIAELQEDLESEKASRNKAEKQKRDLSEELE 1180
Cdd:PRK11281 39 ADVQAQLDALN-----KQKLLEA-----EDKLVQQDleQTLALL----DKIDRQKEETEQLKQQLAQAPAKLRQAQAELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1181 ALKTELEDTLDTTAAQQELRTkREQEVAELKKAIEEETKN-HEAQIQEIRQRHA-----TALEELSEQLEQAKRFKANLE 1254
Cdd:PRK11281 105 ALKDDNDEETRETLSTLSLRQ-LESRLAQTLDQLQNAQNDlAEYNSQLVSLQTQperaqAALYANSQRLQQIRNLLKGGK 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1255 KNKQGLESDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELtakvteGERLRVELAEKANKLQNELdnvsSLLEEA- 1330
Cdd:PRK11281 184 VGGKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAi 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1331 -EKKGIKFAKDAASLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNNLQeqqeeeeeaRKNLE-KQML--ALQ 1401
Cdd:PRK11281 251 nSKRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQ 320
|
..
gi 45382679 1402 AQ 1403
Cdd:PRK11281 321 SE 322
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1221-1955 |
1.10e-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: 57.16 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1221 HEAQIQEIRQRhATALEELSEQLEQAKrfkANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAkvt 1300
Cdd:pfam12128 232 AIAGIMKIRPE-FTKLQQEFNTLESAE---LRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRD--- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1301 egeRLRVELA---EKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQklnLSSRIRQLEEEKN 1377
Cdd:pfam12128 305 ---ELNGELSaadAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA---LTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1378 NLqeqqeeeeearknlekqmlalqaqlaeaKKKVDDDLGTIegLEENKKKLLKDMESLSQRLEEKAMAYDKLEktkNRLQ 1457
Cdd:pfam12128 379 RR----------------------------RSKIKEQNNRD--IAGIKDKLAKIREARDRQLAVAEDDLQALE---SELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1458 QELDDLMVDL-DHQRQIVSNLEKKQKKFDQMLAEEKNISARyaEERDRAEAEAREKETKAlslaraleealeakeeferq 1536
Cdd:pfam12128 426 EQLEAGKLEFnEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDERIERAREEQEAA-------------------- 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1537 nkqlRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA---TEDAKLRLEVNM--QAMKAQFERDL 1611
Cdd:pfam12128 484 ----NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPqagTLLHFLRKEAPDweQSIGKVISPEL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1612 QARDEQNEEKKRMLVKQVRELEA-ELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQR 1690
Cdd:pfam12128 560 LHRTDLDPEVWDGSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1691 ELEEARASrdeiFAQSKESEKKLKG-LEAEILQLQEefaASERARRHAEQERDELADEIANSASGKSALLDEKRR--LEA 1767
Cdd:pfam12128 640 EETFARTA----LKNARLDLRRLFDeKQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREA 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1768 RIAQLeeeleeeqsnmELLNERFRKTTLQVDTLNSELAGERSAAQKSENArqqLERQNK-ELKAKLQELEgsvkskfkaT 1846
Cdd:pfam12128 713 RTEKQ-----------AYWQVVEGALDAQLALLKAAIAARRSGAKAELKA---LETWYKrDLASLGVDPD---------V 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1847 ISTLEAKIAQLEEQLEQEAKERAAanklVRRTEKKLKEVFMQvederrHADQYKEQMEKANARMK----QLKRQLEEAEE 1922
Cdd:pfam12128 770 IAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLATQLSNIERAISelqqQLARLIADTKL 839
|
730 740 750
....*....|....*....|....*....|...
gi 45382679 1923 EATRANASRRKLQRELDDATEANEGLSREVSTL 1955
Cdd:pfam12128 840 RRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1535-1751 |
1.23e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 56.27 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1535 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQA-------TEDAKLRLEVNMQAMKAQF 1607
Cdd:COG4942 38 KQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKlrkqiadLNARLNALEVQEREQRRRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1608 ERDLQA--------------RDEQNEEKKRMLV----------KQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQ 1663
Cdd:COG4942 118 AEQLAAlqrsgrnpppallvSPEDAQRSVRLAIyygalnparaERIDALKATLKQLAAVRAEIAAEQAELTTLLSEQRAQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1664 IEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKGLEAEILQLQEEFAASERARRHAEQERDE 1743
Cdd:COG4942 198 QAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRL-------KNEIASAEAAAAKAREAAAAAEAAAARARAAEAK 270
|
....*...
gi 45382679 1744 LADEIANS 1751
Cdd:COG4942 271 RTGETYKP 278
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
883-1873 |
1.25e-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: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 883 EELQAK-DEELMKVKEKQTK-VEAELEEMERKHQQLLEekNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 960
Cdd:TIGR01612 699 DDLKSKiDKEYDKIQNMETAtVELHLSNIENKKNELLD--IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 961 RveeeeernqilQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIA 1040
Cdd:TIGR01612 777 E-----------KDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1041 ECTSQLAEEEEKAKNLAklkNKQEMMITDLEERLKKEEKTRQeLEKAKRKLDgettDLQDQIAELQAQIEE--LKIQLAK 1118
Cdd:TIGR01612 846 NKVDKFINFENNCKEKI---DSEHEQFAELTNKIKAEISDDK-LNDYEKKFN----DSKSLINEINKSIEEeyQNINTLK 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1119 KEEELqAALARGDEEAVQK--NNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELedTLDTTAA- 1195
Cdd:TIGR01612 918 KVDEY-IKICENTKESIEKfhNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDA--SLNDYEAk 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1196 -----------QQELRTKRE----QEVAELKKA---IEEETKNHEAQIQEIRQRHATALEELSEQLEqaKRFKANLEK-N 1256
Cdd:TIGR01612 995 nnelikyfndlKANLGKNKEnmlyHQFDEKEKAtndIEQKIEDANKNIPNIEIAIHTSIYNIIDEIE--KEIGKNIELlN 1072
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1257 KQGLESDNKELACEVKVLQQVK------------AESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVS 1324
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQI 1152
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1325 SLLEEAEKKGIkFAKDAASLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNNLQEQQEEEEEARKNLEKQML 1398
Cdd:TIGR01612 1153 NDLEDVADKAI-SNDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYGKNLGKLFL 1228
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1399 AlqaQLAEAKKKVDDDLGTIEGLEENkkklLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDD----LMVDLDHQRQIv 1474
Cdd:TIGR01612 1229 E---KIDEEKKKSEHMIKAMEAYIED----LDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDdkdhHIISKKHDENI- 1300
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1475 SNLEKKQKKFDQMLAEEKNIS------ARYAEERDRAEAEAREKETKALSLARALEEALEakeeferqnKQLRADMEDLM 1548
Cdd:TIGR01612 1301 SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI---------KKIIDEVKEYT 1371
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1549 SSKDDVGKNVH-ELEKSKrTLEQQVEEmRTQLEELEDELQATEDAK---------LRLEVNMQAMKAQFERDLQARDEQN 1618
Cdd:TIGR01612 1372 KEIEENNKNIKdELDKSE-KLIKKIKD-DINLEECKSKIESTLDDKdidecikkiKELKNHILSEESNIDTYFKNADENN 1449
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1619 EEKKrMLVKQVreleaELEDERKQRALAVA---AKKKMEMDLKDLEGQIEAANKARDEA---IKQLRKLQAQMKDYQRE- 1691
Cdd:TIGR01612 1450 ENVL-LLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDv 1523
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1692 --------------------------LEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELA 1745
Cdd:TIGR01612 1524 tellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLE 1603
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1746 D------EIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnerfrkTTLQVDTLNSELAGERSAAQKSENARQ 1819
Cdd:TIGR01612 1604 NfenkflKISDIKKKINDCLKETESIEKKI-----------------------SSFSIDSQDTELKENGDNLNSLQEFLE 1660
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1820 QLERQNKELKAKLQELEgSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANK 1873
Cdd:TIGR01612 1661 SLKDQKKNIEDKKKELD-ELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1389-1771 |
1.35e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.89 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1389 ARKNLEKQMLALQAQLAEAKKKvdddlgtiegleenkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQELDDL----- 1463
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQ---------------------LAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhln 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1464 --MVDLDHQRQI---VSNLEKKQKKfdqmLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNK 1538
Cdd:PRK04863 339 lvQTALRQQEKIeryQADLEELEER----LEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1539 QLRADMEDLMSSKDDVGKNVHELEKskrtLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQARDEQN 1618
Cdd:PRK04863 415 QYQQAVQALERAKQLCGLPDLTADN----AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1619 EEKKRMLVKQV-RELeaeLEDERKQRALAVAAkKKMEMDLKDLEGQIE---AANKARDEAIKQLRK---LQAQMKDYQRE 1691
Cdd:PRK04863 487 GEVSRSEAWDVaREL---LRRLREQRHLAEQL-QQLRMRLSELEQRLRqqqRAERLLAEFCKRLGKnldDEDELEQLQEE 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1692 LEEARASRDEIFAQSKES----EKKLKGLEAEILQL----QEEFAASERARRHAEQERDELADE------IANSASGKSA 1757
Cdd:PRK04863 563 LEARLESLSESVSEARERrmalRQQLEQLQARIQRLaaraPAWLAAQDALARLREQSGEEFEDSqdvteyMQQLLERERE 642
|
410
....*....|....
gi 45382679 1758 LLDEKRRLEARIAQ 1771
Cdd:PRK04863 643 LTVERDELAARKQA 656
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1323-1896 |
1.54e-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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 56.66 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1323 VSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknnlqeqqeeeeeaRKNLEKQMLALQA 1402
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELERKASALARQLERESDRNQELQKRIRLLEK---------------REAEAEEALREQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1403 QLAEAKKKVDDDLGTIEGLEENKKKLLKDMES-LSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQ 1481
Cdd:pfam05557 76 ELNRLKKKNLEALNKKLNEKESQLADAREVIScLKNELSELRRQIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1482 KKFDQMLAEEKNISARYAEERDRAEAEAREKEtkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL 1561
Cdd:pfam05557 156 QNLEAQQSSLAEAEQRIKELEFEIQSQEQDSE-----IVKNSKSELARIPELERELERLREHNKHLNENIENKLLLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1562 EKSKRTLEQQvEEMRTQLEELEDELQATEdAKLRLEVNMQAMKAQFER---DLQARDEQNEEKKRMLVKQVRELEAELED 1638
Cdd:pfam05557 231 EDLKRKLERE-EGYREELATLELEKEKLE-QELKSWEKLAQDTGLNLRspeDLSRRIEQLQQREITLKEENSSLTSSARQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1639 ERKQRALavaakkkMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQSKESEKKLKG 1715
Cdd:pfam05557 309 LEKAQRE-------LEQELAQYLKNIEDLNKKLKRHKALVRRLQRRVLLLTKERDGMRAileSYDKELTPSNYSPQLLER 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1716 LE--AEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR-- 1791
Cdd:pfam05557 382 IEeaEDMTQDMQAHNEEMEAQLSVAEEELGGYKQQATTLERELQALRQQESLADPSYSKEEVDSLRRKLETLEAERQRlr 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1792 --KTTLQVDTLNSELAGERSAA-----QKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQE 1864
Cdd:pfam05557 462 eqKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRANDLEKLQAEIERLKRRLKKLEDDLEQVGSLPETTSTMN 541
|
570 580 590
....*....|....*....|....*....|....*
gi 45382679 1865 AKERAAANKLVRRTEKK---LKEVFMQVEDERRHA 1896
Cdd:pfam05557 542 FKEVLELRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1628-1959 |
1.70e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1628 QVRELEAELEDerKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYqrelEEARASRDEIFAQSK 1707
Cdd:PRK02224 188 SLDQLKAQIEE--KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEH----EERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1708 ESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1787
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1788 ERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSkFKATISTLEAKIAQLEEQLEQEAKE 1867
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE-LRERFGDAPVDLGNAEDFLEELREE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1868 RAAANKLVRRTEKKLKEVFMQVEDERR------------------HAD---QYKEQMEKANARMKQLKRQLEEAEEEATR 1926
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegspHVEtieEDRERVEELEAELEDLEEEVEEVEERLER 500
|
330 340 350
....*....|....*....|....*....|...
gi 45382679 1927 ANASrRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:PRK02224 501 AEDL-VEAEDRIERLEERREDLEELIAERRETI 532
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1552-1749 |
1.83e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 56.19 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1552 DDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT-EDAKL----RLEVNMQAMKAQFE-RDLQARDEQNEEKKRML 1625
Cdd:COG4372 77 DDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKArQEREAvrqeLAAARQNLAKAQQElARLTKQAQDLQTRLKTL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1626 VKQVRELEAELED-ERKQRALAVAAKkkmEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARASRDEIFA 1704
Cdd:COG4372 157 AEQRRQLEAQAQSlQASQKQLQASAT---QLKSQVLDLKLRSAQIEQEAQNLATRANAAQART--EELARRAAAAQQTAQ 231
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45382679 1705 QSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIA 1749
Cdd:COG4372 232 AIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVA 276
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1236-1750 |
2.32e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1236 LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1315
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1316 LQNELDNVSSlLEEAEKKGIKFAKDAASLEsqlqdtqellQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEk 1395
Cdd:PRK01156 265 LSMELEKNNY-YKELEERHMKIINDPVYKN----------RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLS- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1396 QMLALQAQLAEAKKKVDD---DLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKL-----------EKTKNRLQQELD 1461
Cdd:PRK01156 333 VLQKDYNDYIKKKSRYDDlnnQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsafiseilkiqEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1462 DLMVDLDHQRQIVSNLEKKQKKFDQMLAE-------------------------EKNISARYAEERDRAEAEAREKETKA 1516
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDElsrnmemlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1517 LSLaraleeALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLEELEDELQAT--EDAKL 1594
Cdd:PRK01156 493 KDI------DEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLklEDLDS 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1595 RLEVNMQAMKAQFERDLQARDEQNEEKKRML---VKQVRELEAELEDERKQRALAVaakKKMEMDLKDLEGQIEAAnKAR 1671
Cdd:PRK01156 566 KRTSWLNALAVISLIDIETNRSRSNEIKKQLndlESRLQEIEIGFPDDKSYIDKSI---REIENEANNLNNKYNEI-QEN 641
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1672 DEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN 1750
Cdd:PRK01156 642 KILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
872-1099 |
2.61e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 55.42 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 872 VKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL 951
Cdd:COG4372 70 RSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQNLAKAQQELARLTKQAQDL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 952 EEILHDLESRVEEEEERNQILQNEKKKMQghiqdleeqldeeeGARQKLQLEKVTAEAKIKKMEEEILLLEDQNskflKE 1031
Cdd:COG4372 150 QTRLKTLAEQRRQLEAQAQSLQASQKQLQ--------------ASATQLKSQVLDLKLRSAQIEQEAQNLATRA----NA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1032 KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQ 1099
Cdd:COG4372 212 AQARTEELARRAAAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE 279
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1010-1372 |
2.68e-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.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 55.63 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1010 KIKKMEEEILLLEDQNSK--FLKEKKLMEdriaECTSQLAEEEEKAKNlaklknkqemMITDLEERLKKEEKTRQELEKA 1087
Cdd:pfam06160 61 SLPDIEELLFEAEELNDKyrFKKAKKALD----EIEELLDDIEEDIKQ----------ILEELDELLESEEKNREEVEEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1088 KRKLDGETTDLQDQ-------IAELQAQIEELKIQLAKKEEELQAalarGDEEAvqknnALKVIRELQAQIAELQEDLES 1160
Cdd:pfam06160 127 KDKYRELRKTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMED 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1161 EKASRNKAEKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKAIEE-ETKNHEAQIQEIRQRhataL 1236
Cdd:pfam06160 198 IPPLYEELKTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----I 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1237 EELSEQLEQAKRFKANLEKNKQGLESD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELTAKVtegERLR 1306
Cdd:pfam06160 273 DQLYDLLEKEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIV 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1307 VELAEKA---NKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQL 1372
Cdd:pfam06160 350 ERLEEKEvaySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1084-1332 |
2.81e-07 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 55.42 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL-----ARGDEEAVQ---------KNNALKVIRELQA 1149
Cdd:COG4372 65 LNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARselqkARQEREAVRqelaaarqnLAKAQQELARLTK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1150 QIAELQEDLESEKASRNKAEKQKRDL---SEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHeAQIQ 1226
Cdd:COG4372 145 QAQDLQTRLKTLAEQRRQLEAQAQSLqasQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRANAAQARTEEL-ARRA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1227 EIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEhkRKKLDAQVQELTAKVTEGERLR 1306
Cdd:COG4372 224 AAAQQTAQAIQQRDAQISQKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLE--AYYQAYVRLRQQAAATQRGQVL 301
|
250 260
....*....|....*....|....*.
gi 45382679 1307 VELAEKANKLQNELDNVSSLLEEAEK 1332
Cdd:COG4372 302 AGAAQRVAQAQAQAQAQAQLLSSANR 327
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1563-1818 |
3.35e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 54.73 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1563 KSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK---AQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1639
Cdd:COG4942 31 FSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLEteiASLEAQLIETADDLKKLRKQIADLNARLNALEVQE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 RKQR---ALAVAAKKKMEMD----LKDLEGQIEAA----------NKARDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1702
Cdd:COG4942 111 REQRrrlAEQLAALQRSGRNpppaLLVSPEDAQRSvrlaiyygalNPARAERIDALKATLKQLAAVRAEIAAEQAELTTL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1703 FAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANsasgksalldEKRRLEARIAQLEEELeeeqsn 1782
Cdd:COG4942 191 LSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKN----------EIASAEAAAAKAREAA------ 254
|
250 260 270
....*....|....*....|....*....|....*.
gi 45382679 1783 mellnERFRKTTLQVDTLNSELAGERSAAQKSENAR 1818
Cdd:COG4942 255 -----AAAEAAAARARAAEAKRTGETYKPTAPEKML 285
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1051-1186 |
3.42e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.60 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1051 EKAK-NLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLakkEEELQAALAR 1129
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKE 581
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1130 GDEEAVQknnalkVIRELQAQIAELQEDLESEKASrnkaEKQKRdLSEELEALKTEL 1186
Cdd:PRK00409 582 AKKEADE------IIKELRQLQKGGYASVKAHELI----EARKR-LNKANEKKEKKK 627
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
1064-1442 |
4.00e-07 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 55.07 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1064 EMMITDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKN--NAL 1141
Cdd:COG4477 121 EQILEDLNELVESEEKNSEEIDHVLELYE----ELRRDVLANRHQYGEAAPELEKKLENIEEELSQFVELTSSGDyiEAR 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1142 KVIRELQAQIAELQEDLESEKASRNKAEKqkrDLSEELEALKTELEDT------LDTTAAQQELRTKREQEVAELKKAIE 1215
Cdd:COG4477 197 EVLEEAEEHMIALRSIMERIPSLLAELQT---ELPGQLQDLKAGYRDMkeegyhLEHVNIDSRLERLKEQLVENSELLTQ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1216 EETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKANLEKNKQGLESDnkelacevkvLQQVKAESEHkrkkldaqVQEL 1295
Cdd:COG4477 274 LELDEAEEELGLIQEK----IESLYDLLEREVEAKNVVEENLPILPDY----------LEKAKENNEH--------LKEE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1296 TAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEE 1375
Cdd:COG4477 332 IERVKESYRLAETELGSVRKFEKELKELESVLDEILENIEAQEVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKD 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1376 KNNlqeqqeeeeeARKNLEKqmlaLQAQLAEAKKKVDDDlgTIEGLEENKKKLLKDMESLSQRLEEK 1442
Cdd:COG4477 412 ELE----------ARENLER----LKSKLHEIKRYMEKS--NLPGLPETFLSLFFTAGHEIQDLMKE 462
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1022-1264 |
5.29e-07 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 54.55 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1022 EDQNSKFLKEKKLMEdRIAECTSQLAEEEEKAKNLAKLKNKQEmmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVS--VKSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELKIqLAKKEEELQaaLARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNK-------AEKQKRD 1174
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1175 LSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELKKAIEEEtknhEAQIQEIRQRHATALEELSEQLEQAkRFKANLE 1254
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 45382679 1255 KNkqGLESDN 1264
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| DUF812 |
pfam05667 |
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of ... |
1489-1752 |
6.04e-07 |
|
Protein of unknown function (DUF812); This family consists of several eukaryotic proteins of unknown function.
Pssm-ID: 428574 [Multi-domain] Cd Length: 601 Bit Score: 54.63 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1489 AEEKNISARYAEERDRAeaeaREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRT- 1567
Cdd:pfam05667 226 WNSQGLASRLTPEEYRK----RKRTKLLKRIAEQLRSAALASTEATSGASRSKQDLAELLSSFGGSSTTDTNLTKGSRFt 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1568 ----LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQAR-DEQNEEKKRML--VKQVRELEAELEDER 1640
Cdd:pfam05667 302 htekLQFTNEEAPAATSSPPTKAETEEELQQQREEELEELQEQLE-ELESSiEELEKEIKKLEssIKQVEEELEELKEQN 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1641 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARASRDEIFAQSKESEKKL---KGL 1716
Cdd:pfam05667 381 EELEKQYKVKKKTLDLLPDAEENIAKLQALVEASAQRLVELAGQWEKHRVPLiEEYRALKEAKSNKESESQRKLeeiKEL 460
|
250 260 270
....*....|....*....|....*....|....*.
gi 45382679 1717 EAEILQLQEEFAASERARRHAEQERDELADEIANSA 1752
Cdd:pfam05667 461 REKIKEVAEEARSKEELYKQLVAEYERLPKDVNRSA 496
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1396-1961 |
7.57e-07 |
|
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: 54.67 E-value: 7.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1396 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLlKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMV---------- 1465
Cdd:TIGR00606 225 QITSKEAQLESSREIVKSYENELDPLKNRLKEI-EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEkvfqgtdeql 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1466 -DLDHQRQIVSNlEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKEtkaLSLARALEEALEAKEEFERQNKQLRADM 1544
Cdd:TIGR00606 304 nDLYHNHQRTVR-EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR---LQLQADRHQEHIRARDSLIQSLATRLEL 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1545 EDLMSSKDDVG--KNVHELEKskRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlQARDEQNEEKK 1622
Cdd:TIGR00606 380 DGFERGPFSERqiKNFHTLVI--ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK-KEILEKKQEEL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1623 RMLVKQVRELEAELEDERKQRAlavaAKKKMEMDLKDLEgqieaankaRDEAIKQLRKLQAQMKDYQRELEEARASRDEI 1702
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQ----ELRKAERELSKAE---------KNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1703 FAQSKESEKKLKGLEaeiLQLQEEFAASERARRHAEQERDELADEIANSASGKS------ALLDEKRRLEARIAQLEEEL 1776
Cdd:TIGR00606 524 MEQLNHHTTTRTQME---MLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQledwlhSKSKEINQTRDRLAKLNKEL 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1777 EEEQSNMELLNERFRKTTLQVDTLNSELAgersAAQKSENARQQLERQNKELKAKlqelegsvkSKFKATISTLEAKIAQ 1856
Cdd:TIGR00606 601 ASLEQNKNHINNELESKEEQLSSYEDKLF----DVCGSQDEESDLERLKEEIEKS---------SKQRAMLAGATAVYSQ 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1857 LEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKqlKRQLEEAEEEATRANASRRKlQR 1936
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE--KRRDEMLGLAPGRQSIIDLK-EK 744
|
570 580
....*....|....*....|....*
gi 45382679 1937 ELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:TIGR00606 745 EIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1353-1739 |
8.73e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 8.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1353 ELLQEETRQKLNLSSRIRQLEEEK---NNLQEQQEEEEEARKNLEKQMLALQAQLAEAKkkvdddlgTIEGLEENKKKLL 1429
Cdd:PRK04863 283 VHLEEALELRRELYTSRRQLAAEQyrlVEMARELAELNEAESDLEQDYQAASDHLNLVQ--------TALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1430 KDMESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMVDL-DHQ-------------RQIVSNLEKKQKKFDQML 1488
Cdd:PRK04863 355 ADLEELEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLaDYQqaldvqqtraiqyQQAVQALERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1489 AEEKNISARYAEERDRAEA---EAREKETKaLSLARALEEALEAKEEFERqnkQLRADMEdlMSSKDDVGKNVHELEKSK 1565
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEateELLSLEQK-LSVAQAAHSQFEQAYQLVR---KIAGEVS--RSEAWDVARELLRRLREQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1566 RTLEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQARDEQNEEKKRMLvkqvRELEAELEDERKQRAL 1645
Cdd:PRK04863 509 RHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQ----EELEARLESLSESVSE 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1646 AVAAKKKMEMDLKDLEGQIEAANK------ARDEAIKQLRK-----------LQAQMKDYQRELEEARASRDEIFAQSKE 1708
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAArapawlAAQDALARLREqsgeefedsqdVTEYMQQLLERERELTVERDELAARKQA 656
|
410 420 430
....*....|....*....|....*....|..
gi 45382679 1709 sekklkgLEAEILQL-QEEFAASERARRHAEQ 1739
Cdd:PRK04863 657 -------LDEEIERLsQPGGSEDPRLNALAER 681
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
835-1268 |
8.75e-07 |
|
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: 54.20 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 835 KAFAKKQQQLSALKILQRNCAAY-----LKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEM 909
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCAAAITctaqcEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 910 ERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQ 989
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 990 LDEEEGARQKLQLE-KVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQE---M 1065
Cdd:TIGR00618 586 IPNLQNITVRLQDLtEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehaL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1066 MITDLEER-LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI 1144
Cdd:TIGR00618 666 SIRVLPKElLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSL 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1145 RELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaQQELRTKREQEVAELKKAIEEETKNHEA- 1223
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF-------FNRLREEDTHLLKTLEAEIGQEIPSDEDi 818
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1224 ------QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELA 1268
Cdd:TIGR00618 819 lnlqceTLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
880-1219 |
1.05e-06 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 54.14 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 880 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHdle 959
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILT--- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 960 srveeeeernqilqnEKKKMQGHIQDLEEQLDEEeGARQKLqlekvTAEAKIKkmeeeILLLEDQNSKFLKEKKLMEDRI 1039
Cdd:PLN02939 164 ---------------EKEALQGKINILEMRLSET-DARIKL-----AAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1040 AECTSQLAEEEE--KAKNLAkLKNKQEMM------ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAqiee 1111
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSP---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1112 LKIQ-LAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRdLSEELEALKTELEDTL 1190
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340
....*....|....*....|....*....
gi 45382679 1191 DTTAAQQELRTKREQEVAELKKAIEEETK 1219
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESK 400
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1047-1311 |
1.06e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1047 AEEEEKAKNLAKLKNKQEMMITDLEErlkKEEKTRQELEKAKRKLDG-----------ETTDLQDQIAELQAQIEELkiq 1115
Cdd:PRK04863 833 ADPEAELRQLNRRRVELERALADHES---QEQQQRSQLEQAKEGLSAlnrllprlnllADETLADRVEEIREQLDEA--- 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1116 lakkeEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELE-----ALKTELEDTL 1190
Cdd:PRK04863 907 -----EEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQrrahfSYEDAAEMLA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1191 DTTAAQQELRTKREQEVAELKKAiEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEK----NKQGLE----S 1262
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRA-REQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpADSGAEerarA 1060
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 45382679 1263 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAE 1311
Cdd:PRK04863 1061 RRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMRE 1109
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1081-1944 |
1.11e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1081 RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQlakkEEELQAA---LARGDEEAVQKNNalkvIRELQAQIAELQED 1157
Cdd:PRK04863 292 RRELYTSRRQLAAEQYRLVEMARELAELNEAESDL----EQDYQAAsdhLNLVQTALRQQEK----IERYQADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1158 LESEKASRNKA-------EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA------IEEETKNHEAQ 1224
Cdd:PRK04863 364 LEEQNEVVEEAdeqqeenEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAkqlcglPDLTADNAEDW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1225 IQEIR---QRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELTAKVT 1300
Cdd:PRK04863 444 LEEFQakeQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1301 EGERlRVELAEKANKLQNELDNVSSLLEEAEKkgikfakDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEknnlq 1380
Cdd:PRK04863 524 ELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQ----- 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1381 eqQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENkkkllkdMESLSQRLEEKAMAYDKLEKTKNRLQQEL 1460
Cdd:PRK04863 591 --LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEY-------MQQLLERERELTVERDELAARKQALDEEI 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1461 DDLmvdldHQRQiVSNLEKKQKKFDQM-------------LAEEKNISARYAEER------DraeaeareketkaLSLAR 1521
Cdd:PRK04863 662 ERL-----SQPG-GSEDPRLNALAERFggvllseiyddvsLEDAPYFSALYGPARhaivvpD-------------LSDAA 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1522 aleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK------SKRTL----------------EQQVE 1573
Cdd:PRK04863 723 -------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKavvvkiADRQWrysrfpevplfgraarEKRIE 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1574 EMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQ-----ARDEQNEEKKRMLVKQVRELEAELED----ERKQR 1643
Cdd:PRK04863 790 QLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGshlavAFEADPEAELRQLNRRRVELERALADhesqEQQQR 864
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1644 ALAVAAKKKMEMdLKDLEGQIEAAnkARDEAIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKGLEAEI 1720
Cdd:PRK04863 865 SQLEQAKEGLSA-LNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSDPEQF 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1721 LQLQEEFAASERARRHAEQERDELADEIANSASGKSAllDEKRRLEARIAqleeeleeeqsnmelLNERFRkttlqvdtl 1800
Cdd:PRK04863 938 EQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAKNSD---------------LNEKLR--------- 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1801 nselagersaaQKSENARQQLERQNKELKAKLQELE--GSVKSKFKATISTLEAKIAQLEEQLE-------QEAKERAAA 1871
Cdd:PRK04863 992 -----------QRLEQAEQERTRAREQLRQAQAQLAqyNQVLASLKSSYDAKRQMLQELKQELQdlgvpadSGAEERARA 1060
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1872 NKlvrrtekklKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1944
Cdd:PRK04863 1061 RR---------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1560-1838 |
1.16e-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: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARdeQNEEKKR-----------MLV 1626
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRelerirqeeiaMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1627 KQVRELE--------------AELEDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL 1692
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1693 EEARASRDEIFAQsKESEKKLKGLEAEILQLQEEFAASERaRRHAEQERDEladeiansasGKSALLDEKRR---LEARI 1769
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEE----------RKQAMIEEERKrklLEKEM 522
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1770 AQLEEELEEEQSNMELLNERFRKTTL----QVDTLNSELAGERSAAQKSENARQQLeRQNKELKAKLQELEGS 1838
Cdd:pfam17380 523 EERQKAIYEEERRREAEEERRKQQEMeerrRIQEQMRKATEERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1004-1193 |
1.23e-06 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 51.86 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1004 KVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQE 1083
Cdd:pfam00769 1 REEAEREKQELEERLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKRKLDGETTDLQD-------QIAELQAQIEELKIQLAKKEEELQAAL----------ARGDEEAVQKNNALKVIRE 1146
Cdd:pfam00769 81 LERELREAQEEVARLEEeserkeeEAERLQEELEEAREEEEEAKEKLLAAStspshhhseeSENEDDEEEEESYEGGSAE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45382679 1147 LQAQIAELQEDLESEKASRNKAEKQKRdLSEELEALKTELEDTLDTT 1193
Cdd:pfam00769 161 LSNDGDMDQLSDRIEEERVTEAEKNER-LQKQLKALKSELAQARDET 206
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1396-1943 |
1.29e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.75 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1396 QMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEkamaYDKLEKTKNRLQQELDDLMVDLDHQRQIVS 1475
Cdd:PRK01156 139 EMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISN----IDYLEEKLKSSNLELENIKKQIADDEKSHS 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1476 NLEKK-----------QKKFDQMLAEEKNISARyAEERDRAEAEAREKETKalslaraleealeaKEEFERQNKQLRADM 1544
Cdd:PRK01156 215 ITLKEierlsieynnaMDDYNNLKSALNELSSL-EDMKNRYESEIKTAESD--------------LSMELEKNNYYKELE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1545 EDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQARDEQN------ 1618
Cdd:PRK01156 280 ERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNnqilel 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1619 ---EEKKRMLVKQVRELEAELEDERKQR----ALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRE 1691
Cdd:PRK01156 359 egyEMDYNSYLKSIESLKKKIEEYSKNIermsAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1692 LEEARASRDEIFAQS------------------KESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAS 1753
Cdd:PRK01156 439 LDELSRNMEMLNGQSvcpvcgttlgeeksnhiiNHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSI 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1754 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRktTLQVDTLNSELAGERSA-AQKSENARQQLERQNKELKAKL 1832
Cdd:PRK01156 519 NEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK--SLKLEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQL 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1833 QELEG---SVKSKFKATISTLEAKIAQLEEQLeqeakeraaanKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANAR 1909
Cdd:PRK01156 597 NDLESrlqEIEIGFPDDKSYIDKSIREIENEA-----------NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI 665
|
570 580 590
....*....|....*....|....*....|....
gi 45382679 1910 MKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1943
Cdd:PRK01156 666 IPDLKEITSRINDIEDNLKKSRKALDDAKANRAR 699
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1561-1898 |
1.33e-06 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 53.10 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1561 LEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERdlqARDEQneekkrmlvKQVRELEAELedeR 1640
Cdd:COG4372 65 LNRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQK---ARQER---------EAVRQELAAA---R 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1641 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAE- 1719
Cdd:COG4372 130 QNLAKAQQELARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEAQNLATRa 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1720 --ILQLQEEFAASERARRHAEQERDELADEIANsasgksalldekrrLEARIAQLEEELEEEQSNMELLNErfrkttlQV 1797
Cdd:COG4372 210 naAQARTEELARRAAAAQQTAQAIQQRDAQISQ--------------KAQQIAARAEQIRERERQLQRLET-------AQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1798 DTLNSELAGERSAAQKSENARQQlerqnkelkaKLQELEGSVKSKFKATISTLEAkIAQLEEQLEQEAKeRAAANKLVR- 1876
Cdd:COG4372 269 ARLEQEVAQLEAYYQAYVRLRQQ----------AAATQRGQVLAGAAQRVAQAQA-QAQAQAQLLSSAN-RPAALRLRRs 336
|
330 340
....*....|....*....|...
gi 45382679 1877 -RTEKKLKEVFMQVEDERRHADQ 1898
Cdd:COG4372 337 pRRGRRQRPVTRHTTRRRRPATR 359
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1102-1379 |
1.58e-06 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 53.32 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKnnaLKviRELQAQIAE------LQEDLESEKASRNKAEKQK--- 1172
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK---LK--KEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1173 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKAIEEETKNHEAQiQEIRQRHATALEElSEQLEQAKRF 1249
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDR-PEIKEKMEAL 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1250 KANLEKNKQGLESD-NKELACEV-KVLQQVKAESEHKRKKLDAQVQELTAK--VTEGERLRVELAEKANKLQNELD---- 1321
Cdd:PLN03229 584 KAEVASSGASSGDElDDDLKEKVeKMKKEIELELAGVLKSMGLEVIGVTKKnkDTAEQTPPPNLQEKIESLNEEINkkie 663
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1322 ---NVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1379
Cdd:PLN03229 664 rviRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1496-1868 |
1.60e-06 |
|
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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 52.97 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1496 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEM 1575
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELAEEKDALLAQRAES 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1576 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMlvkQVRELEAELEDERKQRALAVAAKKKMEM 1655
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNSLAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1656 DLKDLEGQIEAANkardeaiKQLRKLQAQMKDYQRE--LEEARASRDEIFAqskeSEKKLKGLEAEIlqlqeEFAASERA 1733
Cdd:pfam07888 205 DTQVLQLQDTITT-------LTQKLTTAHRKEAENEalLEELRSLQERLNA----SERKVEGLGEEL-----SSMAAQRD 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1734 RRHAEQERDEL-ADEIANSASGKSALLDEKRrleariAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQ 1812
Cdd:pfam07888 269 RTQAELHQARLqAAQLTLQLADASLALREGR------ARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMERE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1813 KSE---------NARQQLE--RQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEQLEQEAKER 1868
Cdd:pfam07888 343 KLEvelgrekdcNRVQLSEsrRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
1016-1244 |
1.60e-06 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 53.13 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1016 EEILLLEDQNSKFLKEKKLMEDRIAEC-TSQLAEEEEKAKNLAKLKnkqemmitDLEERLKKEEKTRQELEKAKRKLDGE 1094
Cdd:COG1269 50 KVAEVAQISLSSLLSEVLDYLRSVKGLeGRLFILPEEVEKLEAELK--------SLEEVIKPAEKFSSEVEELTRKLEER 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1095 TTDLQDQIAELQAQIEELKIqLAKKEEELqAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN------KA 1168
Cdd:COG1269 122 LSELDEELEDLEDLLEELEP-LAYLDFDL-SLLRGLKFLLVRLGLVRREKLEALVGVIEDEVALYGENVEASvvivvaHG 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1169 EKQKRDLSEELEALKTELedtldttAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR---QRHATALEELSEQLE 1244
Cdd:COG1269 200 AEDLDKVSKILNELGFEL-------YEVPEFDGGPSELISELEEVIAEIQDELESLRSELEalaEKIAEELLAVREILE 271
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1081-1889 |
1.64e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 53.35 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1081 RQELEKAKRKLDGEttdlQDQIAELQAQIEELKIQLAKKEEELQAALARgdEEAVQknNALK---VIRELQAQIAELQED 1157
Cdd:COG3096 292 RRELYTSRQQLAAE----QYRHVDMSRELAELNGAEGDLEADYQAASDH--LNLVQ--TALRqqeKIERYQADLEELTIR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1158 LESEK-----ASRNKAEKQKRDLSEELE--ALKTELEDTLDTTAAQQELRTKREQEVAELKKA------IEEETKNHEAQ 1224
Cdd:COG3096 364 LEEQNevveeANERQEENEARAEAAELEvdELKSQLADYQQALDVQQTRAIQYQQAIAALERAkelchlPDLTADSAEEW 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1225 IQEIRQRHATALE---ELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQ-VQELTAKVT 1300
Cdd:COG3096 444 LETFQAKEEEATEkllSLEQKMSMAQAAHSQFEQAYQLVVAIAGELARSEAWDVARELLREGPDQRHLAEqVQPLRMRLS 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1301 EGERlRVELAEKANKLQNELDNVSSLLEEAEKkgikFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQ 1380
Cdd:COG3096 524 ELEQ-RLRQQQSAERLLADFCKRQGKNLDAEE----LEALHQELEALIESLSDSVSNAREQRMALRQEQEQLQSRIQSLM 598
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1381 EQQEEEEEARKNLEKqmlaLQAQLAEAKkkvdddlgtiegleENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEL 1460
Cdd:COG3096 599 QRAPVWLAAQNALEQ----LSEQSGEEF--------------TDSQDVTEYMQQLLEREREATVERDELGARKNALDEEI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1461 DDLMVDLDHQRQIVSNLEKK------QKKFDQMLAEEKN-ISARYAEERdraeaeaREKETKALSLARAleealeakeef 1533
Cdd:COG3096 661 ERLSQPGGSEDQRLNALAERfggvllSEIYDDVTIEDAPyFSALYGPSR-------HAIVVPDLSQVKE----------- 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1534 erQNKQLRADMEDLM------SSKDDVGKNVHELEK------SKRTL----------------EQQVEEMRTQLEELede 1585
Cdd:COG3096 723 --HLEGLTDCPEDLYliegdpQSFDDSVFSVDELEKavvvkiADRQWrysrfpeiplfgraarEQRLESLHAERDVL--- 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1586 lqATEDAKLRLEVN-MQAMKAQFERDLQ-----ARDEQNEEKKRMLVKQVRELEAEL----EDERKQRALAVAAKKKMEM 1655
Cdd:COG3096 798 --SERHATLSFDVQkTQRLHQAFSRFIGshlavAFEADPEAEIRQLNSRRNELERALsnheNDNQQQRIQFDQAKEGVTA 875
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1656 dlkdLEGQIEAANKARDEAikqlrkLQAQMKDYQRELEEAraSRDEIFAQS-----KESEKKLKGLEAE---ILQLQEEF 1727
Cdd:COG3096 876 ----LNRLIPQLNLLADES------LADRVEEIRERLDEA--QEAARFIQQhgntlSKLEPIASVLQSDpeqFEQLKEDY 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1728 AASERARRHAEQERDELADEIANSA----SGKSALLDEKRRLEARIAQLEEELeeeQSNMELLNERFRKTTLQVDTLNSE 1803
Cdd:COG3096 944 AQAQQMQRQARQQAFALTEVVQRRAhfsySDSAEMLSENSDLNEKLRQRLEQA---EAERTRAREQLRQHQAQLSQYNQV 1020
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1804 LAGERSAAQKSENARQQLERQNKEL----KAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTE 1879
Cdd:COG3096 1021 LASLKSSYDTKKELLNELQQELQDIgvraDSGAEERARIRRDELHAQLSTNRSRRNQLEKQLTFCEAEMDNLTRKLRKLE 1100
|
890
....*....|
gi 45382679 1880 KKLKEVFMQV 1889
Cdd:COG3096 1101 RDYFEMREQV 1110
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1308-1939 |
1.68e-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: 53.19 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1308 ELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNNLQEQQEE 1385
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1386 EEEA-----RKNLEKQMLALQAQLAEAKK-------KVDDDLGTIEGLEENKKKLLKDmeslsqrlEEKAMAYDKLEKTK 1453
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEIND--------KEKQVSLLLIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1454 NrlQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEF 1533
Cdd:pfam05483 252 K--ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1534 ERQNKqlrADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAMKAQFERD 1610
Cdd:pfam05483 330 TEEKE---AQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKFKNNKEVE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1611 LQARDEQNEEKKRMLV--KQVRELEAELEDERKQRALAVAAKKKmemDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDY 1688
Cdd:pfam05483 407 LEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1689 QRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAaserarrHAEQERDELADEIANSASGKSALLDEKRRLEAR 1768
Cdd:pfam05483 484 KLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDII-------NCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1769 IAQLEEELE----EEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKlqeleGSVKSKfk 1844
Cdd:pfam05483 557 FIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK-----GSAENK-- 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1845 aTISTLEAKIAQLEEQLEqeakerAAANKLVRRTEKKLKEVfmqvEDERRHADQYKEQMEKANARMKQLKrqleeaeeea 1924
Cdd:pfam05483 630 -QLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---------- 688
|
650
....*....|....*
gi 45382679 1925 tranasrrKLQRELD 1939
Cdd:pfam05483 689 --------KLQKEID 695
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1113-1371 |
1.70e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 53.52 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1113 KIQLAKKEEELQAALARGDEEAVQknnalkvirELQAQIAELQEdlesEKASRNKAEKQKR------DLSEELEALKTEL 1186
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEIVE---------ALQSALNWLEE----RKGSLERAKQYQQvidnfpKLSAELRQQLNNE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1187 ED---TLDTTAAQQELrtkrEQEVAELKKAIEEETknHEAQIQEIRQRH-ATALEELSEQLEQAKRFKANLEKNKQGLES 1262
Cdd:PRK10929 92 RDeprSVPPNMSTDAL----EQEILQVSSQLLEKS--RQAQQEQDRAREiSDSLSQLPQQQTEARRQLNEIERRLQTLGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1263 DNKELACEVKVLQQvkAESEHKRKKLD----AQV-----QELTakvtegeRLRVELAEK-ANKLQNELDNVSSLL----- 1327
Cdd:PRK10929 166 PNTPLAQAQLTALQ--AESAALKALVDelelAQLsannrQELA-------RLRSELAKKrSQQLDAYLQALRNQLnsqrq 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1328 ---EEAEKKGIKFAKDAASLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1371
Cdd:PRK10929 237 reaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
914-1768 |
2.59e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 914 QQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQIlqnekKKMQGHIQDLEEQLDEE 993
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKI-----ERYQADLEELEERLEEQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 994 EGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKF-----LKEKKLME--------DRIAECTSQLAEEEEKAKN-LAKL 1059
Cdd:PRK04863 368 NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYqqaldVQQTRAIQyqqavqalERAKQLCGLPDLTADNAEDwLEEF 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1060 KNKQEMM---ITDLEERLKKEEKTRQELEKAK---RKLDGETT--DLQDQIAELQAQIEELKIQlAKKEEELQAALARGD 1131
Cdd:PRK04863 448 QAKEQEAteeLLSLEQKLSVAQAAHSQFEQAYqlvRKIAGEVSrsEAWDVARELLRRLREQRHL-AEQLQQLRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1132 EEAVQKNNALKVIRELQaQIAELQEDLESEkasrnkaekqkrdLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELK 1211
Cdd:PRK04863 527 QRLRQQQRAERLLAEFC-KRLGKNLDDEDE-------------LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1212 KAIEEetknHEAQIQEIRQRHAtALEELSEQleqakrFKANLEkNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQ 1291
Cdd:PRK04863 593 ARIQR----LAARAPAWLAAQD-ALARLREQ------SGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEE 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1292 VQELTAKVT-EGERLRVeLAEKANK-----------------------------LQNELDNVSSLLEEAEK--------K 1333
Cdd:PRK04863 661 IERLSQPGGsEDPRLNA-LAERFGGvllseiyddvsledapyfsalygparhaiVVPDLSDAAEQLAGLEDcpedlyliE 739
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1334 GIKFAKDAASLESQLQDTQELLQEETRQkLNLS--------------SRIRQLEEEKNNLQEQQEEEEEARKNLE----- 1394
Cdd:PRK04863 740 GDPDSFDDSVFSVEELEKAVVVKIADRQ-WRYSrfpevplfgraareKRIEQLRAEREELAERYATLSFDVQKLQrlhqa 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1395 -KQMLALQAQLAEAkkkVDDDlgtiegleenkkkllKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdldhqRQI 1473
Cdd:PRK04863 819 fSRFIGSHLAVAFE---ADPE---------------AELRQLNRRRVELERALADHESQEQQQRSQLEQA-------KEG 873
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1474 VSNLEKKQKKFDqMLAEEKNIsaryaeerDRAEaEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskDD 1553
Cdd:PRK04863 874 LSALNRLLPRLN-LLADETLA--------DRVE-EIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQF----EQ 939
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1554 VGKNVHELEKSKRTLEQQVEEMrTQLEELEDELqATEDAklrleVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELE 1633
Cdd:PRK04863 940 LKQDYQQAQQTQRDAKQQAFAL-TEVVQRRAHF-SYEDA-----AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQ 1012
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1634 AELeDERKQRalavaakkkmemdLKDLEGQIEAANKARDEAIKQLRKLQAQmkdYQRELEE-ARASRDEIFAQSKESEKK 1712
Cdd:PRK04863 1013 AQL-AQYNQV-------------LASLKSSYDAKRQMLQELKQELQDLGVP---ADSGAEErARARRDELHARLSANRSR 1075
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1713 LKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALL------DEKRRLEAR 1768
Cdd:PRK04863 1076 RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLrlvkdnGVERRLHRR 1137
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1006-1244 |
2.83e-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: 52.45 E-value: 2.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1006 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTS----QLAEEEEKAKNLAKLKNKqemmITDLEErlKKEEKTR 1081
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPehldNVEEKVEKAQSLAKLVDQ----YKELVA--SERIVFQ 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1082 QELEK--------AKRKLDGETTDLQDQIAELQAQIEELKIQLA--KKEEELQAALARGDEEAVQKNNALKVIRELQAQI 1151
Cdd:pfam09731 261 QELVSifpdiipvLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAelKKREEKHIERALEKQKEELDKLAEELSARLEEVR 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1152 A--ELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEvAELKKAIEEETKNHEAQIQEIr 1229
Cdd:pfam09731 341 AadEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNEL- 418
|
250
....*....|....*
gi 45382679 1230 qrhATALEELSEQLE 1244
Cdd:pfam09731 419 ---LANLKGLEKATS 430
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
892-1137 |
3.33e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 51.65 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 892 LMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVeeeeernQI 971
Cdd:COG4942 33 AAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARL-------NA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 972 LQNEKkkmqghiqdleeqldeeegARQKLQLEKVTAEAKIKKMEEEILLL----EDQNSKFL--------KEKKLMEDRI 1039
Cdd:COG4942 106 LEVQE-------------------REQRRRLAEQLAALQRSGRNPPPALLvspeDAQRSVRLaiyygalnPARAERIDAL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1040 AECTSQLAEEEEKaknLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKK 1119
Cdd:COG4942 167 KATLKQLAAVRAE---IAAEQAELTTLLSEQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASA 243
|
250
....*....|....*...
gi 45382679 1120 EEelQAALARGDEEAVQK 1137
Cdd:COG4942 244 EA--AAAKAREAAAAAEA 259
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
880-1188 |
3.51e-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: 52.53 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 880 RQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQL-QAETELFAEAEEMRARLAAKKQELeeilhDL 958
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKnKALAERKDSANERLNSLEAQLKQL-----DK 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 959 ESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEeillledQNSKFLKEKKLMEDR 1038
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALET-------WYKRDLASLGVDPDV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1039 IAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEektRQELEKAKRKLDGETTDLQDQiaeLQAQIEELKIQLAK 1118
Cdd:pfam12128 770 IAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQR---RPRLATQLSNIERAISELQQQ---LARLIADTKLRRAK 843
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1119 KEEELQAAlargDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQ------KRDLSEELEALKTELED 1188
Cdd:pfam12128 844 LEMERKAS----EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLaqledlKLKRDYLSESVKKYVEH 915
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1339-1768 |
4.55e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.88 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1339 KDAASLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQlaEAKKKVDDDLgti 1418
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLVEMA---RELAELNEAESDLEQDYQAASDHLNLVQTALRQQ--EKIERYQADL--- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1419 egleenkkkllkdmESLSQRLEEKAMA-------YDKLEKTKNRLQQELDDLMVDL-DHQ-------------RQIVSNL 1477
Cdd:PRK04863 358 --------------EELEERLEEQNEVveeadeqQEENEARAEAAEEEVDELKSQLaDYQqaldvqqtraiqyQQAVQAL 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1478 EKKQKKFDQMLAEEKNISARYAEERDRAEA---EAREKETKaLSLARALEEALEAKEEFERQnkqLRADMEdlMSSKDDV 1554
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFQAKEQEateELLSLEQK-LSVAQAAHSQFEQAYQLVRK---IAGEVS--RSEAWDV 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1555 GKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQARDEQNEEKKRMLvkqvRELEA 1634
Cdd:PRK04863 498 ARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA--------ERLLAEFCKRLGKNLDDEDELEQLQ----EELEA 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1635 ELEDERKQRALAVAAKKKMEMDLKDLEGQIEaankardeaikQLRKLQAQMKDYQRELEEARASRDEIFAQSKesekklk 1714
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQ-----------RLAARAPAWLAAQDALARLREQSGEEFEDSQ------- 627
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1715 GLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEAR 1768
Cdd:PRK04863 628 DVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
905-1503 |
5.08e-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: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 905 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqghiq 984
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 985 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMED--------------------RIAECts 1044
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1045 qLAEEEEKAKNLAKLK-NKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQIEELKIQLAKKEEEL 1123
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1124 QAALA-RGDEEAVQKNNALKVIRELqaqiaeLQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK 1202
Cdd:TIGR01612 1698 EIGIIeKIKEIAIANKEEIESIKEL------IEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAG 1771
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1203 REQEVAElkkaiEEETKNheaqiqEIRQRHATALEELSEQLEQAKRFKANLeknkqglesDNKElacevkvLQQVKAESE 1282
Cdd:TIGR01612 1772 CLETVSK-----EPITYD------EIKNTRINAQNEFLKIIEIEKKSKSYL---------DDIE-------AKEFDRIIN 1824
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1283 HKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVS---------------------SLLEEAEKKGIKFAKDA 1341
Cdd:TIGR01612 1825 HFKKKLDHVNDKFTKEYSKINEGFDDISKSIENVKNSTDENLlfdilnktkdayagiigkkyySYKDEAEKIFINISKLA 1904
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1342 ASLESQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNNLQEQQEEEEEARKNlEKQMLAL- 1400
Cdd:TIGR01612 1905 NSINIQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIi 1983
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1401 --QAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEE---------------KAMAYDKLEKTKNRLQQELDDL 1463
Cdd:TIGR01612 1984 feNQQLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKF 2063
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 45382679 1464 MVDLDHQ--RQIVSNLEKKQKKFDQMLAEEKNISARYAEERD 1503
Cdd:TIGR01612 2064 GIDFDVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1003-1442 |
5.22e-06 |
|
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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 51.65 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1003 EKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRiaectsqlaEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQ 1082
Cdd:pfam05557 28 ARIELERKASALARQLERESDRNQELQKRIRLLEKR---------EAEAEEALREQAELNRLKKKNLEALNKKLNEKESQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1083 ELEKAKRKLDgettdLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQE------ 1156
Cdd:pfam05557 99 LADAREVISC-----LKNELSELRRQIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEaeqrik 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1157 -----------------DLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK--REQEVAELKKAIEEE 1217
Cdd:pfam05557 174 elefeiqsqeqdseivkNSKSELARIPELERELERLREHNKHLNENIENKLLLKEEVEDLKRKleREEGYREELATLELE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1218 TKNHEAQIQE---IRQRHATAL---EELSEQLEQAKRFKANLEKNKQGLESDnkelaceVKVLQQVKAESEHKRKKLDAQ 1291
Cdd:pfam05557 254 KEKLEQELKSwekLAQDTGLNLrspEDLSRRIEQLQQREITLKEENSSLTSS-------ARQLEKAQRELEQELAQYLKN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1292 VQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1371
Cdd:pfam05557 327 IEDLNKKLKRHKALVRRLQRRVLLLTKERDGMRAILESYDKE-LTPSNYSPQLLERIEEAEDMTQDMQAHNEEMEAQLSV 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1372 LEEEKNNLqeqqeeeeearkNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKlLKDMESLSQRLEEK 1442
Cdd:pfam05557 406 AEEELGGY------------KQQATTLERELQALRQQESLADPSYSKEEVDSLRRK-LETLEAERQRLREQ 463
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1078-1355 |
5.43e-06 |
|
Intermediate filament protein;
Pssm-ID: 425436 [Multi-domain] Cd Length: 313 Bit Score: 50.68 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1078 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALK 1142
Cdd:pfam00038 18 DKVRF-LEQQNKDLETKISELRQKkgaepsrlyslyereIRELRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1143 VIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKAIEEETKNHE 1222
Cdd:pfam00038 97 LRQSAEADIVGLRKDLDEATLARVDLEMKIESLKEELAFLKKN-----------------HEEEVRELQSQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1223 aqIQEIRQRH-ATALEELSEQLE-QAKRFKANLEKN-KQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKV 1299
Cdd:pfam00038 160 --MDAARKLDlTSALAEIRAQYEeIAEKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1300 TEGERLRVELAEKANKLQNELDNVSSLLE--EAEKKGIKfakdaASLESQLQDTQELL 1355
Cdd:pfam00038 238 KQKASLERQLAETEERYELQLADYQELISelEAELQQIR-----QEMARQLREYQELL 290
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1102-1358 |
5.91e-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: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 51.76 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELKIQLAKKEeelQAALARGDEEAVQKNNAlKVIRELQAQIAEL---QEDLES--EKASRNKAEKQKRDLS 1176
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDD---AAQNALADKERAEADRQ-RLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1177 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKAIEEE---TKNH-EAQIQEIRQRHATALEELSEQLE 1244
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQEQlddAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1245 QAKRFKANLEKNKQGLESDNKelacevkvlqqvKAESEHKRKKLDAQVQELTAKVTEgerlrvelaEKANklqneldnvs 1324
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAE---------SDAN---------- 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 45382679 1325 SLLEEAEKKGIKFAKDAASLESQLQ-DTQELLQEE 1358
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1142-1317 |
5.98e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 50.73 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1142 KVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL---EALKTELEDTLDTTAAQqelRTKREQEVAELKKAIEEEt 1218
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQALLAELAGA---GAAAEGRAGELAQELDSE- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1219 knheaqiQEIRQRHATALEELSEQLEQAKRfkanleknkqglesdnkELAcevkVLQQVKAESEHKRKKLDAQVQELtak 1298
Cdd:PRK09039 129 -------KQVSARALAQVELLNQQIAALRR-----------------QLA----ALEAALDASEKRDRESQAKIADL--- 177
|
170
....*....|....*....
gi 45382679 1299 vteGERLRVELAEKANKLQ 1317
Cdd:PRK09039 178 ---GRRLNVALAQRVQELN 193
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1097-1730 |
6.30e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 6.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1097 DLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLS 1176
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1177 EELEA---LKTELEDTLDTTAAQQELRTKREQEVAELKKAIE---EETKNHEAQIQEIRQRH--ATALEELSEQLEQAKR 1248
Cdd:PRK01156 267 MELEKnnyYKELEERHMKIINDPVYKNRNYINDYFKYKNDIEnkkQILSNIDAEINKYHAIIkkLSVLQKDYNDYIKKKS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1249 FKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLdaqvqeltakvtegERLRVELAEKANKLQNELDNVSSLLE 1328
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNI--------------ERMSAFISEILKIQEIDPDAIKKELN 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1329 EAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIR------QLEEEKNNlqeqqeeeeEARKNLEKQMLALQA 1402
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgtTLGEEKSN---------HIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1403 QLAEAKKKVDDdlgtiegLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKnrlQQELDDLMVDLdhqrqivSNLEKKQK 1482
Cdd:PRK01156 484 KIREIEIEVKD-------IDEKIVDLKKRKEYLESEEINKSINEYNKIESA---RADLEDIKIKI-------NELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1483 KFDQMLAEEKNISARYAEERdraeaeaREKETKALSLARAleealeakeeferqnkqlrADMEDLMSSKDDVGKNVHELE 1562
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSK-------RTSWLNALAVISL-------------------IDIETNRSRSNEIKKQLNDLE 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1563 KSKRTLEQQVEEMRT----QLEELEDELQATEDAKLRLEVNMQAMkaqferdlqardeqneEKKRMLVKQVRELEAELED 1638
Cdd:PRK01156 601 SRLQEIEIGFPDDKSyidkSIREIENEANNLNNKYNEIQENKILI----------------EKLRGKIDNYKKQIAEIDS 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1639 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEaikqLRKLQAQMKDYQRELEEARASRDEIFaqskESEKKLKGLEA 1718
Cdd:PRK01156 665 IIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR----LESTIEILRTRINELSDRINDINETL----ESMKKIKKAIG 736
|
650
....*....|..
gi 45382679 1719 EILQLQEEFAAS 1730
Cdd:PRK01156 737 DLKRLREAFDKS 748
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1628-1950 |
6.54e-06 |
|
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 characteristic 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: 50.84 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1628 QVRELEAELEDERkqralavAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1707
Cdd:pfam19220 49 RLLELEALLAQER-------AAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1708 ESEKKLKG-------LEAEILQLQEEFAASERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQ 1780
Cdd:pfam19220 122 ALERQLAAeteqnraLEEENKALREEAQAAEKALQRAEGELATARERLA-------LLEQENRRLQALSEEQAAELAELT 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1781 SNMELLNERFRKTTLQVDTLNSELAGERSAAQKSEnarqqlerqnkelkaklqelegsvkskfkatistleakiAQLEEQ 1860
Cdd:pfam19220 195 RRLAELETQLDATRARLRALEGQLAAEQAERERAE---------------------------------------AQLEEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1861 LEQEAKERA-------AANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRK 1933
Cdd:pfam19220 236 VEAHRAERAslrmkleALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQE 315
|
330
....*....|....*..
gi 45382679 1934 LQRELDDATEANEGLSR 1950
Cdd:pfam19220 316 MQRARAELEERAEMLTK 332
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1447-1712 |
8.32e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1447 DKLEKTKNR-LQQELDDLMVDLDH-QRQIVS--------------NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAR 1510
Cdd:PHA02562 169 DKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1511 EKETKALSLaraleealeakeeferqnKQLRADMEDLMSSKDDVGKNVHELEKSKR--TLEQQVEEMRTQLEELEDelqa 1588
Cdd:PHA02562 249 DIEDPSAAL------------------NKLNTAAAKIKSKIEQFQKVIKMYEKGGVcpTCTQQISEGPDRITKIKD---- 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1589 tedaklrlevNMQAMKAQFERDLQARDEQNE--EKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEmdlkdlegqiea 1666
Cdd:PHA02562 307 ----------KLKELQHSLEKLDTAIDELEEimDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVK------------ 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 45382679 1667 ankardeaiKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1712
Cdd:PHA02562 365 ---------AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1001-1464 |
8.69e-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: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1001 QLEKVTAEA-------KIKKMEEEILLLEDQNSKFLKEKKLMEDRIAEC-TSQLAEEEEKAKNLAKLKNKQEMMITDLEE 1072
Cdd:TIGR01612 1154 DLEDVADKAisnddpeEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIeKDKTSLEEVKGINLSYGKNLGKLFLEKIDE 1233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1073 RLKKEEKTRQELEKAKRKLDG------ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI-- 1144
Cdd:TIGR01612 1234 EKKKSEHMIKAMEAYIEDLDEikekspEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKIIed 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1145 -----------RELQAQIAELQED--------------------------LESEKASRNKAEKQKRDLSEE--------- 1178
Cdd:TIGR01612 1314 fseesdindikKELQKNLLDAQKHnsdinlylneianiynilklnkikkiIDEVKEYTKEIEENNKNIKDEldkseklik 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1179 -------LEALKTELEDTLD----------TTAAQQELRTKREQEVAELKKAIE------------EETKNHEAQIQEIR 1229
Cdd:TIGR01612 1394 kikddinLEECKSKIESTLDdkdidecikkIKELKNHILSEESNIDTYFKNADEnnenvlllfkniEMADNKSQHILKIK 1473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1230 QRHATA-----LEELSEQLEQAKRFKANLEKNKQGLESD---------------NKELACEVK-VLQQVKAESE------ 1282
Cdd:TIGR01612 1474 KDNATNdhdfnINELKEHIDKSKGCKDEADKNAKAIEKNkelfeqykkdvtellNKYSALAIKnKFAKTKKDSEiiikei 1553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1283 ---HKRKKLDAQVQELTAKVTEGERLRVE-LAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELlqEE 1358
Cdd:TIGR01612 1554 kdaHKKFILEAEKSEQKIKEIKKEKFRIEdDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESI--EK 1631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1359 TRQKLNLSSRIRQLEEEKNN---LQEQQEEEEEARKNLEKQmlalqaqlaeaKKKVDDDLGTIEGLEENKKKLLKDME-S 1434
Cdd:TIGR01612 1632 KISSFSIDSQDTELKENGDNlnsLQEFLESLKDQKKNIEDK-----------KKELDELDSEIEKIEIDVDQHKKNYEiG 1700
|
570 580 590
....*....|....*....|....*....|.
gi 45382679 1435 LSQRLEEKAMA-YDKLEKTKNRLQQELDDLM 1464
Cdd:TIGR01612 1701 IIEKIKEIAIAnKEEIESIKELIEPTIENLI 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1579-1958 |
9.11e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1579 LEELEdELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEkkRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLK 1658
Cdd:PTZ00121 1029 IEELT-EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQD--EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1659 DLEGQIEAANKARdEAIKQLRKLqaqmkdyqRELEEARasRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAE 1738
Cdd:PTZ00121 1106 TETGKAEEARKAE-EAKKKAEDA--------RKAEEAR--KAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAED 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1739 QERDELA---DEIANSASGKSAllDEKRRLEAriAQLEEELEEEQSNMELLNERFRKTTLQVDtlnselagerSAAQKSE 1815
Cdd:PTZ00121 1175 AKKAEAArkaEEVRKAEELRKA--EDARKAEA--ARKAEEERKAEEARKAEDAKKAEAVKKAE----------EAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1816 NARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAqleEQLeQEAKERAAANKLVRRTEKKLKEVFMQVEDERRH 1895
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKA---DEL-KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKK 1316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1896 ADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1958
Cdd:PTZ00121 1317 ADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK 1379
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1006-1331 |
9.81e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.60 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1006 TAEAKIKKMEEEILLL---EDQNSKFLKE---------KKLMEDR------IAECTSQLAEEEEKAKNLAKLKN-----K 1062
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEEFSQFVELTEsgdyvE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1063 QEMMITDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQIEELKIQ---------------LAKKEEELQAAL 1127
Cdd:PRK04778 196 AREILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeiqdLKEQIDENLALL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1128 ARGDEEAVQKNNalkviRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEV 1207
Cdd:PRK04778 273 EELDLDEAEEKN-----EEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSYTLNESEL 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1208 aELKKAIEEETKNHEAQIQEIRQRHATA----------LEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQV 1277
Cdd:PRK04778 348 -ESVRQLEKQLESLEKQYDEITERIAEQeiayselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRNK 426
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1278 KAESEHKRKKL------DAQVQELTAKVTEGERLRVELaekaNKLQNELDNVSSLLEEAE 1331
Cdd:PRK04778 427 LHEIKRYLEKSnlpglpEDYLEMFFEVSDEIEALAEEL----EEKPINMEAVNRLLEEAT 482
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
688-712 |
1.25e-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: 1.25e-05
10 20
....*....|....*....|....*
gi 45382679 688 YKESLTKLMATLRNTNPNFVRCIIP 712
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1002-1170 |
1.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1002 LEKVTAEAKIKKMEEEIllledqnSKFLKE-KKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQ-EMMITDLEERLKKEEK 1079
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRErRNELQKLEKRLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1080 T----RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvqKNNAL-KVIRELQAQIAEL 1154
Cdd:PRK12704 97 NldrkLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEA--KEILLeKVEEEARHEAAVL 174
|
170
....*....|....*.
gi 45382679 1155 QEDLESEkaSRNKAEK 1170
Cdd:PRK12704 175 IKEIEEE--AKEEADK 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
876-1183 |
1.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 876 LQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERkhqqLLEEKNILAEQLQAETELFAEAEEmraRLAAKKQELEEil 955
Cdd:PRK03918 459 AELKRIEKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLKELEEKLKKYNLE---ELEKKAEEYEK-- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 956 hdLESRVEEEEERNQILQNEKKKMQGhiqdleeqldeeegarqkLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKklm 1035
Cdd:PRK03918 530 --LKEKLIKLKGEIKSLKKELEKLEE------------------LKKKLAELEKKLDELEEELAELLKELEELGFES--- 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 edrIAECTSQLAEEEEKAKNLAKLKNKQEmmitDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQIEELKIQ 1115
Cdd:PRK03918 587 ---VEELEERLKELEPFYNEYLELKDAEK----ELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKK 655
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1116 LAKKE-EELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1183
Cdd:PRK03918 656 YSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVE 724
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1264-1510 |
1.38e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 50.02 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1264 NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELaekaNKLQNELDNVSSLLEEAEKKGIKFAKDAAS 1343
Cdd:COG4372 66 NRNLRSGVFQLDDIRPQLRALRTELGTAQGEKRAAETEREAARSEL----QKARQEREAVRQELAAARQNLAKAQQELAR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1344 LESQLQDTQELLQeetrqklNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvDDDLGTIEGLEE 1423
Cdd:COG4372 142 LTKQAQDLQTRLK-------TLAEQRRQLEAQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQE-AQNLATRANAAQ 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1424 NKKKLLKDMESLSQRLEEKAMAYDKLEKTKNrlqQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEERD 1503
Cdd:COG4372 214 ARTEELARRAAAAQQTAQAIQQRDAQISQKA---QQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRLRQ 290
|
....*..
gi 45382679 1504 RAEAEAR 1510
Cdd:COG4372 291 QAAATQR 297
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1071-1457 |
1.48e-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: 50.21 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1071 EERLKKEEKTRQELEKAKRKLDGETTDLQD-------QIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV 1143
Cdd:pfam10174 358 ESFLNKKTKQLQDLTEEKSTLAGEIRDLKDmldvkerKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1144 IRELQAQIAELQEDLESEKASRNKAEKQKRdlsEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaieeETKNHEA 1223
Cdd:pfam10174 438 LTTLEEALSEKERIIERLKEQREREDRERL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK-----EHASSLA 509
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1224 QIQEIRQRHATALE-ELSEQLEQAKRFKANLEKNKQGLESD--NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVT 1300
Cdd:pfam10174 510 SSGLKKDSKLKSLEiAVEQKKEECSKLENQLKKAHNAEEAVrtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILR 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1301 EGERLRVELAEKANKLQN-----------ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQ--------EETRQ 1361
Cdd:pfam10174 590 EVENEKNDKDKKIAELESltlrqmkeqnkKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQleelmgalEKTRQ 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1362 KLN-----LSSRIRQLEEEKNNLQEQQEEEeeaRKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLs 1436
Cdd:pfam10174 670 ELDatkarLSSTQQSLAEKDGHLTNLRAER---RKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMAL- 745
|
410 420
....*....|....*....|.
gi 45382679 1437 qRLEEKAMAYDKLEKTKNRLQ 1457
Cdd:pfam10174 746 -KREKDRLVHQLKQQTQNRMK 765
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
932-1490 |
1.54e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 50.29 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 932 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 1011
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1012 K-KMEEEILLLEDQN--SKFLKEKKLMEDRIAECTSQLAEEEEKAKNlaklknkqemmITDLEERLKKEEKTRQeleKAK 1088
Cdd:PRK01156 228 NnAMDDYNNLKSALNelSSLEDMKNRYESEIKTAESDLSMELEKNNY-----------YKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1089 RKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQ--AALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRN 1166
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKklSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1167 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRhataLEELSEQL--- 1243
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1244 ---------------EQAKRFKANLEKNKQGLESDNKELACEVKVL-----QQVKAESEHKRKKL------DAQVQELTA 1297
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIdekivDLKKRKEYLESEEInksineYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1298 KVTEGERLRVELAEKANKLQNELDNVSSL-LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLN-LSSRIRQLEEE 1375
Cdd:PRK01156 530 DLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNdLESRLQEIEIG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1376 KNNLQEQQEEEEEARKNlEKQMLALQAQLAEAKKKVDDdlgTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNR 1455
Cdd:PRK01156 610 FPDDKSYIDKSIREIEN-EANNLNNKYNEIQENKILIE---KLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKK 685
|
570 580 590
....*....|....*....|....*....|....*
gi 45382679 1456 LQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1490
Cdd:PRK01156 686 SRKALDDAKANRARLESTIEILRTRINELSDRIND 720
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1295-1649 |
1.55e-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 characteristic 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: 49.68 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1295 LTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA---EKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQ 1371
Cdd:pfam19220 36 IEAILRELPQAKSRLLELEALLAQERAAYGKLRRELaglTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1372 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEK 1451
Cdd:pfam19220 116 KTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1452 TKNRLQQELDDlmvdldhQRQIVSNLEKKqkkFDQMLAEEKNISARYAEERDRAEAEAReketkalSLARALEEALEAKE 1531
Cdd:pfam19220 196 RLAELETQLDA-------TRARLRALEGQ---LAAEQAERERAEAQLEEAVEAHRAERA-------SLRMKLEALTARAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1532 EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLE--VNM-----QAMK 1604
Cdd:pfam19220 259 ATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerAEMltkalAAKD 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1605 AQFER------DLQARDEQ----NEEKKRMLVKQVRELEAELEDERKQRALAVAA 1649
Cdd:pfam19220 339 AALERaeeriaSLSDRIAEltkrFEVERAALEQANRRLKEELQRERAERALAQGA 393
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1006-1241 |
1.57e-05 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 49.64 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1006 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECtsqlaeEEEKAKNLAKLKNKQEMMiTDLEERLKKEEKTRQELE 1085
Cdd:COG4372 92 TAQGEKRAAETEREAARSELQKARQEREAVRQELAAA------RQNLAKAQQELARLTKQA-QDLQTRLKTLAEQRRQLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1086 KAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE--------------------LQAALARGDEEAVQKNnalKVIR 1145
Cdd:COG4372 165 AQAQSLQASQKQLQASATQLKSQVLDLKLRSAQIEQEaqnlatranaaqarteelarRAAAAQQTAQAIQQRD---AQIS 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1146 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaAQQELRTKREQEVAELKKAIEEETKNHEAQI 1225
Cdd:COG4372 242 QKAQQIAARAEQIRERERQLQRLETAQARLEQEVAQLEAYYQAYVRL--RQQAAATQRGQVLAGAAQRVAQAQAQAQAQA 319
|
250
....*....|....*.
gi 45382679 1226 QEIRQRHATALEELSE 1241
Cdd:COG4372 320 QLLSSANRPAALRLRR 335
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1084-1240 |
2.18e-05 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKRKLDGETTDLQDQIAELQAQIEelkiQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA 1163
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELD----RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1164 SRNKAEKQKRDLsEELEALKTELEDTLDTTAAQQE-LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1240
Cdd:pfam00529 132 LAPIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
1170-1408 |
2.24e-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: 49.57 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1170 KQKRDLSEELEALKTELEDT----------LDTTAAQQEL-RTKREQEVAE----LKKAIEEETKNHEAQIQE----IRQ 1230
Cdd:pfam07902 78 KSLEEMLSQLKELNLELTDTknsnlwskikLNNNGMLREYhNDTIKTEIVEsaegIATRISEDTDKKLALINEtisgIRR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1231 RHATALEELSEqleqakRFKANLEKNKQGLESDNKELACEVKV-LQQVKAESEHKRKKLDAQVQELTAKVTEG------- 1302
Cdd:pfam07902 158 EYQDADRQLSS------SYQAGIEGLKATMASDKIGLQAEIQAsAQGLSQRYDNEIRKLSAKITTTSSGTTEAyeskldd 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1303 ---------ERLRVELAEKANKL----QNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQEL----------LQEET 1359
Cdd:pfam07902 232 lraeftrsnQGMRTELESKISGLqstqQSTAYQISQEISNREGAVSRVQQDLDSYQRRLQDAEKNyssltqtvkgLQSTV 311
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 45382679 1360 R-QKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAK 1408
Cdd:pfam07902 312 SdPNSKLESRITQLAGLIEQKVTRGDVESIIRQSGDSIMLAIKAKLPQSK 361
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1081-1243 |
2.25e-05 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 47.75 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1081 RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKvirelQAQIAELQEDLES 1160
Cdd:COG1579 26 IKEIRKALKKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAVKD-----ERELRALNIEIQI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1161 EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQqelrtkrEQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1240
Cdd:COG1579 101 AKERINSLEDELAELMEEIEKLEKEIEDLKERLERL-------EKNLAEAEARLEEEVAEIREEGQELSSKREELKEKLD 173
|
...
gi 45382679 1241 EQL 1243
Cdd:COG1579 174 PEL 176
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1265-1915 |
2.59e-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: 49.36 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1265 KELACEVKVLQQVkaeSEHKRKKLDAQVQELTAkvtegerlrVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKdaasl 1344
Cdd:pfam07111 76 RRLEEEVRLLRET---SLQQKMRLEAQAMELDA---------LAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGS----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1345 ESQLQDTQELLQEEtrqklnLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEEN 1424
Cdd:pfam07111 139 QRELEEIQRLHQEQ------LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1425 KKKLLKDMESLSQRLEEKAMA---YDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARYAEE 1501
Cdd:pfam07111 213 LEAQVTLVESLRKYVGEQVPPevhSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1502 RDRAEAEAREKETKALSLARALEEALEAkeeferqnkQLRADMEDLMSSKDDVGKNVHELEK--SKRTLEQQVEEMRTQL 1579
Cdd:pfam07111 293 SDSLEPEFPKKCRSLLNRWREKVFALMV---------QLKAQDLEHRDSVKQLRGQVAELQEqvTSQSQEQAILQRALQD 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1580 EELEDELQATEDAKLRLEVNmQAMKAQfeRDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKD 1659
Cdd:pfam07111 364 KAAEVEVERMSAKGLQMELS-RAQEAR--RRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSY 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1660 LEGQIEAANK--ARDEAIKQLRKLQAQM--------KDYQRELEEARASRDEIFAQSKesekklkgLEAEILQLQeefaa 1729
Cdd:pfam07111 441 AVRKVHTIKGlmARKVALAQLRQESCPPpppappvdADLSLELEQLREERNRLDAELQ--------LSAHLIQQE----- 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1730 SERARRHAEQERdeladeiansasgksalldekRRLEARIAQLEEELEEEQSNMELLNERfrkttlqvdtLNSELAGERS 1809
Cdd:pfam07111 508 VGRAREQGEAER---------------------QQLSEVAQQLEQELQRAQESLASVGQQ----------LEVARQGQQE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1810 AAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKiaqLEEQLEQEAKERAAANKLVRRT--EKKLKEVFM 1887
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQHRAtqEKERNQELR 633
|
650 660
....*....|....*....|....*...
gi 45382679 1888 QVEDERRhadqyKEQMEKANARMKQLKR 1915
Cdd:pfam07111 634 RLQDEAR-----KEEGQRLARRVQELER 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1140-1410 |
2.60e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.95 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1140 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtk 1219
Cdd:COG4942 29 AAFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNAL-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1220 nheaQIQEIRQRhatalEELSEQLEQAKRFKAN-----LEKNKQGLESDN--KELACEVKVLQQVKAESEHKRKKLDAQV 1292
Cdd:COG4942 107 ----EVQEREQR-----RRLAEQLAALQRSGRNpppalLVSPEDAQRSVRlaIYYGALNPARAERIDALKATLKQLAAVR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1293 QELTAKVTEGERLRVELAEKANKLQNELdnvsslleeAEKKGIKfakdaASLESQLQDTQELLQEETRQKLNLSSRIRQL 1372
Cdd:COG4942 178 AEIAAEQAELTTLLSEQRAQQAKLAQLL---------EERKKTL-----AQLNSELSADQKKLEELRANESRLKNEIASA 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 45382679 1373 EEEknnlqeqqeEEEEARKNLEKQMLALQAQLAEAKKK 1410
Cdd:COG4942 244 EAA---------AAKAREAAAAAEAAAARARAAEAKRT 272
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
998-1161 |
2.75e-05 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 47.75 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 998 QKLQLEKVTAEAKIK-------KMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKaknLAKLKNKQeMMITDL 1070
Cdd:COG1579 13 QKLDLEKDRLEPRIKeirkalkKAKAELEALNKALEALEIELEDLENQVSQLESEIQEIRER---IKRAEEKL-SAVKDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1071 EErLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNnalKVIRELQAQ 1150
Cdd:COG1579 89 RE-LRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIR---EEGQELSSK 164
|
170
....*....|.
gi 45382679 1151 IAELQEDLESE 1161
Cdd:COG1579 165 REELKEKLDPE 175
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1084-1245 |
2.90e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.42 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKrkldgeTTDLQDQIAELQAQieelkiqLAKKEEE---LQAALARGDEEAvqknnalkviRELQAQIAELQEDLES 1160
Cdd:PRK09039 71 LERQG------NQDLQDSVANLRAS-------LSAAEAErsrLQALLAELAGAG----------AAAEGRAGELAQELDS 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1161 EKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELS 1240
Cdd:PRK09039 128 EKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIADLGRRLNVALAQRV 189
|
....*
gi 45382679 1241 EQLEQ 1245
Cdd:PRK09039 190 QELNR 194
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
1065-1334 |
3.25e-05 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 48.90 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1065 MMITDLEERLK--KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKI---QLAKKEEELQAALARGDEEAVQKNN 1139
Cdd:COG1269 31 VHLEDLEEGEKglKELEKLKVAEVAQISLSSLLSEVLDYLRSVKGLEGRLFIlpeEVEKLEAELKSLEEVIKPAEKFSSE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1140 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKrDLSEELEALKTELEDTLDttaAQQELRTKREQEVAELKKAIEEETK 1219
Cdd:COG1269 111 VEELTRKLEERLSELDEELEDLEDLLEELEPLA-YLDFDLSLLRGLKFLLVR---LGLVRREKLEALVGVIEDEVALYGE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1220 NHEAQIQEIRQRHATALEELSEQLeqakrfkanlekNKQGLEsdnkelacevkvLQQVKAESEHKRKKLDAQVQELTAKV 1299
Cdd:COG1269 187 NVEASVVIVVAHGAEDLDKVSKIL------------NELGFE------------LYEVPEFDGGPSELISELEEVIAEIQ 242
|
250 260 270
....*....|....*....|....*....|....*
gi 45382679 1300 TEGERLRVELAEKANKLQNELDNVSSLLEEAEKKG 1334
Cdd:COG1269 243 DELESLRSELEALAEKIAEELLAVREILEIEKALG 277
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1423-1959 |
3.28e-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: 49.20 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1423 ENKKKLLKDMESLSQRLEEKAMAYD-------KLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNIS 1495
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAkkkslhgKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1496 ARYAEERDRAEAEAReketkalslaraleealeakeeFERQNKQLRADMEDLMSSKddvgkNVHELEKSKRTLEQQVEEM 1575
Cdd:TIGR00618 243 AYLTQKREAQEEQLK----------------------KQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1576 RTQLEELEDELQATEDAKLRLEVNMQAM-KAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKK-- 1652
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRaKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqh 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1653 -MEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASE 1731
Cdd:TIGR00618 376 tLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1732 RARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAqleeELEEEQSNMELLNERFRKTTLQVdTLNSELAGERSAA 1811
Cdd:TIGR00618 456 LEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA----RLLELQEEPCPLCGSCIHPNPAR-QDIDNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1812 QKSENARQQLERQNKELKAKLQELEGSVKSkFKATIsTLEAKIAQLEEQLEQEAKEraAANKLVRRTEKKLKEVFMQVED 1891
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRAS-LKEQM-QEIQQSFSILTQCDNRSKE--DIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1892 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEL 674
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1274-1402 |
3.82e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1274 LQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAAslESQLQDTQE 1353
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 45382679 1354 LLQEETRqklnlSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQA 1402
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1085-1341 |
3.85e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1085 EKAKRKLDGETTDLQDQIAELqaqiEELKIQLAKKEEELQAALArgdeeavqknnalkvirelqaQIAELQEDLEsekas 1164
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASL----EELERELEQKAEEAEALLK---------------------EAEKLKEELE----- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1165 rnkaeKQKRDLSEELEALKTELEDtldttaaqqelrtKREQEVAELKKAIEEETKN-HEAQIQEIRQRHATALEELSEQL 1243
Cdd:PRK00409 555 -----EKKEKLQEEEDKLLEEAEK-------------EAQQAIKEAKKEADEIIKElRQLQKGGYASVKAHELIEARKRL 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1244 EQAKRfKANLEKNKQGLESDNKELACEVKVLQ-QVKAESEHKRKKLDAQVQE----LTAKVTEGERLRVELAEKANKLQN 1318
Cdd:PRK00409 617 NKANE-KKEKKKKKQKEKQEELKVGDEVKYLSlGQKGEVLSIPDDKEAIVQAgimkMKVPLSDLEKIQKPKKKKKKKPKT 695
|
250 260 270
....*....|....*....|....*....|...
gi 45382679 1319 ELDNVSSL----------LEEAEKKGIKFAKDA 1341
Cdd:PRK00409 696 VKPKPRTVsleldlrgmrYEEALERLDKYLDDA 728
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N-terminus of SMC proteins. The ... |
995-1413 |
3.90e-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: 48.81 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 995 GARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKaknlaKLKNKQEMMITDLEERL 1074
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK-----EQREKEELKKLKLEAEE 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1075 KKEEKTRQELEKAKRKLDgettDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKviRELQAQIAEL 1154
Cdd:pfam02463 722 LLADRVQEAQDKINEELK----LLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK--LKVEEEKEEK 795
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1155 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEvaELKKAIEEETKNHEAQIQEIRQRHAT 1234
Cdd:pfam02463 796 LKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK--LEKLAEEELERLEEEITKEELLQELL 873
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1235 ALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKAN 1314
Cdd:pfam02463 874 LKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEEN 953
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1315 KLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLE 1394
Cdd:pfam02463 954 NKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGW 1033
|
410
....*....|....*....
gi 45382679 1395 KQMLALQAQLAEAKKKVDD 1413
Cdd:pfam02463 1034 NKVFFYLELGGSAELRLED 1052
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1155-1509 |
4.72e-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: 48.58 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1155 QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKkaiEEETKNheaQIQEIRQrhat 1234
Cdd:pfam17380 298 QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR---QEERKR---ELERIRQ---- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1235 alEELSEQLEQAKRfkanLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELtakvtegERLRVElAEKAN 1314
Cdd:pfam17380 368 --EEIAMEISRMRE----LERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEM-------EQIRAE-QEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1315 KLQneldnVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNL--SSRIRQLEEEKNnlqeqqeeeeeaRKN 1392
Cdd:pfam17380 434 QRE-----VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELekEKRDRKRAEEQR------------RKI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1393 LEKQMLALQAQLAEakkkvdddlgtieglEENKKKLL-KDMESlsqrlEEKAMAydklEKTKNRLQQELDDLMVDLDHQR 1471
Cdd:pfam17380 497 LEKELEERKQAMIE---------------EERKRKLLeKEMEE-----RQKAIY----EEERRREAEEERRKQQEMEERR 552
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 45382679 1472 QIVSNLEK---KQKKFDQMLAEEKNISARYAEERDRAEAEA 1509
Cdd:pfam17380 553 RIQEQMRKateERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
970-1178 |
4.72e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 48.18 E-value: 4.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 970 QILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEE 1049
Cdd:COG4942 34 AADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNARLNALEVQEREQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1050 EEK-AKNLA-----------KLKNKQE-------------MMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1104
Cdd:COG4942 114 RRRlAEQLAalqrsgrnpppALLVSPEdaqrsvrlaiyygALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLSE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1105 LQAQIEELKIQLA---KKEEELQAALARGD----EEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSE 1177
Cdd:COG4942 194 QRAQQAKLAQLLEerkKTLAQLNSELSADQkkleELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRTG 273
|
.
gi 45382679 1178 E 1178
Cdd:COG4942 274 E 274
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1067-1358 |
5.48e-05 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 47.82 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1067 ITDLEERLKKEEKTRQE-LEKAKRKLDGEttdLQDQIAELQAQiEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIr 1145
Cdd:COG3206 140 LDDLLESLKVLRAGRSRvIELSYTSNDPK---LAAKLANALAQ-AYLADQLEAQLEAFRRASDSLDERLEELRARLQEA- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1146 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldTTAAQQELRTKREQEVAELKKAIEEETKNHEAqI 1225
Cdd:COG3206 215 EAQVEDFRAQHGLTDAARGQLLSEQQLSALNTQLQSARAR------LAQAEARLASLLQLLPLGREAAALREVLESPT-I 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1226 QEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEHKRKKLDAQVQELTAKVtegERL 1305
Cdd:COG3206 288 QDLRQQYAQVRQQIADLSTELGAKHPQLVALEAQLAELRQQIAAE---LRQILASLPNELALLEQQEAALEKEL---AQL 361
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1306 RVELAeKANKLQNELDNVSSLLEEAEkkgikfakdaASLESQLQDTQELLQEE 1358
Cdd:COG3206 362 KGRLS-KLPKLQVQLRELEREAEAAR----------SLYETLLQRYQELSIQE 403
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA ... |
1030-1413 |
5.68e-05 |
|
AAA domain; This family of domains contain a P-loop motif that is characteristic 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: 433006 [Multi-domain] Cd Length: 712 Bit Score: 48.13 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1030 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE------EKTRQELEKAKRKLDGETTDLQDQIA 1103
Cdd:pfam13166 89 EESIEIQAKIAKLKKEIDDHEEKLEALTANLQKADKEKEKLEADFLDEcwkkikRKKDSALSEALNGFRYEANFKSRLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1104 ELQAQIEELKIQLAkkEEELQAALARGDEEAVQKnnaLKVIRELQAQI--AELQEDLESEKASRNK--AEKQKR-DLSEE 1178
Cdd:pfam13166 169 EIEKDNFNAGVLLT--DEDLKAALETVFGDNKPE---IAPLSFDVIDFdaLEKAEILKQKVIGKSSaiAELIKNpDLADW 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1179 LEALKTELEDTLDTTA-AQQELRTKReqeVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLeqakrfkanleknK 1257
Cdd:pfam13166 244 VEEGLELHKAHLDTCPfCGQPLPAER---KAALEAHFDDEFTEFQRRLQKLIEKYESAISSLLAQL-------------P 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1258 QGLESDNKELACEVKVlQQVKAESEHKRKKLDAQVQELTAKVTEGERlRVELAEKANKLQNELDNVSSLLEEAEK---KG 1334
Cdd:pfam13166 308 AVSDLASLLSAFELDV-EDLKAEAEVLNSQLDGLRQALEAKRKEPFK-SIELDSVDAKIESIKDLVAAINELIAKhneIT 385
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1335 IKFAKDAASLESQLQdtQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1413
Cdd:pfam13166 386 DNLEEEKNKAKKKLW--LFLVEEFKAEIDEYKDAYAGLEKAINSLTKEIKNATAEIKKLRAEIRELEKQLRDHKPGADE 462
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1663-1943 |
5.69e-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: 5.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1663 QIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKGLEAEILQLQEEfaasERARRHAE 1738
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1739 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnERFRKTTLQVDTLnSELAGERSAAQKSENAR 1818
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEM-EQIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1819 QQLERQNKELKAKLQELEgsvKSKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRT-EKKLKEVFMQ-VEDERRHA 1896
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 45382679 1897 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1943
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1017-1167 |
5.83e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1017 EILLLEDQNSKFLkekklmEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLkkeektrQELEKAKRKLDGETT 1096
Cdd:PRK09039 67 DLLSLERQGNQDL------QDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRA-------GELAQELDSEKQVSA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1097 DLQDQIAELQAQIEELKIQLAKKEEELQAALARGdeeavqknnalkviRELQAQIAELQEDLESEKASRNK 1167
Cdd:PRK09039 134 RALAQVELLNQQIAALRRQLAALEAALDASEKRD--------------RESQAKIADLGRRLNVALAQRVQ 190
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
874-1247 |
5.89e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 874 PLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 952
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 953 EILHDLESrvEEEEERNQILQnekkkmqghiqdleeqldeeegARQKLQLekvtaeakIKKMEEEILLLEDQNskflkek 1032
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1033 klMEDRIAECTSQLAEEEEKA-------KNLAKLKNKQEMMITDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1099
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1100 ----DQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvqknnalkviRELQAQIAELQEDLESEKASRNKAEKQKRDL 1175
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQL----------RQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1176 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKAIEEETKNHEAQiqeirQRHATALEE----LSEQLEQ 1245
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 45382679 1246 AK 1247
Cdd:PRK04863 1114 AK 1115
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
876-1123 |
5.98e-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: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 876 LQVTRQEEelqaKDEELMKVKEKQTKVEAE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 954
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 955 LHDLESrveEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLkEKKL 1034
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1035 MEDRIAectsqLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKldgettDLQDQIaeLQAQIEELKI 1114
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR------RIQEQM--RKATEERSRL 568
|
....*....
gi 45382679 1115 QLAKKEEEL 1123
Cdd:pfam17380 569 EAMEREREM 577
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
877-1231 |
6.53e-05 |
|
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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 47.80 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETEL---FAEAEEMRARLAAKKQELEE 953
Cdd:pfam05557 119 QIQRQELELSSTNSELEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEAEQRIKELefeIQSQEQDSEIVKNSKSELAR 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 954 IlHDLESRVEEEEERNqilqnekKKMQGHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK 1032
Cdd:pfam05557 199 I-PELERELERLREHN-------KHLNENIENKLLLKEEVEDLKRKLeREEGYREELATLELEKEKLEQELKSWEKLAQD 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1033 KLMEDRIAECTSQLAEEEEKAKNLAKLKNkqemmiTDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEEL 1112
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQLQQREITLKEEN------SSLTSSARQLEKAQRELEQELAQYLKNIEDLNKKLKRHKALVRRL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1113 --KIQLAKKEEE-LQAALARGDEEAVQKN---NALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1186
Cdd:pfam05557 345 qrRVLLLTKERDgMRAILESYDKELTPSNyspQLLERIEEAEDMTQDMQAHNEEMEAQLSVAEEELGGYKQQATTLEREL 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 45382679 1187 EdtLDTTAAQQELRTKREQEVAELKKAIEEetknHEAQIQEIRQR 1231
Cdd:pfam05557 425 Q--ALRQQESLADPSYSKEEVDSLRRKLET----LEAERQRLREQ 463
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
873-1276 |
6.56e-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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 47.57 E-value: 6.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 873 KPLLQVTRQEEELQAKD--EELMKVKEKQTKVEAELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 950
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 951 LEEILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLK 1030
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKVEELEEKYKELSRSGEELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1031 EKKLMEDRIAECTSQLAEEEEKAKNLaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIE 1110
Cdd:pfam07888 151 ELERMKERVKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1111 ELKIQLAKKeEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESE-KASRNKAEKQKRDLSEELEALK------ 1183
Cdd:pfam07888 224 TAHRKEAEN-EALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAElHQARLQAAQLTLQLADASLALRegrarw 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1184 -TELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANL---EKNKQG 1259
Cdd:pfam07888 303 aQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKEKEQ 382
|
410
....*....|....*..
gi 45382679 1260 LESDNKELACEVKVLQQ 1276
Cdd:pfam07888 383 LQAEKQELLEYIRQLEQ 399
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1560-1874 |
6.74e-05 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 47.44 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRtQLEELEDELQATEDAKLRLEVNMQAMK-AQFERDLQARDeQNEEKKRMLVKQVRELEAELED 1638
Cdd:COG3206 87 EILQSRSVLEKVIDKLK-LDDDPEFVGKPLIASFLRLLKDLIGPDpTIFEISYRLDD-LLESLKVLRAGRSRVIELSYTS 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1639 ERKQRAlAVAAKKKMEMDLKD-LEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEkklkgLE 1717
Cdd:COG3206 165 NDPKLA-AKLANALAQAYLADqLEAQLEAFRRASDSLDERLEELRARLQEAEAQVEDFRAQHGLTDAARGQLL-----SE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1718 AEILQLQEEFAASERARRHAEQERDELADEIANSasgkSALLDEKRRLEARIAQLeeeleeeqsnmelLNERFRKTTLQV 1797
Cdd:COG3206 239 QQLSALNTQLQSARARLAQAEARLASLLQLLPLG----REAAALREVLESPTIQD-------------LRQQYAQVRQQI 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1798 DTLNSELAGERSAAQKSENARQQLERQnkeLKAKLQELEGSVKSKFKAtistLEAKIAQLEEQLEQEAKERAAANKL 1874
Cdd:COG3206 302 ADLSTELGAKHPQLVALEAQLAELRQQ---IAAELRQILASLPNELAL----LEQQEAALEKELAQLKGRLSKLPKL 371
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1581-1858 |
7.22e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1581 ELEDELQATEDAKLRLEvnmqAMKAQFERDLQARDEQNEEKKRmlvkqvrELEAELEDERKQRALAVAAKKKMEMDLKDL 1660
Cdd:PRK05035 440 AIEQEKKKAEEAKARFE----ARQARLEREKAAREARHKKAAE-------ARAAKDKDAVAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1661 EGQIEAANKARdEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEF-----AASERARR 1735
Cdd:PRK05035 509 KAGARPDNSAV-IAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEvdpkkAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1736 HAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMEllnerfrkTTLQVDTLNSELAGERSAAQKSE 1815
Cdd:PRK05035 588 RAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAE--------PEEPVDPRKAAVAAAIARAKARK 659
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 45382679 1816 NARQQLErqnkelkAKLQELEGSVKSKFKATISTLEAKIAQLE 1858
Cdd:PRK05035 660 AAQQQAN-------AEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
882-1379 |
7.26e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEKQTKVEA-------ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 954
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKshsitlkEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 955 LHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEeillLEDQNSKFLKE 1031
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1032 KKLMEDRIAECT----------SQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELKIQLAKKEEELQAALARG----------------------------DEEAVQKNNALKVIRELQAQIAE 1153
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgeeksnhiinhynekksrlEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1154 LQEDLESEKASRNKAEKQKrdlseeLEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-IEEETKNHEAQIQEIRQRH 1232
Cdd:PRK01156 505 RKEYLESEEINKSINEYNK------IESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVIS 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1233 ATALEELSEQLEQAKRFKANLEKNKQGLESDnkelacevkvLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEK 1312
Cdd:PRK01156 579 LIDIETNRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKL 648
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1313 ANKLQN------ELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNL 1379
Cdd:PRK01156 649 RGKIDNykkqiaEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDI 721
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1198-1994 |
7.33e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 7.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1198 ELRTKREQEVAELKKAIEEEtknheaqiqeiRQRHatalEELSEQLEQAKRFKANLEknkQGLESDNKELACEVKVLQQV 1277
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAE-----------QYRL----VEMARELAELNEAESDLE---QDYQAASDHLNLVQTALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1278 KAEsehkrKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELdnvssllEEAEKkgikfakDAASLESQLQDTQELLQE 1357
Cdd:PRK04863 348 EKI-----ERYQADLEELEERLEEQNEVVEEADEQQEENEARA-------EAAEE-------EVDELKSQLADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1358 -ETR-----QKLNLSSRIRQL-----------EEEKNNLQEQQEEEEEARKNLEKQMLALQA---QLAEAKKKVDDDLGT 1417
Cdd:PRK04863 409 qQTRaiqyqQAVQALERAKQLcglpdltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKIAGE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1418 IEGLE--ENKKKLLKDMES---LSQRLEEkamaydklektknrLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEk 1492
Cdd:PRK04863 489 VSRSEawDVARELLRRLREqrhLAEQLQQ--------------LRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDE- 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1493 nisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsSKDDVGKNVHEL-----EKSKRT 1567
Cdd:PRK04863 554 ----------DELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA-ARAPAWLAAQDAlarlrEQSGEE 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1568 LE--QQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQVR-ELEAELEDE----- 1639
Cdd:PRK04863 623 FEdsQDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLNALAERFGgVLLSEIYDDvsled 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 ---------RKQRALAV----AAKKKME------MDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDyqRELEEARASRD 1700
Cdd:PRK04863 699 apyfsalygPARHAIVVpdlsDAAEQLAgledcpEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIAD--RQWRYSRFPEV 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1701 EIFAQsKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSAS---------GKSALLDEKRRLEARIAQ 1771
Cdd:PRK04863 777 PLFGR-AAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAvafeadpeaELRQLNRRRVELERALAD 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1772 LEEELEEEQSNMELLNERF--------RKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELkAKLQELEGSVKSKf 1843
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLsalnrllpRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNAL-AQLEPIVSVLQSD- 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1844 KATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTE------------------KKLKEVFMQVEDERrhaDQYKEQMEK 1905
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaaemlaknsdlnEKLRQRLEQAEQER---TRAREQLRQ 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1906 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDAT-----EANEGLSREVSTLKNRLRRggpitfssSRSGRRQLHIE 1980
Cdd:PRK04863 1011 AQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsGAEERARARRDELHARLSA--------NRSRRNQLEKQ 1082
|
890
....*....|....
gi 45382679 1981 GASLELSDDDAESK 1994
Cdd:PRK04863 1083 LTFCEAEMDNLTKK 1096
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
1264-1869 |
8.43e-05 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 47.92 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1264 NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRvELAEKANKLQNELDNVSSLLEeaekkgikfakdaas 1343
Cdd:COG4717 180 NPQINQLLEKLKQERNEIDEAEKEYATYHKLLESRRAEHARLA-ELRSELRADRDHIRALRDAVE--------------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1344 LESQLQDTQELLQEETRQKLNLSS----RIRQLEEEKNNLQEQQEEEEEARKNLEkQMLALQAQLAEAKKKVDDDLgtiE 1419
Cdd:COG4717 244 LWPRLQEWKQLEQELTRRREELATfprdGVLRLEKREAHLQKTEAEIDALLVRLA-ELKDLASQLIPAKEAVLQAL---V 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1420 GLEENKKKLLKDMESLSQRLEE-KAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSnlekKQKKFDQMLAEEKNISARY 1498
Cdd:COG4717 320 RLHQQLSEIKASAFELTETLAGiEADLRDKEEAAGNGFEAERVHDLRSLECMLRYQS----SQRELKQTEAAYCKRLDEK 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1499 AEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQ 1578
Cdd:COG4717 396 RLFEDEAEEEARQRLADDEEEVRAGDEAREEKIAANSQVIDKEEVCNLYDRRDTAWQKQRFLREKQTAFERQKTEHTKII 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1579 LEELEDELQATEDAKLRL---EVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAEL--EDERKQRALAVAAKKKM 1653
Cdd:COG4717 476 ALRLAGMLLVALSRLLTSlifQIIFAVAQIVFLSAEIKSSSRAVREEKAAVTDIPEELARLliTDELPELAVDLLVQSRI 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1654 EMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARA--------SRDEI------FAQSKESEKKLKGLEAE 1719
Cdd:COG4717 556 RQHWQQLRKALDQLEAAYEALEGRFAAAEAAMAEWQSEWEEALDelglsrelSPEQQldilstMKDLKKLMQKKAELTHQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1720 ILQLQEEfaaserarRHAEQERDE-LADEIANSASGKSALLDEKRRL--------EARIAQLEEELEEEQSNMELLNERF 1790
Cdd:COG4717 636 VARLREE--------QAAFEERVEgLLAVLEAQFIDLSTLFCVQRLRvaaelqkeEARLALEGNIERTKELNDELRAELE 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1791 RKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLEQEAKERA 1869
Cdd:COG4717 708 LHRKEILDLFDCGTADTEDAFREAAREEQQLTQRESRLESLEAQLEGVAAEAYELSASLDQRELKEEELALLEEAIDAL 786
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1059-1490 |
9.06e-05 |
|
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.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1059 LKNKQEMMITDLEERlKKEEKTR---QELEKAKR-KLDGETtdlQDQIAELQAQIEELK-IQLAKKEEELQAAlargdEE 1133
Cdd:pfam06160 4 LRKKIYKEIDELEER-KNELMNLpvqEELSKVKKlNLTGET---QEKFEEWRKKWDDIVtKSLPDIEELLFEA-----EE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1134 AVQKNN---ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDtldttaAQQELRTKREQeVAEL 1210
Cdd:pfam06160 75 LNDKYRfkkAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRE------LRKTLLANRFS-YGPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1211 KKAIEEETKNHEAQIQEirqrhataLEELSEQ--LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVkaesehkrkkL 1288
Cdd:pfam06160 148 IDELEKQLAEIEEEFSQ--------FEELTESgdYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE----------L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1289 DAQVQELTAKVTEGER-----LRVELAEKANKLQNELDNVSSLLEEAEKKgiKFAKDAASLESQLQDTQELLQEETRQKL 1363
Cdd:pfam06160 210 PDQLEELKEGYREMEEegyalEHLNVDKEIQQLEEQLEENLALLENLELD--EAEEALEEIEERIDQLYDLLEKEVDAKK 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1364 NLSSRIRQLEEEKNNLqeqqeeeeearknlEKQMLALQAQLAEAKKK---VDDDLGTIEGLEENKKKLLKDMESLSQRLE 1440
Cdd:pfam06160 288 YVEKNLPEIEDYLEHA--------------EEQNKELKEELERVQQSytlNENELERVRGLEKQLEELEKRYDEIVERLE 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 45382679 1441 EKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAE 1490
Cdd:pfam06160 354 EKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDE 403
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1031-1233 |
9.27e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.62 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1031 EKKLMEDRIaectsQLAEEEEKAKNLAklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQ------DQIAE 1104
Cdd:PLN03188 1046 EKKLEQERL-----RWTEAESKWISLA------EELRTELDASRALAEKQKHELDTEKRCAEELKEAMQmameghARMLE 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1105 LQAQIEELKIQLAKKEEELQAAL---ARGDEEAVQKNNALKVIRELQAQIAELqedleseKASRnkaEKQKRDLSEELEA 1181
Cdd:PLN03188 1115 QYADLEEKHIQLLARHRRIQEGIddvKKAAARAGVRGAESKFINALAAEISAL-------KVER---EKERRYLRDENKS 1184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1182 LKTELEDTLDTTAAQQELRT-------------KR----EQEVAELKKAIEEETKNHEAQIQEIRQRHA 1233
Cdd:PLN03188 1185 LQAQLRDTAEAVQAAGELLVrlkeaeealtvaqKRamdaEQEAAEAYKQIDKLKRKHENEISTLNQLVA 1253
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
1074-1478 |
1.00e-04 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 47.28 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1074 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAalargdeeavqknnalkvIRELQAQIAE 1153
Cdd:COG5185 245 LKLEDNYEPSEQELKLGFEKFVHIINTDIANLKTQNDNLYEKIQEAMKISQK------------------IKTLREKWRA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1154 LQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaQQELRTKREQEvAELKKAIEEETKNHEaQIQEIRQRHa 1233
Cdd:COG5185 307 LKSDSNKYENYVNAMKQKSQEWPGKLEKLKSEIELK------EEEIKALQSNI-DELHKQLRKQGISTE-QFELMNQER- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1234 talEELSEQLEQAKRFKANLEKNKQGLESDNKELACEV-KVLQQVKAESEHKRKKLDAQVQ-----ELTAKVTEGERLRV 1307
Cdd:COG5185 378 ---EKLTRELDKINIQSDKLTKSVKSRKLEAQGIFKSLeKTLRQYDSLIQNITRSRSQIGHnvndsSLKINIEQLFPKGS 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1308 ELAEKANKLQNEL-DNVSSLLEEAEKKGIKFAKDAASLESqlqDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEE 1386
Cdd:COG5185 455 GINESIKKSILELnDEIQERIKTEENKSITLEEDIKNLKH---DINELTQILEKLELELSEANSKFELSKEENERELVAQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1387 EEARKNLEKQMLALQAQLAEAKKKVDDDLGTIE-GLEENKKKLLKDMESLSQrleEKAMAYDKLEKTKNRLQQELDDLMV 1465
Cdd:COG5185 532 RIEIEKLEKELNDLNLLSKTSILDAEQLVQSTEiKLDELKVDLNRKRYKIHK---QVIHVIDITSKFKINIQSSLEDLEN 608
|
410
....*....|...
gi 45382679 1466 DLDHQRQIVSNLE 1478
Cdd:COG5185 609 ELGKVIEELRNLE 621
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
1096-1267 |
1.05e-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: 430106 [Multi-domain] Cd Length: 176 Bit Score: 44.92 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1096 TDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKnnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDL 1175
Cdd:pfam08614 10 NRLADRTALLEAENAALQSEPESVPPSTSSSTASASPVQSAS------IQSLEQLLAQLREELAELYRSRGELAQQLVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1176 SEELEALKTELEdtldttAAQQELRtKREQEVAELkkaiEEETKNHEAQIQEIRQRHATALEE---LSEQLEQAkrfkan 1252
Cdd:pfam08614 84 NEELQELEKKLR------EDERRLA-ELEAERAQL----EEKLRDREEELREKRKLNQDLQDElvaLQLQLNMA------ 146
|
170
....*....|....*
gi 45382679 1253 lEKNKQGLESDNKEL 1267
Cdd:pfam08614 147 -EEKLRKLEKENREL 160
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown]; |
1052-1247 |
1.16e-04 |
|
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 226400 [Multi-domain] Cd Length: 265 Bit Score: 45.86 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1052 KAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLA------KKEEELQA 1125
Cdd:COG3883 25 FAALLSDKIQNQDSKLSELQKEKKNIQNEIESLDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAelkeniVERQELLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1126 ALARGDE-------------------EAVQKNNALKVIRELQAQIAELQEDlesEKASRNKAEKQKRDLSEELEALKTEL 1186
Cdd:COG3883 105 KRARAMQvngtatsyidvilnsksfsDLISRVTAISVIVDADKKILEQQKE---DKKSLEEKQAALEDKLETLVALQNEL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1187 EDTLDTTAAQQELRTK-------REQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAK 1247
Cdd:COG3883 182 ETQLNSLNSQKAEKNAliaalaaKEASALGEKAALEEQKALAEAAAAEAAKQEAAAKAAAQEQAALQA 249
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
1079-1441 |
1.17e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 434900 [Multi-domain] Cd Length: 384 Bit Score: 46.60 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1079 KTRQELEKAKRKLDGET---TDLQDQIAELQAQIEELKIQLAKKEEELQaalargdeeavqknnalkvirelqaQIAELQ 1155
Cdd:pfam15742 59 KIKAELKQAQQKLLDSTkmcSSLTAEWEHCQQKIRELELEVLKQAQSIK-------------------------SQNSLQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1156 EDLESEKASRNKAEKQKRDLSEELE-ALKTELEDTLDTTAAQQELRTKREQEvaelkkaIEEETKNHEAQIQEIRQRHAT 1234
Cdd:pfam15742 114 EKLAQEKSKVADAEKKILELQQKLEhAHKVCLTETCILEKKQLEEEIKEAQE-------NEAKLKQQYQEEQQKRKLLDQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1235 ALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKAN 1314
Cdd:pfam15742 187 NVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKSNQELSEKLSSLQQEKEALQEELQQVLK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1315 KLQNELDNVSslleeaEKKGIKFAKdaaslesqLQDTQELLQEETRQKlnlSSRIRQLEEEKNNLQEQQEEEeearKNLE 1394
Cdd:pfam15742 267 QLDVHVRKYN------EKHHHHKAK--------LRRAKDRLVHEVEQR---DERIKQLENEIRILRQQIEKE----KAFQ 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 45382679 1395 KQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEE 1441
Cdd:pfam15742 326 KQVTAENDTLLLEKRKLLEQLTEQEEVIKNNKRTISSVQNRVLFLEK 372
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1560-1771 |
1.26e-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: 46.38 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamKAQferdlQARDEQNEEKKrmlvkQVRELEAELEDE 1639
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK----------QAE-----QAAKQAEEKQK-----QAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 RKQRALAVAAKKKMEmdlkdlegqiEAANKARDEAIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKGLEAE 1719
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1720 ILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
875-1322 |
1.47e-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: 47.14 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 875 LLQVTRQEEELQAKDEELMKVKEKQTKVEAEL-----------EEMERKHQQLLEEKNILAEqlqAETELFAEAEEMRAR 943
Cdd:pfam12128 463 LLQLENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasEALRQASRRLEERQSALDE---LELQLFPQAGTLLHF 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 944 LAAKKQELE---------EILH--DLESRVEEEEERNQI------LQNEKKKMQGHIQDLEEQLDEEEGARQKLQlekvT 1006
Cdd:pfam12128 540 LRKEAPDWEqsigkvispELLHrtDLDPEVWDGSVGGELnlygvkLDLKRIDVPEWAASEEELRERLDKAEEALQ----S 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1007 AEAKIKKMEEEILLLedqNSKFLKEKKLMEDriAECTSQLAEEEEKAKNLAKlKNKQEMMITDLEERLKKEEKTRQELEK 1086
Cdd:pfam12128 616 AREKQAAAEEQLVQA---NGELEKASREETF--ARTALKNARLDLRRLFDEK-QSEKDKKNKALAERKDSANERLNSLEA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1087 AKRKLDgetTDLQDQIAELQAQIEELKIQLAKK----EEELQAALARGDEEAVQKNNALKvirelqAQIAELQEDLESEK 1162
Cdd:pfam12128 690 QLKQLD---KKHQAWLEEQKEQKREARTEKQAYwqvvEGALDAQLALLKAAIAARRSGAK------AELKALETWYKRDL 760
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1163 ASRNKAEKQKRDLSEELEALKTELEDTldttaaqqelrTKREQEVAELKKAIEE----ETKNHEAQIQEIRQRHATALEE 1238
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKIERI-----------AVRRQEVLRYFDWYQEtwlqRRPRLATQLSNIERAISELQQQ 829
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1239 LSEQLEQAKRFKANLEKNKQGLESDNKELACEvkvLQQVKAESEH-KRKKLDAQVQELTAKVTE----GERLRVELAEKA 1313
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQVRLSEN---LRGLRCEMSKlATLKEDANSEQAQGSIGErlaqLEDLKLKRDYLS 906
|
....*....
gi 45382679 1314 NKLQNELDN 1322
Cdd:pfam12128 907 ESVKKYVEH 915
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1371-1917 |
1.57e-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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 46.65 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1371 QLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEenkKKLLKDMESLSQRLEEkAMAYDKLE 1450
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELERKASALARQLERESDRNQELQKRIRLLE---KREAEAEEALREQAEL-NRLKKKNL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1451 KTKNRLQQELDDLMVDLdhqRQIVSNLekkqkkfdqmlaeeKNISARYAEERDRAEAEAREKETKalslaraleealeak 1530
Cdd:pfam05557 86 EALNKKLNEKESQLADA---REVISCL--------------KNELSELRRQIQRQELELSSTNSE--------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1531 eeferqnkqlradMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRT---QLEELEDELQATEDAKLRLEvNMQAMKAQF 1607
Cdd:pfam05557 134 -------------LEELQERLDLQKAKAQEAEQLRQNLEAQQSSLAEaeqRIKELEFEIQSQEQDSEIVK-NSKSELARI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1608 ---ERDLQARDEQNE------EKKRMLVKQVRELEAELEDERKQRALAVA---AKKKMEMDLKDLEG------------- 1662
Cdd:pfam05557 200 pelERELERLREHNKhlneniENKLLLKEEVEDLKRKLEREEGYREELATlelEKEKLEQELKSWEKlaqdtglnlrspe 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1663 ----------QIEAANKARDEAI-KQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKGLEAEILQLQEEFAASE 1731
Cdd:pfam05557 280 dlsrrieqlqQREITLKEENSSLtSSARQLEKAQRELEQELAQYLK-------NIEDLNKKLKRHKALVRRLQRRVLLLT 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1732 RARRHAEQERDELADEIANSASGKSaLLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAA 1811
Cdd:pfam05557 353 KERDGMRAILESYDKELTPSNYSPQ-LLERIEEAEDMTQDMQAHNEEMEAQLSVAEEELGGYKQQATTLERELQALRQQE 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1812 QKSENARQQLERQnkELKAKLQELEGSVkSKFKATISTLEAKIAQLEEQLEQEAKeraaanklvrrtekKLKEVFMQVED 1891
Cdd:pfam05557 432 SLADPSYSKEEVD--SLRRKLETLEAER-QRLREQKNELEMELERRCLQGDYDPK--------------KTKVLHLSMNP 494
|
570 580
....*....|....*....|....*.
gi 45382679 1892 ERRHADQYKEQMEKANARMKQLKRQL 1917
Cdd:pfam05557 495 AAEAYQQRANDLEKLQAEIERLKRRL 520
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
908-1365 |
1.59e-04 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 46.51 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 908 EMERKHQQLLEEKNIlaEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEeerNQILQNE---KKKMQGHIQ 984
Cdd:COG5185 210 DMCLQPLKTLDQQDR--YELMVEKLLFDYFTESYKSFLKLEDNYEPSEQELKLGFEKF---VHIINTDianLKTQNDNLY 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 985 DLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQE 1064
Cdd:COG5185 285 EKIQEAMKISQKIKTLREKWRALKSDSNKYENYVNAMKQKSQEWPGKLEKLKSEIELKEEEIKALQSNIDELHKQLRKQG 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1065 MMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGDEEAVQKNNALkvi 1144
Cdd:COG5185 365 ISTEQFELMNQEREKLTRELDKINIQSDKLTKSVKSRKLEAQGIFKSLE-KTLRQYDSLIQNITRSRSQIGHNVNDS--- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1145 rELQAQIAELQEDLESEKASRNKAEKQKRDLSEELeaLKTELEDTLdttaaqqelrtKREQEVAELKKAIEEETKnheaQ 1224
Cdd:COG5185 441 -SLKINIEQLFPKGSGINESIKKSILELNDEIQER--IKTEENKSI-----------TLEEDIKNLKHDINELTQ----I 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1225 IQEIRQRHATALEELSEQLEQAKRfkanlEKNKQGLESDNKElacevKVLQQVKAESEHKRKKLDAQVQELTAKVtegER 1304
Cdd:COG5185 503 LEKLELELSEANSKFELSKEENER-----ELVAQRIEIEKLE-----KELNDLNLLSKTSILDAEQLVQSTEIKL---DE 569
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1305 LRVELAEKANKLQNEldnVSSLLEEAekkgIKFakdAASLESQLQDTQELLQEETRQKLNL 1365
Cdd:COG5185 570 LKVDLNRKRYKIHKQ---VIHVIDIT----SKF---KINIQSSLEDLENELGKVIEELRNL 620
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1665-1771 |
1.71e-04 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 45.32 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1665 EAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDEL 1744
Cdd:pfam00769 2 EEAEREKQELEERLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQL 81
|
90 100
....*....|....*....|....*..
gi 45382679 1745 ADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:pfam00769 82 ERELREAQEEVARLEEESERKEEEAER 108
|
|
| COG4913 |
COG4913 |
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown]; |
1067-1766 |
1.75e-04 |
|
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 227250 [Multi-domain] Cd Length: 1104 Bit Score: 46.94 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1067 ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE-LQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIR 1145
Cdd:COG4913 264 LVQLKNRREKAQQSKDHANALKKALPTVGNRIKKEEQEtLVRQFTVEQTQAKSKVESAKIETDRAREMETLAHDNVKQIV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1146 ELQAQI-AELQEDLESEKASRNKAekqkrdlSEELEALKTELEDTLDTTAAQ-QELRTKREQEVAELKKAIE----EETK 1219
Cdd:COG4913 344 GAQHGIlSAKREGAVDKRRTISTA-------RAGLDALVKGLGGAAPESAEElLELNNAARLTVDEYPAAREalesAGQR 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1220 NHEAqIQEIRQRHATALEELSEQLEQAKRFKANLEKNK----QGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQeL 1295
Cdd:COG4913 417 NVED-RTRAVDEFKAADQELSSLSKGSSNIEYRLLQVRenlcQDLGVSPRDMPFAGELIDPNNAEWEPVVQRILGGFA-A 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1296 TAKVTEGERLRVELAEKANKLQNELdNVSSLLEEAEKKGIKFAKDAASLESQLQDT--QELLQEETRQKLNLS--SRIRQ 1371
Cdd:COG4913 495 EMLVPHGLLPRVRDWVNAKHLAALL-KFNGVVTTGEYKTSRFPADSLIRKVDVVESpfRDWVNQELGKRFNIRcvRTPEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1372 LEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDDDlgTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEK 1451
Cdd:COG4913 574 LSALGPGVTILGQTGDPTTRWEKDDRRKLGDRSTYRLGSTNDA--KVETLRETVKAMLSREDFYMIKIMRQQGEYIKLQE 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1452 TKNRLQ--QELDDLMVDLDH-QRQIvsnlEKKQKKFDQmLAEEKNISARYAEERDRAEAEAREKETKALSLARALEEALE 1528
Cdd:COG4913 652 QANALAhiQALNFASIDLPSaQRQI----AELQARLER-LTHTQSDIAIAKAALDAAQTRQKVLERQYQQEVTECAGLKK 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1529 AKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQL-EELEDELQATEDAKLRLEVNM-QAMKAQ 1606
Cdd:COG4913 727 DLKRAAMLSRKVHSIAKQGMTGALQALGAAHFPQVAPEQHDDIVDIERIEHrRQLQKRIDAVNARLRRLREEIiGRMSDA 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1607 FERDLQARDEQNEEkkrmlVKQVRELEAELEDERKQRALAVAAKKKMEMdlkdlegqieaaNKARDEAIKQlrkLQAQMK 1686
Cdd:COG4913 807 KKEDTAALSEVGAE-----LDDIPEYLARLQTLTEDALPEFLARFQELL------------NRSSDDGVTQ---LLSHLD 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1687 DYQRELEEARASRDEIFAQSKESE--------KKLKGLEAEILQLQEEFAASERAR------------RHAEQER--DEL 1744
Cdd:COG4913 867 HERALIEERIEAINDSLRRVDFNSgrylhidiAKQPVPHDSMRTFQQALRALTSGRfvgddgesqykaLQALVGLiiDAC 946
|
730 740
....*....|....*....|..
gi 45382679 1745 ADEIANSASGKSALLDEKRRLE 1766
Cdd:COG4913 947 ERHDSADTRWARAVLDPRFRLE 968
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1000-1209 |
1.92e-04 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 46.28 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1000 LQLEKVTAEAKIKKMEEEILLLEDQNSKFLkEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEK 1079
Cdd:COG3206 207 LRARLQEAEAQVEDFRAQHGLTDAARGQLL-SEQQLSALNTQLQSARARLAQAEARLASLLQLLPLGREAAALREVLESP 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1080 TRQELEKAKrkldgetTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQ----KNNALKVIRELQAQIAELQ 1155
Cdd:COG3206 286 TIQDLRQQY-------AQVRQQIADLSTELGAKHPQLVALEAQLAELRQQIAAELRQilasLPNELALLEQQEAALEKEL 358
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1156 EDLESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEVAE 1209
Cdd:COG3206 359 AQLKGRLSKLPKLQVQLRELEREAEAARSLYETLL---QRYQELSIQEASPIGN 409
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1560-1961 |
2.10e-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: 46.50 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQARDEQNEEKKRMLVKQVRELEAELEDE 1639
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAH---IKAVTQIEQQAQRIHTELQSKMRSRAKL 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQlrklqaqmkdyqreleearASRDEIFAQSKESEKKLKGLEA- 1718
Cdd:TIGR00618 327 LMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVA-------------------TSIREISCQQHTLTQHIHTLQQq 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1719 -EILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQv 1797
Cdd:TIGR00618 388 kTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQ- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1798 dtlnsELAGERSAAQKSENARQQLERQNKELKAKLQELEGSvKSKFKATISTLEAKIAQLEEqLEQEAKERAAANKLVRR 1877
Cdd:TIGR00618 467 -----SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEE-PCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1878 TEKKLKEVFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeeeATRANASRRKLQRELDDATEANEGLSREVSTLKN 1957
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
....
gi 45382679 1958 RLRR 1961
Cdd:TIGR00618 613 EQHA 616
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
825-1413 |
2.33e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 825 QAVCRGYLARKAFAKKQQQLSALKILQRncAAYLKLrhwQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEA 904
Cdd:PRK10246 261 RRQQALQQALAAEEKAQPQLAALSLAQP--ARQLRP---HWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 905 eleemeRKHQQLLEEKNILAEQLQAETE-------------LFAEAEEMRARLAAKKQELEEILHDLES----------- 960
Cdd:PRK10246 336 ------KQSAELQAQQQSLNTWLAEHDRfrqwnnelagwraQFSQQTSDREQLRQWQQQLTHAEQKLNAlpaitltltad 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 961 ---RVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEillLEDQNSKFLKEKKL--M 1035
Cdd:PRK10246 410 evaAALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQR---YKEKTQQLADVKTIceQ 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1036 EDRIAECTSQLAeeeekaknlaKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQIEEL 1112
Cdd:PRK10246 487 EARIKDLEAQRA----------QLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDAlekEVKKLGEEGAALRGQLDAL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1113 KIQLAKKEEELQAALArgDEEAVQKN-----NALKVIRELQAQIA---------ELQEDLESEK----ASRNKAEKQKRD 1174
Cdd:PRK10246 557 TKQLQRDESEAQSLRQ--EEQALTQQwqavcASLNITLQPQDDIQpwldaqeehERQLRLLSQRhelqGQIAAHNQQIIQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1175 LSEELEALKTELEDTLDTTA-------AQQELRTKREQEVAELKKaieeetknHEAQIQEIRQRHAtALEELSEQLEQAK 1247
Cdd:PRK10246 635 YQQQIEQRQQQLLTALAGYAltlpqedEEASWLATRQQEAQSWQQ--------RQNELTALQNRIQ-QLTPLLETLPQSD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1248 RFKANLE----KNKQGLESDNKELACEVKVLQQvkAESEHKRKKLDAQVQ---ELTAKVTEG----------ERLRVELA 1310
Cdd:PRK10246 706 DLPHSEEtvalDNWRQVHEQCLSLHSQLQTLQQ--QDVLEAQRLQKAQAQfdtALQASVFDDqqaflaalldEETLTQLE 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1311 EKANKLQNELDNVSSLLEEAEK----------KGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKnnlq 1380
Cdd:PRK10246 784 QLKQNLENQRQQAQTLVTQTAQalaqhqqhrpDGLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNR---- 859
|
650 660 670
....*....|....*....|....*....|...
gi 45382679 1381 eqqeeeeearknleKQMLALQAQLAEAKKKVDD 1413
Cdd:PRK10246 860 --------------QQQQALMQQIAQATQQVED 878
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1560-1698 |
2.48e-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: 45.44 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQ-NEEKKRMLVKQVRELEAELED 1638
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1639 ERKqrALAVAAKKKMEmDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARAS 1698
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1011-1333 |
2.59e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 46.05 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1011 IKKMEEEILLLE-------DQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMiTDLEERLKKEEKTRQE 1083
Cdd:PLN02939 137 IQNAEKNILLLNqarlqalEDLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEIL-EEQLEKLRNELLIRGA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKA-KRKLDGETTDLQDQIAELQAQIEELKIQLA--KKEEELQAALARgdEEAVQKNNalkvIRELQAQIAELQEDLes 1160
Cdd:PLN02939 216 TEGLcVHSLSKELDVLKEENMLLKDDIQFLKAELIevAETEERVFKLEK--ERSLLDAS----LRELESKFIVAQEDV-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1161 EKASRNKAEKqkrdLSEELEalktELEDTLDTTAAQQelrtkrEQEVAELKkaieeetknheaQIQEIRQRhataLEELS 1240
Cdd:PLN02939 288 SKLSPLQYDC----WWEKVE----NLQDLLDRATNQV------EKAALVLD------------QNQDLRDK----VDKLE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1241 EQLEQAKRFKANLEKnkqglesdnkelaceVKVLQQ-VKAESEHkrkkLDAQVQELTAKVTEGERLRVELAekanklqne 1319
Cdd:PLN02939 338 ASLKEANVSKFSSYK---------------VELLQQkLKLLEER----LQASDHEIHSYIQLYQESIKEFQ--------- 389
|
330
....*....|....
gi 45382679 1320 lDNVSSLLEEAEKK 1333
Cdd:PLN02939 390 -DTLSKLKEESKKR 402
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
882-1216 |
2.82e-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.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.62 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLleEKNILA-------------EQLQAETELFAEAEEMRAR---LA 945
Cdd:pfam06160 99 EEDIKQILEELDELLESEEKNREEVEELKDKYREL--RKTLLAnrfsygpaideleKQLAEIEEEFSQFEELTESgdyLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 946 AKK--QELEEILHDLESRVEEEEERNQILQNEKKKmqghiqdleeqldeeegarqklQLEKVtaEAKIKKMEEEILLLED 1023
Cdd:pfam06160 177 AREvlEKLEEETDALEELMEDIPPLYEELKTELPD----------------------QLEEL--KEGYREMEEEGYALEH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1024 QNskFLKEKKLMEDRIAECTSQLA--EEEEKAKNLAKLKNKqemmITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:pfam06160 233 LN--VDKEIQQLEEQLEENLALLEnlELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELK--IQLAKKEEELQAALArgdeeavqknnalKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL 1179
Cdd:pfam06160 307 NKELKEELERVQqsYTLNENELERVRGLE-------------KQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQL 373
|
330 340 350
....*....|....*....|....*....|....*....
gi 45382679 1180 EALKTELEDTLDTTAA--QQELRTKreQEVAELKKAIEE 1216
Cdd:pfam06160 374 EEIEEEQEEFKESLQSlrKDELEAR--EKLDEFKLELRE 410
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1631-1877 |
2.85e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1631 ELEAELeDERKQRALAVAAKKKMEMDLK---DLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1707
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1708 ES------EKKLKGLEAEILQLQEEFA-----------ASERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1766
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAeynsqlvslqtQPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1767 ARIAQleeeleeeqsnMELLNErFRKTTLQVDTLNSELaGERSAAQKSENArQQLERQnkelkakLQELEGSVKSKfkat 1846
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDL-LQKQRDYLTARI-QRLEHQ-------LQLLQEAINSK---- 253
|
250 260 270
....*....|....*....|....*....|.
gi 45382679 1847 isTLEAKIAQLEEQLEQEAKERAAANKLVRR 1877
Cdd:PRK11281 254 --RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1011-1186 |
2.87e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 44.23 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1011 IKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKnLAKLKNKQEMM------ITDLEERLKKEEKTRQEL 1084
Cdd:COG1842 33 IRDMESELAKARQALAQAIARQKQLERKLEEAQARAEKLEEKAE-LALQAGNEDLArealeeKQSLEDLAKALEAELQQA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1085 EKAKRKLDGETTDLQDQIAELQAQIEELKIQL--AKKEEELQAALARGDEEAVQKnnALKVIRELQAQI---AELQEDLE 1159
Cdd:COG1842 112 EEQVEKLKKQLAALEQKIAELRAKKEALKARKaaAKAQEKVNRSLGGGSSSSAMA--AFERMEEKIEERearAEAAAELA 189
|
170 180 190
....*....|....*....|....*....|.
gi 45382679 1160 SEKAS--RNKAEKQKRD--LSEELEALKTEL 1186
Cdd:COG1842 190 EGSGDdlDKEFAQAGAQsaVDSRLAALKARM 220
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1084-1244 |
2.97e-04 |
|
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: 426264 [Multi-domain] Cd Length: 170 Bit Score: 43.41 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKRKLDGETTDLQDQIAElqaQIEELKIQLAKKEEELQAALARGDEEAVQKNNalKVIRELQAQIAELQEDLEseKA 1163
Cdd:pfam01442 8 AEELQEQLGPVAQELVDRLEK---ETEALRERLQKDLEEVRAKLEPYLEELQAKLQ--QNVEELRQRLEPYTEELR--KR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1164 SRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKAIEEETKNHEAQ----IQEIRQRHAT 1234
Cdd:pfam01442 81 LNADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAEEVQAQlsqrLQELREKLEP 160
|
170
....*....|
gi 45382679 1235 ALEELSEQLE 1244
Cdd:pfam01442 161 QAEDLREKLD 170
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1481-1959 |
3.06e-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: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1481 QKKFDQMLAEEKNISAryaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQnkQLRADMEDLMSSKDDVGKNVHE 1560
Cdd:TIGR00606 172 KQKFDEIFSATRYIKA---LETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD--QITSKEAQLESSREIVKSYENE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1561 LEKSKRTLeQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDER 1640
Cdd:TIGR00606 247 LDPLKNRL-KEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1641 KQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEarasrdEIFAQSKESEKKLKGLEAEI 1720
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL------DGFERGPFSERQIKNFHTLV 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1721 LQLQEEFAaserarRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMellneRFRKTTLQVDTL 1800
Cdd:TIGR00606 400 IERQEDEA------KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL-----KFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1801 NSELAGERSAAQKSENARQQLERQNKELKAKLQElEGSVKSKfKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEK 1880
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKE-VKSLQNE-KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1881 KLKEVFmqvEDERRHADQYKEQMEKANARmKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:TIGR00606 547 KDEQIR---KIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQL 621
|
|
| COG4372 |
COG4372 |
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown]; |
1471-1741 |
3.07e-04 |
|
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 226809 [Multi-domain] Cd Length: 499 Bit Score: 45.40 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1471 RQIVSNLEKKQKKFDQMLAEEKNISaryaEERDRAEAEaREKETKALSLARALEEALEAKEEFERQNKqLRADMEdlmss 1550
Cdd:COG4372 70 RSGVFQLDDIRPQLRALRTELGTAQ----GEKRAAETE-REAARSELQKARQEREAVRQELAAARQNL-AKAQQE----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1551 kddvgknVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQARDEQNEEKKRMLVKQ-- 1628
Cdd:COG4372 139 -------LARLTKQAQDLQTRLKTLAEQRRQLEAQAQSLQASQKQLQASATQLKSQ-VLDLKLRSAQIEQEAQNLATRan 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1629 -VRELEAELEderkqralavaakkkmemdlkdlegQIEAANKARDEAIKQLRKlQAQMKDyqreleEARASRDEifaQSK 1707
Cdd:COG4372 211 aAQARTEELA-------------------------RRAAAAQQTAQAIQQRDA-QISQKA------QQIAARAE---QIR 255
|
250 260 270
....*....|....*....|....*....|....
gi 45382679 1708 ESEKKLKGLEAEILQLQEEFAASERARRHAEQER 1741
Cdd:COG4372 256 ERERQLQRLETAQARLEQEVAQLEAYYQAYVRLR 289
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
832-1315 |
3.14e-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: 45.90 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 832 LARKAFAKKQQQLSALKILQRNCAAYlklrhwqwwrVFTKVKPllQVTRQEEELQAKD--EELMKVKEKQTKVEAELEEM 909
Cdd:pfam07111 201 LLRKQLSKTQEELEAQVTLVESLRKY----------VGEQVPP--EVHSQTWELERQEllDTMQHLQEDRADLQATVELL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 910 ERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQEL-----EEIL--------HDLESRVEEEEERNQILQ--- 973
Cdd:pfam07111 269 QVRVQSL---THMLALQEEELTRKIQPSDSLEPEFPKKCRSLlnrwrEKVFalmvqlkaQDLEHRDSVKQLRGQVAElqe 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 974 ------NEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIaecTSQLA 1047
Cdd:pfam07111 346 qvtsqsQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWL---ETTMT 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1048 EEEEKAKNLAKLKN------KQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEE 1121
Cdd:pfam07111 423 RVEQAVARIPSLSNrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAH 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1122 ELQAALARGDEEA-VQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELedtldttAAQQELR 1200
Cdd:pfam07111 503 LIQQEVGRAREQGeAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL-------TQQQEIY 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1201 TKREQE-VAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELAceVKVLQQVKA 1279
Cdd:pfam07111 576 GQALQEkVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKEEG--QRLARRVQE 653
|
490 500 510
....*....|....*....|....*....|....*.
gi 45382679 1280 ESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANK 1315
Cdd:pfam07111 654 LERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDK 689
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown]; |
1661-1884 |
3.40e-04 |
|
Uncharacterized N-terminal domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 226400 [Multi-domain] Cd Length: 265 Bit Score: 44.71 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1661 EGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERArrhaeqe 1740
Cdd:COG3883 37 DSKLSELQKEKKNIQNEIESLDNQIEEIQSKIDELQKEIDQSKAEIKKLQKEIAELKENIVERQELLKKRARA------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1741 rdelADEIANSASGKSALLDEKRRLEA--RIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENAR 1818
Cdd:COG3883 110 ----MQVNGTATSYIDVILNSKSFSDLisRVTAISVIVDADKKILEQQKEDKKSLEEKQAALEDKLETLVALQNELETQL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1819 QQLERQNKELKAKLQELegsvkskfKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKE 1884
Cdd:COG3883 186 NSLNSQKAEKNALIAAL--------AAKEASALGEKAALEEQKALAEAAAAEAAKQEAAAKAAAQE 243
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA ... |
1007-1153 |
3.74e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteristic 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: 433006 [Multi-domain] Cd Length: 712 Bit Score: 45.44 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1007 AEAKIKKM--EEEILLLEDQNSKFLKEKKLMEDRIA---ECTSQLAEEEEKAKNL--AKLKNKQEMMITDLEERLKKEEK 1079
Cdd:pfam13166 344 LEAKRKEPfkSIELDSVDAKIESIKDLVAAINELIAkhnEITDNLEEEKNKAKKKlwLFLVEEFKAEIDEYKDAYAGLEK 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1080 TRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDE-EAVQKNNALKVIRELQAQIAE 1153
Cdd:pfam13166 424 AINSLTKEIKNATAEIKKLRAEIRELEKQLRDHKPGADEINKLLAAFGFGELElAFNEEGKGYRIVRKGGSQAAE 498
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1030-1360 |
4.16e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227608 [Multi-domain] Cd Length: 1213 Bit Score: 45.69 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1030 KEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQI 1109
Cdd:COG5283 36 QFWKMLEKQQKLTKDGLSASKGKYEGLSEAMEKQKKAYEDLKQEVKEVNRATQASKKAYQEYNAQYTQAENKLRSLSGQF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1110 EELKIQLAKKEEELQAalargdeeavqknnalkvireLQAQIAEL----QEDLESEKASRNKAEKQKRDLSE-------E 1178
Cdd:COG5283 116 GVASEQLMLQQKEIQR---------------------LQYAISTLnksmAAQARLLEQTGNKFGTADAKVVGlresfgrQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1179 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEetknheaQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQ 1258
Cdd:COG5283 175 TEALNKQLERTKKVADALTYVLDEAQQKLSQALSARLE-------RLQESRTQMSQSSGQLGKRLETDKAGAGALGLLGA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1259 GLESDNKELACEVKVLQQVKAESEHKRKKLDAQvQELTAKVTEGERlrvELAEKANKLQNEL-DNVSSLLEEAEKKGIKF 1337
Cdd:COG5283 248 ALAGSFAAIGAAVRRTAQMNGELMDKTKQVKGA-RDNLGKVTSQGE---EMSDAIQETAEHIkDSGRELSKAAAIGAAAA 323
|
330 340
....*....|....*....|...
gi 45382679 1338 AKDAASLESQLQDTQELLQEETR 1360
Cdd:COG5283 324 MGVAAGKFPTGQEAKPTLKEMAR 346
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1031-1413 |
4.18e-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: 428594 [Multi-domain] Cd Length: 562 Bit Score: 45.40 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1031 EKKLMEDRIAECTSQLAEEEEkaknlAKLKNKQEMMIT---------DLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:pfam05701 43 ELEKVQEEIPEYKKQSEAAEA-----AKAQVLEELESTkrlieelklNLERAQTEEAQAKQDSELAKLRVEEMEQGIADE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 I-AELQAQIEELKIQLAKKEEELQAAlaRGDEEAVQKNNALKVI-RELQAQIAElqedlESEKASRnKAEKQKRDLSEEL 1179
Cdd:pfam05701 118 AsVAAKAQLEVAKARHAAAVAELKSV--KEELESLRKEYASLVSeRDIAIKRAE-----EAVSASK-EIEKTVEELTIEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1180 EALKTELEdtldttAAQQELRTKREQEVAeLKKAIEEETKNHEAQIQEIRQRhataLEELSEQLEQAKRFKANLEKNKQG 1259
Cdd:pfam05701 190 IATKESLE------SAHAAHLEAEEHRIG-AALAREQDKLNWEKELKQAEEE----LQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1260 LESDNKELACEVkvlqqvkaesehkrkklDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEA--EKKGIKF 1337
Cdd:pfam05701 259 LLDLKAELAAYM-----------------ESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEKAkdEVNCLRV 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1338 AkdAASLESQLQDTQELLqEETRQKLNLSS-RIRQLEEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKVDD 1413
Cdd:pfam05701 322 A--AASLRSELEKEKAEL-ASLRQREGMASiAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQEAEE 395
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1109-1247 |
4.50e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1109 IEELKIQLAKKEEELQAalargdEEAVQKNNALKVIRELQAQ--IAELQEDLESE-KASRNKAEKQKRDLSEELEALKTE 1185
Cdd:PRK12704 28 IAEAKIKEAEEEAKRIL------EEAKKEAEAIKKEALLEAKeeIHKLRNEFEKElRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1186 LEDTldttaaqqelrTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSE----QLEQAK 1247
Cdd:PRK12704 102 LELL-----------EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisglTAEEAK 156
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1009-1224 |
4.51e-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: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1009 AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAecTSQLAEEEEKAKNLAKLKnkqemmITDLEERLKKEEKTRQELEKAK 1088
Cdd:pfam12795 30 DKIDASKQRAAAYQKALDDAPAELRELRQELA--ALQAKAEAAPKEILASLS------LEELEQRLLQTSAQLQELQNQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1089 RKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKV-IRELQAQIAELQEDLESEKASRNK 1167
Cdd:pfam12795 102 AQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAeLAALKAQIDMLEQELLSNNNRQDL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1168 AEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKAIEEETKNHEAQ 1224
Cdd:pfam12795 182 LKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1015-1375 |
4.78e-04 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 45.40 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1015 EEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDge 1094
Cdd:COG5281 320 KENMGTLETAWDALADAAKKMWDAVLGIGREDKQAALLAAKLAAEKLARVTAQGALNARLKLAQDDLTQAELNYAAAD-- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1095 ttdlQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRD 1174
Cdd:COG5281 398 ----QAANQEGALNAREDEAEVLSTQEERRDILKNLLADAEKRTARQEELNKALAKAKILQADKAAKAYQEDILQREAQS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1175 LSEELEALKTELEDTLDTTAAQQELRT---------KREQEVAELKKAIEEETKNHEAQIQEIRQrHATALEELSEQLEQ 1245
Cdd:COG5281 474 RGKTAAAERSQEQMTAALKALLAFQQQiadlsgakeKASDQKSLLWKAEEQYALLKEEAKQRQLQ-EQKALLEHKKETLE 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1246 AKRFKANLeknkQGLESDNKELAceVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKlqNELDNVSS 1325
Cdd:COG5281 553 YTSQLAEL----LDQQADRFELS--AQAAGSQKERGSDLYREALAQNAAALNKALNELAAYWSALDLLQG--DWKAGALS 624
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1326 LLEEAEKKGIKFAKDAASLESQLQD--TQELLQEETRQKLNLSSRIRQLEEE 1375
Cdd:COG5281 625 ALANYRDSATDVASQAAQLFTNAFDgmANNAAKFATTGKLSFKSFTRSVLSD 676
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1217-1917 |
5.09e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 45.26 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1217 ETKNHEAQIQEIRQRHATALEELSEQ---LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEhKRKKLDAQVQ 1293
Cdd:COG3096 280 ERRVHLDQALEFRRELYTSRQQLAAEqyrHVDMSRELAELNGAEGDLEADYQAASDHLNLVQTALRQQE-KIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1294 ELTAKVTEgerlRVELAEKANKLQneldnvssllEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLE 1373
Cdd:COG3096 359 ELTIRLEE----QNEVVEEANERQ----------EENEARAEAAELEVDELKSQLADYQQALDVQQTRAIQYQQAIAALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1374 EEKNNLQEQQEEEeearKNLEKQMLALQAQLAEAKkkvdddlgtiEGLEENKKKLlkDMESLSQRLEEKA------MAYD 1447
Cdd:COG3096 425 RAKELCHLPDLTA----DSAEEWLETFQAKEEEAT----------EKLLSLEQKM--SMAQAAHSQFEQAyqlvvaIAGE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1448 KLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEK---------NISARYAEERDRAEAEAREKETKALS 1518
Cdd:COG3096 489 LARSEAWDVARELLREGPDQRHLAEQVQPLRMRLSELEQRLRQQQsaerlladfCKRQGKNLDAEELEALHQELEALIES 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1519 LARALEEALEAKEEFERQNKQLRADMEDLMS------SKDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDa 1592
Cdd:COG3096 569 LSDSVSNAREQRMALRQEQEQLQSRIQSLMQrapvwlAAQNALEQLSEQSGEEFTDSQDVTEYMQQLLEREREATVERD- 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1593 klRLEVNMQAMKAQFERdLQARDEQNEEKKRMLVKQ-----VRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEaa 1667
Cdd:COG3096 648 --ELGARKNALDEEIER-LSQPGGSEDQRLNALAERfggvlLSEIYDDVTIEDAPYFSALYGPSRHAIVVPDLSQVKE-- 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1668 nkardeaikQLRKLQAQMKDYQRELEEARASRDEIFAqskeSEKKLKGLEAEILQLQEEF-----------AASERARRH 1736
Cdd:COG3096 723 ---------HLEGLTDCPEDLYLIEGDPQSFDDSVFS----VDELEKAVVVKIADRQWRYsrfpeiplfgrAAREQRLES 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1737 AEQERDELADEIANSASGKSALldekRRLEARIAQ--LEEELEEEQSNMELLnerfrkttlqVDTLNSELAGERSAAQKS 1814
Cdd:COG3096 790 LHAERDVLSERHATLSFDVQKT----QRLHQAFSRfiGSHLAVAFEADPEAE----------IRQLNSRRNELERALSNH 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1815 ENARQQLERQNKELKAKLQELEGSVKSKFKATISTLEAKIAQLEEQLeQEAKERAAANKLVRRTEKKLKEVFMQVEDERR 1894
Cdd:COG3096 856 ENDNQQQRIQFDQAKEGVTALNRLIPQLNLLADESLADRVEEIRERL-DEAQEAARFIQQHGNTLSKLEPIASVLQSDPE 934
|
730 740
....*....|....*....|...
gi 45382679 1895 HADQYKEQMEKANARMKQLKRQL 1917
Cdd:COG3096 935 QFEQLKEDYAQAQQMQRQARQQA 957
|
|
| COG1579 |
COG1579 |
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ... |
1560-1686 |
5.20e-04 |
|
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];
Pssm-ID: 224495 [Multi-domain] Cd Length: 239 Bit Score: 43.89 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE-RDLQARDEQNEEKKRMLVKQVRELEAELED 1638
Cdd:COG1579 42 ALNKALEALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAVKDERElRALNIEIQIAKERINSLEDELAELMEEIEK 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 45382679 1639 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMK 1686
Cdd:COG1579 122 LEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELK 169
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1657-1915 |
6.00e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1657 LKDLEGQIEAANKARDEAIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKGLEAEILQLQEEFAASERarRH 1736
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1737 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNERFRKTTLQVDTLNSELAGERS 1809
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1810 AAQKSENARQQLERQNKELKAKLQElegsVKSKFKATISTLEAKIAQLEEQLEQeakeraaanklVRRTEKKLKEVFMQV 1889
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQ----ARNERKKTLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 45382679 1890 EDE-RRHADQYKEQMEKANARMKQLKR 1915
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1565-1719 |
6.07e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1565 KRTLEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQARDEQNEEKKRMLVKQVRELEAELED 1638
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1639 ERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKg 1715
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 45382679 1716 LEAE 1719
Cdd:PRK12704 184 EEAD 187
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1671-1836 |
6.11e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1671 RDEAIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkGLEAEILQLQEEFAASERARRHAEQERDELADEiAN 1750
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1751 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNErfrkttlQVDTLNSELAGERSAAQKSENARQQLERQ------ 1824
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 45382679 1825 --NKELKAKLQELE 1836
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| RmuC |
COG1322 |
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and ... |
1106-1277 |
6.42e-04 |
|
DNA anti-recombination protein (rearrangement mutator) RmuC [Replication, recombination and repair];
Pssm-ID: 224241 [Multi-domain] Cd Length: 448 Bit Score: 44.30 E-value: 6.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1106 QAQIEELKIQLAK-KEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESeKASRNKAEKQKRDLSEELEALKT 1184
Cdd:COG1322 2 QAILAILLILLLLvNLAFIRQLLLRLGRLEQMLGELAAVLEQLLLLLAFRAEAEQL-RTFARSLQALNLELIQELNELKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1185 ELEDTLDTTAAQQEL----RTKREQEVAELKKAIEEETKN-----HEAQIQEIRQRHATALEELSEQLEQ-----AKRFK 1250
Cdd:COG1322 81 RLQQQLLQSREQLQLliesLAQLSSEFQELANEIFEELNRrlaelNQQNLKQLLKPLREVLEKFREQLEQrihesAEERS 160
|
170 180
....*....|....*....|....*..
gi 45382679 1251 ANLEKNKQGLESdNKELACEVKVLQQV 1277
Cdd:COG1322 161 TLLEEIDRLLGE-IQQLAQEAGNLTAA 186
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1040-1183 |
6.45e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1040 AECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELqaqiEELKIQLAKK 1119
Cdd:PRK12705 35 AERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKL----DNLENQLEER 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1120 EEELQAALARGDEEAVQKNNALKVIRELQAQ------IAELQEDLESEKASRNKAEKQKRDLSEELEALK 1183
Cdd:PRK12705 111 EKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1108-1276 |
6.92e-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: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1108 QIEELKIQLAKKEEELQAALARGDEEavqknnaLKVIRELQAQIAELQEDLESEKASRNKAEKQKRDL-SEELEALKTEL 1186
Cdd:smart00787 141 LLEGLKEGLDENLEGLKEDYKLLMKE-------LELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCdPTELDRAKEKL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1187 EDTLDTTAAQQELRTKREQEVAELKKAIEEETknheAQIQEIRqrhataleelsEQLEQAKRFkanLEKNKQGLESDNKE 1266
Cdd:smart00787 214 KKLLQEIMIKVKKLEELEEELQELESKIEDLT----NKKSELN-----------TEIAEAEKK---LEQCRGFTFKEIEK 275
|
170
....*....|
gi 45382679 1267 LACEVKVLQQ 1276
Cdd:smart00787 276 LKEQLKLLQS 285
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1558-1798 |
7.02e-04 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 44.36 E-value: 7.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1558 VHELEKSKRTLEQQVEEMRTQLEELEDELQATEdakLRLEVNMQAMKAQFERDLQARDEQneekkrmlvkQVRELEAELE 1637
Cdd:COG3206 183 ADQLEAQLEAFRRASDSLDERLEELRARLQEAE---AQVEDFRAQHGLTDAARGQLLSEQ----------QLSALNTQLQ 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1638 DERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQREL-EEARASRDEIFAQSKESEKKLKGL 1716
Cdd:COG3206 250 SARARLAQAEARLASLLQLLPLGREAAALREVLESPTIQDLRQQYAQVRQQIADLsTELGAKHPQLVALEAQLAELRQQI 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1717 EAEILQLQEEfAASERARrhAEQERDELADEIANsASGKSALLDEkrrLEARIAQLEEELEEEQSNMELLNERFRKTTLQ 1796
Cdd:COG3206 330 AAELRQILAS-LPNELAL--LEQQEAALEKELAQ-LKGRLSKLPK---LQVQLRELEREAEAARSLYETLLQRYQELSIQ 402
|
..
gi 45382679 1797 VD 1798
Cdd:COG3206 403 EA 404
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1043-1219 |
7.08e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1043 TSQLAEEEEKAKNLAKLKNKQEmmitdleERLKKEEKT--RQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1120
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEA-------EAIKKEALLeaKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1121 EELQaalargdeeavQKNNALKvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEledtldtTAAQQ--- 1197
Cdd:PRK12704 103 ELLE-----------KREEELE---KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE-------EAKEIlle 161
|
170 180
....*....|....*....|..
gi 45382679 1198 ELRTKREQEVAELKKAIEEETK 1219
Cdd:PRK12704 162 KVEEEARHEAAVLIKEIEEEAK 183
|
|
| APG17 |
pfam04108 |
Autophagy protein Apg17; Apg17 is required for activating Apg1 protein kinases. |
1078-1354 |
7.09e-04 |
|
Autophagy protein Apg17; Apg17 is required for activating Apg1 protein kinases.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 43.92 E-value: 7.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1078 EKTRQELEKAKRKLDgETTD----LQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAE 1153
Cdd:pfam04108 17 TDARSLLEELVVLLA-KIAFlrrgLSVQLANLEKVREGLEKVLNELKKDFKQLLKDLDAALERLEETLDKLRNTPVEPAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1154 LQE-----------DLESEKASRNKAEKQKRDLSEELEALKTELeDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHE 1222
Cdd:pfam04108 96 PPGeekqktlldfiDEDSVEILRDALKELIDELQAAQESLDSDL-KRFDDDLRDLQKELESLSSPSESISLIPTLLKELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1223 AQIQEIRQrHATALEELSEQLEQAKR-FKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTE 1301
Cdd:pfam04108 175 SLEEEMAS-LLESLTNHYDQCVTAVKlTEGGRAEMLEVLENDARELDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDE 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1302 GerlrVELAEKANKLQNELDNVSSLLEEAEKkgiKFAKDAASLESQLQDTQEL 1354
Cdd:pfam04108 254 L----LSALQLIAEIQSRLPEYLAALKEFEE---RWEEEKETIEDYLSELEDL 299
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
1009-1189 |
7.16e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 43.85 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1009 AKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAEcTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKAK 1088
Cdd:PRK06669 2 PKVIFKRSNVINKEKLKTHEIQKYRFKVLSIKE-KERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1089 RKLDGETTDLQDQIAELQAQIEELKIQLAK-KEEELQAALARGDEEAVQKNNAlkvirELQAQIAELQEDLesekasRNK 1167
Cdd:PRK06669 81 EELLKKTDEASSIIEKLQMQIEREQEEWEEeLERLIEEAKAEGYEEGYEKGRE-----EGLEEVRELIEQL------NKI 149
|
170 180
....*....|....*....|..
gi 45382679 1168 AEKQKRDLSEELEALKTELEDT 1189
Cdd:PRK06669 150 IEKLIKKREEILESSEEEIVEL 171
|
|
| HSP70 |
pfam00012 |
Hsp70 protein; Hsp70 chaperones help to fold many proteins. Hsp70 assisted folding involves ... |
1005-1113 |
7.46e-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: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1005 VTAEAKIKKMEEEILLledQNSKFLKEKKlmEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKtrQEL 1084
Cdd:pfam00012 480 VSAKDKGTGKEQEITI---EASEGLSDDE--IERMVKDAEEYAEEDKKRKERIEAKNEAEEYVYSLEKSLEEEGD--KVP 552
|
90 100 110
....*....|....*....|....*....|....
gi 45382679 1085 EKAKRKLDGETTDL-----QDQIAELQAQIEELK 1113
Cdd:pfam00012 553 EAEKSKVESAIEWLkdeleGDDKEEIEAKTEELA 586
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1009-1194 |
7.53e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.23 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1009 AKIKKMEEEILLLEDQ----NSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQEL 1084
Cdd:PHA02562 174 DKIRELNQQIQTLDMKidhiQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1085 EKAKRKLDGETTDLQDQIAELQ-----------------------AQIEELKIQLAKKEEELQAALARGDEEAVQKNNAL 1141
Cdd:PHA02562 254 SAALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctqqisegpDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1142 ---KVIRELQAQIAELQEDLESE-------KASRNKAEKQKRDLSEELEALKTELEDTLDTTA 1194
Cdd:PHA02562 334 eqsKKLLELKNKISTNKQSLITLvdkakkvKAAIEELQAEFVDNAEELAKLQDELDKIVKTKS 396
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1043-1205 |
7.64e-04 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 43.95 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1043 TSQLAEEEEKAkNLAKLKNKQEmmitdleeRLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1122
Cdd:pfam00529 55 DYQAALDSAEA-QLAKAQAQVA--------RLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQID 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1123 LQAALARGDEEAVQKNNALkvirELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEAL--KTELEDTLDTTAAQQELR 1200
Cdd:pfam00529 126 LARRRVLAPIGGISRESLV----TAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvrSELSGAQLQIAEAEAELK 201
|
....*
gi 45382679 1201 TKREQ 1205
Cdd:pfam00529 202 LAKLD 206
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1616-1739 |
7.86e-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: 281941 [Multi-domain] Cd Length: 218 Bit Score: 43.14 E-value: 7.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1616 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIE------------AANKARDEAIKQLRKLQA 1683
Cdd:pfam04012 19 DKAEDPEKMLEQAIRDMQSELGKARQALAQVIARQKQLERKLEEQKEQAKklenkaraaltkGNEELAREALAEIATLEK 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1684 QMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEilqlQEEFAASERARRHAEQ 1739
Cdd:pfam04012 99 LAEALETQLTQQRSAVEQLRKQLAALETKIQQLKAK----KTALKARLKAAKAQEA 150
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
883-1298 |
8.74e-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: 434960 [Multi-domain] Cd Length: 1050 Bit Score: 44.49 E-value: 8.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 883 EELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFaeaeemRARLAAKKQELEEilhdlesrv 962
Cdd:pfam15818 14 EELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVF------KKQLQMKMCALEE--------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 963 eeeeernqilqnEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEI---LLLEDQNSKFLKEkklMEDRI 1039
Cdd:pfam15818 79 ------------EKGKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKVqlhLLAKEDHHKQLNE---IEKYY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1040 AECTSQLA---EEEEKA-----------KNLAKLKNKQEMMITDLEERLKK-----------------EEKT-----RQE 1083
Cdd:pfam15818 144 ATITGQFGlvkENHEKLeqnvqeaiqlnKRLSALNKKQESEICSLKKELKKvtsdlikskvtcqykmgEENInltikEQK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKRKLDGEtTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRElQAQIAELQEDLESEKA 1163
Cdd:pfam15818 224 FQELQERLNME-LELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKE-NNQTLERDNELQREKV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1164 SRNKA---------EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHAt 1234
Cdd:pfam15818 302 KENEEkflnlqnehEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKLEEDKKFQNVPEVNNENS- 380
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1235 alEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAK 1298
Cdd:pfam15818 381 --EMSTEKSENIIIQKYNSGQEIREENTKSFCSDTEYREKEKKKGPPVEEIIIEDLQVLEKSFK 442
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
996-1209 |
9.17e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 225177 [Multi-domain] Cd Length: 548 Bit Score: 44.05 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 996 ARQKLQLEKVTAEAKIKKMEEEILLLEDqnskfLKEKKLMEDRIAECTSQLAEEEEKaknLAKLKNKQEMMITDLEERLK 1075
Cdd:COG2268 272 AETEAEVAAWKAETRREAEQAEILAEQA-----IQEEKAQAEQEVQHAKALEAREMR---VGLIERQKETELEPQERSYF 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1076 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQ 1155
Cdd:COG2268 344 INAAQRQAQEEAKAAANIAEAIGAQAEAAVETARETEEAERAEQAALVAAAEAAEQEQVEIAVRAEAAKAEAEAQAAEIK 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1156 EDLEsekASRNKAEKQ---KRDLSEELEALKTEledtldTTAAQQELRTKREQEVAE 1209
Cdd:COG2268 424 AEAE---AIREKGKAEaeaKRALAEAIQVLGDA------AAAELFKALVQALPEVAE 471
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteristic of the AAA ... |
1146-1479 |
9.27e-04 |
|
AAA domain; This family of domains contain a P-loop motif that is characteristic 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: 433006 [Multi-domain] Cd Length: 712 Bit Score: 44.28 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1146 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL-------------RTKREQEVAELKK 1212
Cdd:pfam13166 93 EIQAKIAKLKKEIDDHEEKLEALTANLQKADKEKEKLEADFLDECWKKIKRKKDsalsealngfryeANFKSRLLREIEK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1213 AI--------EEETKNHEAQIQEIRQRHATALEELSEQLEQAKRfKANLEKNKQGLESDNKELACEVKVLQQVKAESEHK 1284
Cdd:pfam13166 173 DNfnagvlltDEDLKAALETVFGDNKPEIAPLSFDVIDFDALEK-AEILKQKVIGKSSAIAELIKNPDLADWVEEGLELH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1285 RKKLDAQV---QELTAKvtegerLRVELAEKANK-LQNELDNVSSLLEEAEKKGIKFAK--DAASLESQLQDTQELLQEE 1358
Cdd:pfam13166 252 KAHLDTCPfcgQPLPAE------RKAALEAHFDDeFTEFQRRLQKLIEKYESAISSLLAqlPAVSDLASLLSAFELDVED 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1359 -TRQKLNLSSRI---RQLEEEKnnlqeqqeeeeeaRKNLEK--QMLALQAQLAEAKKKVDDDLGTIE-------GLEENK 1425
Cdd:pfam13166 326 lKAEAEVLNSQLdglRQALEAK-------------RKEPFKsiELDSVDAKIESIKDLVAAINELIAkhneitdNLEEEK 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 45382679 1426 KKLLKDME-----SLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEK 1479
Cdd:pfam13166 393 NKAKKKLWlflveEFKAEIDEYKDAYAGLEKAINSLTKEIKNATAEIKKLRAEIRELEK 451
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1049-1647 |
9.44e-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: 44.36 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1049 EEEKAKNLAKLKNKQEMMITDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQ 1124
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1125 AALARgdEEAVQKNNALKVIRELQAQIAEL--QEDLESEKASRnkaeKQKRDLSEELEALKTELEDTLDTTAAQQELRTK 1202
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWELerQELLDTMQHLQ----EDRADLQATVELLQVRVQSLTHMLALQEEELTR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1203 REQEVAELKKaieEETKNHEAQIQEIRQRHATALEELSEQ----LEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1278
Cdd:pfam07111 289 KIQPSDSLEP---EFPKKCRSLLNRWREKVFALMVQLKAQdlehRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1279 AESEhkrkkldaqVQELTAKVTEGERLRVELAEKANKLQneldnvsslLEEAEKKgIKFAKDA-ASLESQLQDTQELLQE 1357
Cdd:pfam07111 366 AEVE---------VERMSAKGLQMELSRAQEARRRQQQQ---------TASAEEQ-LKFVVNAmSSTQIWLETTMTRVEQ 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1358 ETRQKLNLSSRIRQLEEEKNNLqeqqeEEEEARKNLEKQMLALQAQLAEAKKKVDDDLGT-IEGLEENKKKLLKDMEsLS 1436
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKVHTI-----KGLMARKVALAQLRQESCPPPPPAPPVDADLSLeLEQLREERNRLDAELQ-LS 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1437 QRL--EEKAMAYDKLEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKkfdqmlaeekniSARYAEERDRAEAEAREKET 1514
Cdd:pfam07111 501 AHLiqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLE------------VARQGQQESTEEAASLRQEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1515 KALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQvEEMRTQLEELEDELQATEDAKL 1594
Cdd:pfam07111 569 TQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQE-KERNQELRRLQDEARKEEGQRL 647
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1595 rlevnmqamkaqferdlqARDEQNEEKKRMLVKQVRELEAELEDERKQRALAV 1647
Cdd:pfam07111 648 ------------------ARRVQELERDKNLMLATLQQEGLLSRYKQQRLLAV 682
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1686-1884 |
9.72e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1686 KDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFaasERARRHAEQERDELADEIAnsasgksalldekrRL 1765
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIK--KEALLEAKEEI---HKLRNEFEKELRERRNELQ--------------KL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1766 EARIAQLEeeleeeqsnmELLNERfrkttlqvdtlNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKSKFK- 1844
Cdd:PRK12704 88 EKRLLQKE----------ENLDRK-----------LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELEr 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45382679 1845 -ATISTLEAKiAQLEEQLEQEAKERAAanKLVRRTEKKLKE 1884
Cdd:PRK12704 147 iSGLTAEEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1220-1449 |
1.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1220 NHEAQIQEIRQRHATaleelsEQLEQAKRFKANLEKnKQGLESDNKELacevKVLQQVKAESEHKrkkldAQVQELTAKV 1299
Cdd:PHA02562 180 NQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK-----AEIEELTDEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1300 TEGERLRVELAEKANKLQNELDNVSSLLEEAEKKgIKFAKDAA---SLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1376
Cdd:PHA02562 244 LNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1377 NNLQEQQEEEEEARK-----------------NLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRL 1439
Cdd:PHA02562 323 DELEEIMDEFNEQSKkllelknkistnkqsliTLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
250
....*....|
gi 45382679 1440 EEKAMAYDKL 1449
Cdd:PHA02562 403 YHRGIVTDLL 412
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
1567-1915 |
1.14e-03 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227606 [Multi-domain] Cd Length: 833 Bit Score: 43.86 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1567 TLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlqarDEQNEEKKRMLVKQVRELEAeLEDERKQRALA 1646
Cdd:COG5281 273 ALNRQFHYLTAAQLEQIAALQRAGDTAAAAAAAAEAAAAM--------DDRTARVKENMGTLETAWDA-LADAAKKMWDA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1647 VAAKKKMEMDLKDLEGQIEAANKARDEAIKQLrklQAQMKDYQRELEEARAS-RDEIFAQSKESEKKLKGLEAEILQLQE 1725
Cdd:COG5281 344 VLGIGREDKQAALLAAKLAAEKLARVTAQGAL---NARLKLAQDDLTQAELNyAAADQAANQEGALNAREDEAEVLSTQE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1726 EFAASERARRHAEQERDELADEIA--NSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSE 1803
Cdd:COG5281 421 ERRDILKNLLADAEKRTARQEELNkaLAKAKILQADKAAKAYQEDILQREAQSRGKTAAAERSQEQMTAALKALLAFQQQ 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1804 LA-----GERSAAQKSENARQQLERQNKELKAKLQELegSVKSKFKATISTLEAKIAQLEEQLEQEAkeraaanklvRRT 1878
Cdd:COG5281 501 IAdlsgaKEKASDQKSLLWKAEEQYALLKEEAKQRQL--QEQKALLEHKKETLEYTSQLAELLDQQA----------DRF 568
|
330 340 350
....*....|....*....|....*....|....*...
gi 45382679 1879 EKKLKEVFMQVEDER-RHADQYKEQMEKANARMKQLKR 1915
Cdd:COG5281 569 ELSAQAAGSQKERGSdLYREALAQNAAALNKALNELAA 606
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
997-1241 |
1.16e-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: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 997 RQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKE--KKLMEDRIAECTSQLAEEEEKAKNlaklknkqemmITDLEERL 1074
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSS-----------LKELLTQL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1075 KKEEKTRQELEKAKRKLdgetTDLQDQIaelQAQIEELKIQLAKKEEElqaalarGDEEAVQKNNALKVIRELQAQIAEL 1154
Cdd:COG5391 375 QDEIKSRESLILTDSNL----EKLTDQN---LEDVEELSRSLRKNSSQ-------RAVVSQQPEGLTSFSKLSYKLRDFV 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1155 QEDleSEKASRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHAT 1234
Cdd:COG5391 441 QEK--SRSKSIESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKS 516
|
....*..
gi 45382679 1235 ALEELSE 1241
Cdd:COG5391 517 VKEQLDR 523
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
1607-1926 |
1.18e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 44.11 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1607 FERDL-QARDEQNEEKKRmLVKQVRELEAELEDERK---------------QRALAVAAK-KKMEMDLKDLEGQIEAANK 1669
Cdd:COG3096 291 FRRELyTSRQQLAAEQYR-HVDMSRELAELNGAEGDleadyqaasdhlnlvQTALRQQEKiERYQADLEELTIRLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1670 ARDEAIKQLRKLQAQMKDYQRELeearasrDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEqerdeLADEIA 1749
Cdd:COG3096 370 VVEEANERQEENEARAEAAELEV-------DELKSQLADYQQALDVQQTRAIQYQQAIAALERAKELCH-----LPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1750 NSASgksALLDEKRRLEARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAgeRSAAQKSEnarQQLERQNKELK 1829
Cdd:COG3096 438 DSAE---EWLETFQAKEEEATEKLLSLEQKMSMAQAAHSQFEQAYQLVVAIAGELA--RSEAWDVA---RELLREGPDQR 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1830 AKLQElegsvkskfkatISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHADQYKEQMEKANAR 1909
Cdd:COG3096 510 HLAEQ------------VQPLRMRLSELEQRLRQQQSAERLLADFCKRQGKNLDAEELEALHQELEALIESLSDSVSNAR 577
|
330 340
....*....|....*....|..
gi 45382679 1910 -----MKQLKRQLEEAEEEATR 1926
Cdd:COG3096 578 eqrmaLRQEQEQLQSRIQSLMQ 599
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1570-1959 |
1.23e-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: 428594 [Multi-domain] Cd Length: 562 Bit Score: 43.86 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1570 QQVEEMRTQ-LEELEDELQATEDAKLRLEvnmqamKAQFErDLQARdeQNEEKKRMLVKQVRE---------LEAELEDE 1639
Cdd:pfam05701 59 EAAEAAKAQvLEELESTKRLIEELKLNLE------RAQTE-EAQAK--QDSELAKLRVEEMEQgiadeasvaAKAQLEVA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 RKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRklqaqmkdyqreleearasrdEIFAQSKESEKKLKGLEAE 1719
Cdd:pfam05701 130 KARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAE---------------------EAVSASKEIEKTVEELTIE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1720 ILQLQEEFAASERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMELL-NERFRKT 1793
Cdd:pfam05701 189 LIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASALLlDLKAELA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1794 TLQVDTLNSELAGERSAAQKSENARQQLERQNKELkaklQELEGSVKsKFKATISTLEAKIAQLEEQLEQEAKERAAank 1873
Cdd:pfam05701 268 AYMESKLKEEADGEGNEKKTSTSIQAALASAKKEL----EEVKANIE-KAKDEVNCLRVAAASLRSELEKEKAELAS--- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1874 lVRRTEKKLKEVFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLS 1949
Cdd:pfam05701 340 -LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAK 418
|
410
....*....|
gi 45382679 1950 REVSTLKNRL 1959
Cdd:pfam05701 419 AAASTVESRL 428
|
|
| EzrA |
COG4477 |
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ... |
894-1331 |
1.26e-03 |
|
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 226883 [Multi-domain] Cd Length: 570 Bit Score: 43.52 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 894 KVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEA----EEMRARLAAKKQELEEILHDLesrveeeeern 969
Cdd:COG4477 101 KAKHEIDDIEQQLTLIEEDIEQILEDLNELVESEEKNSEEIDHVlelyEELRRDVLANRHQYGEAAPEL----------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 970 qilqnekkkmqghiqdleeqldeeegarqklqlekvtaEAKIKKMEEEILLLEDQNSKflkekklmEDRIaECTSQLAEE 1049
Cdd:COG4477 170 --------------------------------------EKKLENIEEELSQFVELTSS--------GDYI-EAREVLEEA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1050 EEKAKNLAKLKNKQEMMITDLEERLKKEektRQELEKAKRKLDGETTDLQDqiAELQAQIEELKIQLAKKEEELqaalar 1129
Cdd:COG4477 203 EEHMIALRSIMERIPSLLAELQTELPGQ---LQDLKAGYRDMKEEGYHLEH--VNIDSRLERLKEQLVENSELL------ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1130 gdeEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTA--------AQQELRT 1201
Cdd:COG4477 272 ---TQLELDEAEEELGLIQEKIESLYDLLEREVEAKNVVEENLPILPDYLEKAKENNEHLKEEIErvkesyrlAETELGS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1202 KR--EQEVAELKKAIEEETKNHEAQIQEIRQRHATaLEELSEQLEQAKRFKANLEKNKQGLESDnkELACEVKVLQQVKA 1279
Cdd:COG4477 349 VRkfEKELKELESVLDEILENIEAQEVAYSELQDN-LEEIEKALTDIEDEQEKVQEHLTSLRKD--ELEARENLERLKSK 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1280 ESEHKRKKLDAQV-----QELTAKVTEGERLRvELAEKANKLQNELDNVSSLLEEAE 1331
Cdd:COG4477 426 LHEIKRYMEKSNLpglpeTFLSLFFTAGHEIQ-DLMKELSEVPINMEAVSALVDIAT 481
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1267-1556 |
1.26e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 43.56 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1267 LACEVKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLES 1346
Cdd:COG4942 22 LSAAVLAAAFSAAADDKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASLEAQLIETADDLKKLRKQIADLNA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1347 QLQDtqeLLQEETRQKLNLSSRIR--QLEEEKNNLQEQQEEEEEARKNLEKQML-ALQAQLAEAKKKVDDDLGTIEGLE- 1422
Cdd:COG4942 102 RLNA---LEVQEREQRRRLAEQLAalQRSGRNPPPALLVSPEDAQRSVRLAIYYgALNPARAERIDALKATLKQLAAVRa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1423 --ENKKKLLKDMESlSQRLEEKAMAYDKLEKTKNrlqqelddlmvdldhQRQIVSNLEKKQKKFDQMLAEEKNISARYAe 1500
Cdd:COG4942 179 eiAAEQAELTTLLS-EQRAQQAKLAQLLEERKKT---------------LAQLNSELSADQKKLEELRANESRLKNEIA- 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1501 erdRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1556
Cdd:COG4942 242 ---SAEAAAAKAREAAAAAEAAAARARAAEAKRTGETYKPTAPEKMLISSTGGFGA 294
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1068-1304 |
1.32e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1068 TDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE----EELQAALARGDEEAVQ---KNNA 1140
Cdd:PRK11637 71 ASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEQQQAAQErllaAQLDAAFRQGEHTGLQlilSGEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1141 LKVIRELQAQIAEL----QEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEE 1216
Cdd:PRK11637 151 SQRGERILAYFGYLnqarQETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQK 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1217 EtknhEAQIQEIRQRHAtaleELSEQLEQAKR-FKANLEKnkqglesdnkelacEVKVLQQVKAesehkrKKLDAQVQEL 1295
Cdd:PRK11637 231 D----QQQLSELRANES----RLRDSIARAEReAKARAER--------------EAREAARVRD------KQKQAKRKGS 282
|
....*....
gi 45382679 1296 TAKVTEGER 1304
Cdd:PRK11637 283 TYKPTESER 291
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1202-1408 |
1.32e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 42.62 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1202 KREQEVAELKKAIEEETKNHEAQIQEIRQRhATALEELSEQLEQAKRFkanleknkqgLESDNKELACEVKVLQQVKAES 1281
Cdd:pfam00769 6 REKQELEERLKQYEEETRKAQEELEESEET-AELLEEKLRVAEEEAEL----------LEQKAQEAEEEKERLEESAEME 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1282 EHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQ 1361
Cdd:pfam00769 75 AEEKEQLERELREAQEEVARLEEESERKEEEAERLQEELEEAREEEEEAKEKLLAASTSPSHHHSEESENEDDEEEEESY 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45382679 1362 KLNLSSRIRQLEEEKNNLQEQQEEEEEARKN--LEKQMLALQAQLAEAK 1408
Cdd:pfam00769 155 EGGSAELSNDGDMDQLSDRIEEERVTEAEKNerLQKQLKALKSELAQAR 203
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1102-1254 |
1.34e-03 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 43.18 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQAQIEELKIQLAKkeeeLQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEA 1181
Cdd:pfam00529 53 PTDYQAALDSAEAQLAK----AQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1182 LKTELED------TLDTT-AAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLE 1254
Cdd:pfam00529 129 RRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| HEC1 |
COG5185 |
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, ... |
1321-1698 |
1.37e-03 |
|
Protein involved in chromosome segregation, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227512 [Multi-domain] Cd Length: 622 Bit Score: 43.43 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1321 DNVSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKQM--- 1397
Cdd:COG5185 249 DNYEPSEQELKLGFEKFVHIINTDIANLKTQNDNLYEKIQEAMKISQKIKTLREKWRALKSDSNKYENYVNAMKQKSqew 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1398 LALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDL-DHQRQIVSN 1476
Cdd:COG5185 329 PGKLEKLKSEIELKEEEIKALQSNIDELHKQLRKQGISTEQFELMNQEREKLTRELDKINIQSDKLTKSVkSRKLEAQGI 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1477 LEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSlaraleealeakEEFERQNKQLRADMEDLMSSKDDVgk 1556
Cdd:COG5185 409 FKSLEKTLRQYDSLIQNITRSRSQIGHNVNDSSLKINIEQLF------------PKGSGINESIKKSILELNDEIQER-- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1557 nVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAEL 1636
Cdd:COG5185 475 -IKTEENKSITLEEDIKNLKHDINELTQILEKLELELSEANSKFELSKEENERELVAQRIEIEKLEKELNDLNLLSKTSI 553
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1637 --EDERKQRA------LAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAqmkDYQRELEEARAS 1698
Cdd:COG5185 554 ldAEQLVQSTeikldeLKVDLNRKRYKIHKQVIHVIDITSKFKINIQSSLEDLEN---ELGKVIEELRNL 620
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1024-1854 |
1.39e-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: 43.89 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1024 QNSKFLKEKKLMEDRIAECTSQLAEEEekaknLAKLKNK-----QEMMITDLEERLKkeektrqeLEKAKRKLDGETTDL 1098
Cdd:TIGR01612 646 QVPEHLKNKDKIYSTIKSELSKIYEDD-----IDALYNElssivKENAIDNTEDKAK--------LDDLKSKIDKEYDKI 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1099 QDQiaelqaQIEELKIQLAKKEEelqaalargdeeavQKNNALKVIRELQAQI-AELQEDLESEKASRNKAEKQkrdLSE 1177
Cdd:TIGR01612 713 QNM------ETATVELHLSNIEN--------------KKNELLDIIVEIKKHIhGEINKDLNKILEDFKNKEKE---LSN 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1178 ELEALKTELEDTLDTTAAQQELRTKREQEVAeLKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFK------- 1250
Cdd:TIGR01612 770 KINDYAKEKDELNKYKSKISEIKNHYNDQIN-IDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKddflnkv 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1251 ---ANLEKN-KQGLESDNKELAcevKVLQQVKAESEhkrkklDAQVQELTAKVTEGERLrveLAEKANKLQNELDNVSSL 1326
Cdd:TIGR01612 849 dkfINFENNcKEKIDSEHEQFA---ELTNKIKAEIS------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTL 916
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1327 LEEAEKkgIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNNlqeqQEEEEEARKNLEKQMLALQAQLAE 1406
Cdd:TIGR01612 917 KKVDEY--IKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKD----KFDNTLIDKINELDKAFKDASLND 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1407 AKKKVDDDLGTIEGLEENKKKLLKDMesLSQRLEEKamaydklEKTKNRLQQELDDLmvdldhqRQIVSNLEKKQKKFDQ 1486
Cdd:TIGR01612 991 YEAKNNELIKYFNDLKANLGKNKENM--LYHQFDEK-------EKATNDIEQKIEDA-------NKNIPNIEIAIHTSIY 1054
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1487 MLAEE------KNISARYAEERDRAEA------EAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDV 1554
Cdd:TIGR01612 1055 NIIDEiekeigKNIELLNKEILEEAEInitnfnEIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKI 1127
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1555 GKNVHELEKSKRTLEQQVEEMRTQLEELEDELQAT---EDAKlRLEVNMQAMKAQFERDLQARDEQNEekkrmLVKQVRE 1631
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAE 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1632 LEAELEDERKQRALAVAAKKKMEmdlKDLEGQIEAANKARDEAIKQlrkLQAQMKDYqreleearasrDEIFAQSKESEK 1711
Cdd:TIGR01612 1202 IEKDKTSLEEVKGINLSYGKNLG---KLFLEKIDEEKKKSEHMIKA---MEAYIEDL-----------DEIKEKSPEIEN 1264
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1712 KLkGLEAEILQLQEEFAAS-ERARRH--AEQERDELADEIANSA-------SGKSALLDEKRRLEARIAQleeeleeEQS 1781
Cdd:TIGR01612 1265 EM-GIEMDIKAEMETFNIShDDDKDHhiISKKHDENISDIREKSlkiiedfSEESDINDIKKELQKNLLD-------AQK 1336
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45382679 1782 NMELLNERFRKTTLQVDTLnsELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVKS-KFKATISTLEAKI 1854
Cdd:TIGR01612 1337 HNSDINLYLNEIANIYNIL--KLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKiKDDINLEECKSKI 1408
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1071-1251 |
1.40e-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 tumor cells.
Pssm-ID: 431106 Cd Length: 713 Bit Score: 43.50 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1071 EERLKKEEKTRQELEKAKRKLDGETtdlQDQIAELQAQIEELKI------QLAKKEEELQaalargDEEAVQKNNALKVI 1144
Cdd:pfam10168 546 EEYLKKHDLAREEIQKRVKLLKLQK---EQQLQELQSLEEERKSlseraeKLAEKYEEIK------DKQEKLMRRCKKVL 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1145 RELQAQIAELQEdlesekasrnkaekQKRDLSEELEALKTELEdTLDttAAQQELRTKREQEVAELKKAIEEETKN---- 1220
Cdd:pfam10168 617 QRLNSQLPVLSD--------------AEREMKKELETINEQLK-HLA--NAIKQAKKKMNYQRYQIAKSQSPRKKSslsl 679
|
170 180 190
....*....|....*....|....*....|....
gi 45382679 1221 ---HEAQIQEIRQRHAtalEELSEQLEQAKRFKA 1251
Cdd:pfam10168 680 sekQRKTIKEILKQLG---SEIDELIKQVKDINK 710
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1616-1815 |
1.44e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 42.30 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1616 EQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEMDL-------KDLEGQIEAANKARDEAIkqLRKLQAQMKDY 1688
Cdd:COG1842 20 DKAEDPEKMLEQAIRDMESELAKARQALAQAIARQKQLERKLeeaqaraEKLEEKAELALQAGNEDL--AREALEEKQSL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1689 QRELEEARASRDEIFAQSKESEKKLKGLEAEILQL---QEEFAASERARRHAEQERDELADeiANSASGKSALLDEKRRL 1765
Cdd:COG1842 98 EDLAKALEAELQQAEEQVEKLKKQLAALEQKIAELrakKEALKARKAAAKAQEKVNRSLGG--GSSSSAMAAFERMEEKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45382679 1766 EARIAQLEEELEEEQSNMELLNERFRKTTLQvDTLNSELAGERSAAQKSE 1815
Cdd:COG1842 176 EEREARAEAAAELAEGSGDDLDKEFAQAGAQ-SAVDSRLAALKARMKGPA 224
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1264-1698 |
1.57e-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: 43.57 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1264 NKELACEVKVLQQVKAESEHKRKKLDAQVQELTAKVtEGERLRVELAEKANKLqneldnvsslleeaekkgikfakdaas 1343
Cdd:pfam17380 261 NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKM-EQERLRQEKEEKAREV--------------------------- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1344 lesqlqdtqellqeETRQKLNLSSRIRQLEEEKnnlqeqqeeeeearknlEKQMLALQAQLAEAKKKvdddlgTIEGLEE 1423
Cdd:pfam17380 313 --------------ERRRKLEEAEKARQAEMDR-----------------QAAIYAEQERMAMERER------ELERIRQ 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1424 NKKKllKDMESLSQrlEEKAMAYDK---LEKTKNRLQQELDDLMVDLDHQRQIVSNLEKKQKKFDQMLAEEKNISARyae 1500
Cdd:pfam17380 356 EERK--RELERIRQ--EEIAMEISRmreLERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE--- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1501 erdraEAEAREKETKALSLARALEEALEAKEEFERQNKqlradMEDLMSSKDDVGKNVHELEKSKRTlEQQVEEMRTQLE 1580
Cdd:pfam17380 429 -----QEEARQREVRRLEEERAREMERVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKIL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1581 ELEdelqatedaklrLEVNMQAMKaqferdlqardeQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKMEM-DLKD 1659
Cdd:pfam17380 498 EKE------------LEERKQAMI------------EEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMeERRR 553
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 45382679 1660 LEGQIEAANKARD--EAIKQLRKLQAQMKDYQRELEEARAS 1698
Cdd:pfam17380 554 IQEQMRKATEERSrlEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| YhaN |
COG4717 |
Uncharacterized protein YhaN, contains AAA domain [Function unknown]; |
882-1460 |
1.64e-03 |
|
Uncharacterized protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 227061 [Multi-domain] Cd Length: 984 Bit Score: 43.68 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAE-EMRARLAAKKQELEEILHDLES 960
Cdd:COG4717 287 EAEIDALLVRLAELKDLASQLIPAKEAVLQALVRLHQQLSEIKASAFELTETLAGIEaDLRDKEEAAGNGFEAERVHDLR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 961 RveeeeernqiLQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKklmedria 1040
Cdd:COG4717 367 S----------LECMLRYQSSQRELKQTEAAYCKRLDEKRLFEDEAEEEARQRLADDEEEVRAGDEAREEKI-------- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1041 ECTSQLAEEEEKAKNLAKLKNKQemmitdLEERLKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQIEELKI---QLA 1117
Cdd:COG4717 429 AANSQVIDKEEVCNLYDRRDTAW------QKQRFLREKQTAFERQKTEHT---KIIALRLAGMLLVALSRLLTSlifQII 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1118 KKEEELQAALARG---DEEAVQKNNALKVIRELQAQIAELQE----DLESEKASRNKAEKQK-RDLSEELEALKTELEDT 1189
Cdd:COG4717 500 FAVAQIVFLSAEIkssSRAVREEKAAVTDIPEELARLLITDElpelAVDLLVQSRIRQHWQQlRKALDQLEAAYEALEGR 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1190 LDT-TAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIR-----QRHATALEELSEQLEQAKR-FKANLEKNKQGLES 1262
Cdd:COG4717 580 FAAaEAAMAEWQSEWEEALDELGLSRELSPEQQLDILSTMKdlkklMQKKAELTHQVARLREEQAaFEERVEGLLAVLEA 659
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1263 DNKELACEVKVLQ-QVKAESEHKRKKLDAQVQELtakVTEGERLRVELAEKANKLQneldnVSSLLEEAEKKGIKFAKDA 1341
Cdd:COG4717 660 QFIDLSTLFCVQRlRVAAELQKEEARLALEGNIE---RTKELNDELRAELELHRKE-----ILDLFDCGTADTEDAFREA 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1342 ASLESQLQDTQELLQEETRQKLNLSSRIRQL---EEEKNNLQEQQEEEEEARKNLEKQMLALQAQLAEAKKKvdddlgtI 1418
Cdd:COG4717 732 AREEQQLTQRESRLESLEAQLEGVAAEAYELsasLDQRELKEEELALLEEAIDALDEEVEELHAQVAALSRQ-------I 804
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 45382679 1419 EGLEENKK--KLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQEL 1460
Cdd:COG4717 805 AQLEGGGTvaELRQRRESLKEDLEEKARKWASLRLAVQVLEEAL 848
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1048-1319 |
1.64e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1048 EEEEKAKNLAKLKNKQEmmitdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAL 1127
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1128 ARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA-----SRNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRTK 1202
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAvaaaiARAKAKKA------AQQAANAEAEEEVDPKKAAVAAAIA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1203 ReqevAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKqgLESDNKELAcevkvlqqVKAESE 1282
Cdd:PRK05035 588 R----AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPE--EPVDPRKAA--------VAAAIA 653
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 45382679 1283 HKRKKLDAQVQELTAKVTEGERLRVELAE-----KANKLQNE 1319
Cdd:PRK05035 654 RAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1098-1336 |
1.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1098 LQDQIAELQAQIEELKIQLAKKEEELqaalargdeeAVQKNNaLKVIRELQAQ-IAELQEDLESEKASRNKAEKQKRDLS 1176
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQI----------KTYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1177 EELEALKTELEdtlDTTAAQQELRTKREQ---EVAELKKAIEEETKNHE------------AQIQEIRQRHA-------- 1233
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAAAKiksKIEQFQKVIKMYEKGGVcptctqqisegpDRITKIKDKLKelqhslek 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1234 --TALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEhkrkKLDAQVqelTAKVTEGERLRVELAE 1311
Cdd:PHA02562 318 ldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE----ELQAEF---VDNAEELAKLQDELDK 390
|
250 260 270
....*....|....*....|....*....|.
gi 45382679 1312 KANKLQN------ELDNVSSLLEEAekkGIK 1336
Cdd:PHA02562 391 IVKTKSElvkekyHRGIVTDLLKDS---GIK 418
|
|
| GumC |
COG3206 |
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane ... |
1091-1412 |
1.71e-03 |
|
Uncharacterized protein involved in exopolysaccharide biosynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225747 [Multi-domain] Cd Length: 458 Bit Score: 43.20 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1091 LDGETTDLQDQIAELQAQIEELK-----IQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLES-EKAS 1164
Cdd:COG3206 68 LEDGQSGLPNDSSSLETEIEILQsrsvlEKVIDKLKLDDDPEFVGKPLIASFLRLLKDLIGPDPTIFEISYRLDDlLESL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1165 RNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAIEEEtknhEAQIQEIRQRhatalEELSEQLE 1244
Cdd:COG3206 148 KVLRAGRSRVIELSYTSNDPKLAAKLANALAQAYLADQLEAQLEAFRRASDSL----DERLEELRAR-----LQEAEAQV 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1245 QAKRFKANLE-KNKQGLESDNkELACEVKVLQQVKAESEHKRKKLdAQVQELTAKVTEGERLRVELAEKA-NKLQNELDN 1322
Cdd:COG3206 219 EDFRAQHGLTdAARGQLLSEQ-QLSALNTQLQSARARLAQAEARL-ASLLQLLPLGREAAALREVLESPTiQDLRQQYAQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1323 VSSLLEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQklNLSSRIRQLEEEKNNLQEQQEEEEEARKNLEKqMLALQA 1402
Cdd:COG3206 297 VRQQIADLSTELGAKHPQLVALEAQLAELRQQIAAELRQ--ILASLPNELALLEQQEAALEKELAQLKGRLSK-LPKLQV 373
|
330
....*....|
gi 45382679 1403 QLAEAKKKVD 1412
Cdd:COG3206 374 QLRELEREAE 383
|
|
| YloA |
COG1293 |
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains ... |
1008-1172 |
1.80e-03 |
|
Predicted component of the ribosome quality control (RQC) complex, YloA/Tae2 family, contains fibronectin-binding (FbpA) and DUF814 domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 224212 [Multi-domain] Cd Length: 564 Bit Score: 43.15 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1008 EAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEKA 1087
Cdd:COG1293 292 EKELKKLENKLEKQEDELEELEKAAEELRQKGELLYANLQLIEEGLKSVRLADFYGNEEIKIELDKSKTPSENAQRYFKK 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1088 KRKLDGETTDLQDQIAELQAqiEELKIQLAKKeeelqaalargdeeAVQKNNALKVIRELQAQIAELQEDLESEKASRNK 1167
Cdd:COG1293 372 YKKLKGAKVNLDRQLSELKE--AIAYYESAKT--------------ALEKAEGKKAIEEIREELIEEGLLKSKKKKRKKK 435
|
....*
gi 45382679 1168 AEKQK 1172
Cdd:COG1293 436 EWFEK 440
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
1006-1127 |
1.87e-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: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1006 TAEAKIKKMEEEILLLEDQnskflkekklmedrIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELE 1085
Cdd:smart00435 274 THEKSMEKLQEKIKALKYQ--------------LKRLKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEE 339
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 45382679 1086 KAKRkldgettdlqdQIAELQAQIEELKIQLAKKEEELQAAL 1127
Cdd:smart00435 340 KKKK-----------QIERLEERIEKLEVQATDKEENKTVAL 370
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1561-1765 |
1.96e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1561 LEKSK-RTLEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1639
Cdd:PHA02562 171 LNKDKiRELNQQIQTLDMKIDHIQQQIKTYNKNIEEQR----KKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1640 RKQRALAVAAKKKMEMDLKDLEGQIEAANK----------------ARDEAIKQLRKLQAQMKDYQRELEEARASRDE-- 1701
Cdd:PHA02562 247 VMDIEDPSAALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctqQISEGPDRITKIKDKLKELQHSLEKLDTAIDEle 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45382679 1702 -IFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1765
Cdd:PHA02562 327 eIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKI 391
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1390-1590 |
2.13e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 41.85 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1390 RKNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLMVDLDH 1469
Cdd:pfam00769 8 KQELEERLKQYEEETRKAQEELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEMEAEEKEQLERELRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1470 QRQIVSNL--EKKQKKFDQMLAEEKNISARYAEERDRAE-AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1546
Cdd:pfam00769 88 AQEEVARLeeESERKEEEAERLQEELEEAREEEEEAKEKlLAASTSPSHHHSEESENEDDEEEEESYEGGSAELSNDGDM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45382679 1547 LMSSKDDVGKNVHELEKSKRtLEQQVEEMRTQLEELEDELQATE 1590
Cdd:pfam00769 168 DQLSDRIEEERVTEAEKNER-LQKQLKALKSELAQARDETKQTQ 210
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1516-1645 |
2.17e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 43.15 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1516 ALSLARALEEALEAKEEFERQNKQLRADMEDLMsskdDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELqatEDAKLR 1595
Cdd:COG2433 393 ALSKVKEEERPREKEGTEEEERREITVYEKRIK----KLEETVERLEEENSELKRELEELKREIEKLESEL---ERFRRE 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1596 LEVnmqamKAQFERDLQARDEQNEEKKRMLV---KQVRELEAELEDERKQRAL 1645
Cdd:COG2433 466 VRD-----KVRKDREIRARDRRIERLEKELEekkKRVEELERKLAELRKMRKL 513
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1107-1332 |
2.18e-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: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1107 AQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTEL 1186
Cdd:pfam06008 12 PAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1187 EDTLDT-TAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQ-LEQAKRFKANLEKNKQGLESDN 1264
Cdd:pfam06008 92 KNLIDNiKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAeLKAAQDLLSRIQTWFQSPQEEN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45382679 1265 KELAcevKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELAEKANKLQNELDNVSSLLEEAEK 1332
Cdd:pfam06008 172 KALA---NALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
919-1122 |
2.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 919 EKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLEsrveeeeernQILQNEKKKMQGHIQDLEEQLDEEEGARQ 998
Cdd:PHA02562 189 KIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEA----------KTIKAEIEELTDELLNLVMDIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 999 KLQLEKVTAEAKIKKMEEEILLLEDQN------SKFLKEKKLME---DRIAECTSQLAEEEEKAKNLAKLKN---KQEMM 1066
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYEKGGvcptctQQISEGPDRITkikDKLKELQHSLEKLDTAIDELEEIMDefnEQSKK 338
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1067 ITDLEERLKKEEKTRQ-------ELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEE 1122
Cdd:PHA02562 339 LLELKNKISTNKQSLItlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1067-1188 |
2.45e-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: 41.83 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1067 ITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRE 1146
Cdd:pfam11932 15 LDQALDLAEKAVAAAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQIEEIERTERE 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 45382679 1147 LQAQIAELQEDLESEKASR---NKAEKQKRdlseeLEALKTELED 1188
Cdd:pfam11932 95 LVPLMLKMLDRLEQFVALDlpfLLEERQAR-----LARLRELMDD 134
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1609-1747 |
2.49e-03 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1609 RDLQARDEQNEEKKRMLVKQVRELEAELeDERKQRALAVAAKKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDY 1688
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAEL-DRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1689 -------QRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADE 1747
Cdd:pfam00529 133 apiggisRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEA 198
|
|
| HOOK |
pfam05622 |
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different ... |
1535-1885 |
2.52e-03 |
|
HOOK protein; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organisms. 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 the 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.
Pssm-ID: 428548 [Multi-domain] Cd Length: 526 Bit Score: 42.73 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1535 RQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLEQQVEEMRTQLEE---LEDE---LQATEDAKLRLEVNMQAMKAQFE 1608
Cdd:pfam05622 66 KQLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTSLAEEaqaLKDEidiLRESSDKVSKLEATVETYKKKLE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1609 --RDLQARDEQNEEKKRMLVKQVRELEAELEDERKQRALAVAAKKKmemdLKDLEGQIEAANKARDEAIKQLRKLQAQMK 1686
Cdd:pfam05622 146 dlGDLRRQVKLLEERNAVYMQNTVSLEEELKKANALRGQLELYKRQ----VQELHGKLSEESKKADKLEFEYKKLEEKLE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1687 DYQRELEEARASRDEIfaqsKESEKKLKgleaeILQLQEEFAASERARRHAEQERDELADEIANSASGKSAL---LDEKR 1763
Cdd:pfam05622 222 ALQKEKERLIIERDTL----RETNEELR-----CAQLQQDELSQADALGSPSSSVDNLAAEILPAEIREKLIrlqHENKM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1764 RLEARIAQLEEELEEEQSNME--------------LLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELK 1829
Cdd:pfam05622 293 LRLQQEGSEREKLTELQALLEdanrrkneletqnrLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLH 372
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1830 AKLQELEgsvksKFKATISTLEA-------KIAQLEEQLEQEAKERAAANKLVRRTEKKLKEV 1885
Cdd:pfam05622 373 EAQEELQ-----KKKEQLEELEPkvdsnlqKIDELQEALRKKDEDMKAMEERYKKYVEKAKSV 430
|
|
| NtpI |
COG1269 |
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion]; |
882-1162 |
2.54e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit I/STV1 [Energy production and conversion];
Pssm-ID: 224188 [Multi-domain] Cd Length: 660 Bit Score: 42.73 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEK----QTKVEAELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlaaKKQELEEILHD 957
Cdd:COG1269 38 EGEKGLKELEKLKVAEVaqisLSSLLSEVLDYLRSVKGLEGRLFILPEEVEKLEAELKSLEE-------VIKPAEKFSSE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 958 LESRVEEEEERNQILQNEKKKMQGHIqdleeqldeeegarqkLQLEKV----TAEAKIKKMEEEILLLEDQNSKFLKEKK 1033
Cdd:COG1269 111 VEELTRKLEERLSELDEELEDLEDLL----------------EELEPLayldFDLSLLRGLKFLLVRLGLVRREKLEALV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1034 LMEDRIAEctsqLAEEEEKAKNlaklknkqEMMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELK 1113
Cdd:COG1269 175 GVIEDEVA----LYGENVEASV--------VIVVAHGAEDLDKVSKILNELGFELYEVPEFDGGPSELISELEEVIAEIQ 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 45382679 1114 IQLAKKEEELQAALARGDEEAVQKNNALkvirELQAQIAELQEDLESEK 1162
Cdd:COG1269 243 DELESLRSELEALAEKIAEELLAVREIL----EIEKALGDVLSKLARTE 287
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
996-1299 |
2.56e-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: 42.59 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 996 ARQKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEE-EKAKNLAKLKNK--QEMMITDLEE 1072
Cdd:pfam15964 390 LRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEmDVTKVCGEMRYQlnQTKMKKDEAE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1073 RLKKEEKTR---------QELEKAKRKLDGETTDL-QDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQK---NN 1139
Cdd:pfam15964 470 KEHREYRTKtgrqleikdQEIEKLGLELSESKQRLeQAQQDAARAREECLKLTELLGESEHQLHLTRLEKESIQQsfsNE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1140 ALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-QELRTKREQEVAELkkaiEEET 1218
Cdd:pfam15964 550 AKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKlEEITQKSRSEVEQL----SQEK 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1219 KNHEAQIQEIRQRHatalEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELTAK 1298
Cdd:pfam15964 626 EYLQDRLEKLQKRN----EELEEQCVQHGRMHERMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
.
gi 45382679 1299 V 1299
Cdd:pfam15964 702 V 702
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
883-980 |
2.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 883 EELQAKDEEL-MKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQaetELFAEAE-EMRARLAAKKQELEEIL----- 955
Cdd:PRK00409 519 NELIASLEELeRELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED---KLLEEAEkEAQQAIKEAKKEADEIIkelrq 595
|
90 100 110
....*....|....*....|....*....|....*.
gi 45382679 956 -----------HDLESRVEEEEERNQILQNEKKKMQ 980
Cdd:PRK00409 596 lqkggyasvkaHELIEARKRLNKANEKKEKKKKKQK 631
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1668-1914 |
2.82e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1668 NKARDEAIKQLRKLQA-QMKDYQRELEEARASR--------DEIFAQSKESEKKLKGLEAEILQLqeEFAASERARRHAE 1738
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEELSNERLRKlrslltklSEALDKLRSYLPKLNPLREEKKKV--SVKSLEELIKDVE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1739 QERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEeqsNMELLNERFRKTTLQ-VDTLNSELAGERSAAQKSENA 1817
Cdd:PRK05771 93 EELEKIEKEIKELEEEISELENEIKELEQEIERLEPWGNF---DLDLSLLLGFKYVSVfVGTVPEDKLEELKLESDVENV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1818 -----------------RQQLERQNKELK-AKLQELEGSVKSKFKATISTLEAKIAQLEEQLEqeakeraaanklvrRTE 1879
Cdd:PRK05771 170 eyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------------SLL 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 45382679 1880 KKLKEVFMQVEDERRHADQYKEQM-EKANARMKQLK 1914
Cdd:PRK05771 236 EELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1448-1651 |
3.27e-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: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1448 KLEKTKNRLQQELDDLmvdLDHqrqiVSNLEKKQKKFDQmLAEEKNISAryaeERDRAEAEAREKETKALSLARALEEAL 1527
Cdd:NF012221 1566 RAEADRQRLEQEKQQQ---LAA----ISGSQSQLESTDQ-NALETNGQA----QRDAILEESRAVTKELTTLAQGLDALD 1633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1528 EAKEEFERQNKQLRAD-----MEDLMSSKDDVGKNVHE-LEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQ 1601
Cdd:NF012221 1634 SQATYAGESGDQWRNPfagglLDRVQEQLDDAKKISGKqLADAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDID 1713
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45382679 1602 AMKAQFE-RDLQARDEQNEEKKRmlvKQVRELEAELEDERKQRALAVAAKK 1651
Cdd:NF012221 1714 DAKADAEkRKDDALAKQNEAQQA---ESDANAAANDAQSRGEQDASAAENK 1761
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
912-1164 |
3.30e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 223571 [Multi-domain] Cd Length: 557 Bit Score: 42.20 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 912 KHQQLL----EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERN-QI-----LQNEKKKMQG 981
Cdd:COG0497 140 LQRQLLdafaGLEELAQEAYQEAYQAWKQARRELEDLQEKERERAQRADLLQFQLEELEELNlQPgedeeLEEERKRLSN 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 982 HiqdlEEQLDEEEGARQKLQLE--KVTAEAKIKKMEEEILLLEDQNSKFlkekKLMEDRIAECTSQLAEEEEKAKNLAKL 1059
Cdd:COG0497 220 S----EKLAEAIQNALELLSGEddTVSALSLLGRALEALEDLSEYDGKL----SELAELLEEALYELEEASEELRAYLDE 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1060 KNKQEMMITDLEERLkkeektrQELEKAKRKLDGETTDLQDQIAELQAQIEELKiQLAKKEEELQAALARGDEEAVQKNN 1139
Cdd:COG0497 292 LEFDPNRLEEVEERL-------FALKSLARKYGVTIEDLLEYLDKIKEELAQLD-NSEESLEALEKEVKKLKAELLEAAE 363
|
250 260 270
....*....|....*....|....*....|.
gi 45382679 1140 ALKVIR-----ELQAQI-AELQEdLESEKAS 1164
Cdd:COG0497 364 ALSAIRkkaakELEKEVtAELKA-LAMEKAR 393
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1067-1183 |
3.32e-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: 41.93 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1067 ITDLEERLKKEEKTRQELEKAKRKLD-GETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlargdEEAVQKNNALKviR 1145
Cdd:smart00787 177 LRDRKDALEEELRQLKQLEDELEDCDpTELDRAKEKLKKLLQEIMIKVKKLEELEEELQEL-----ESKIEDLTNKK--S 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 45382679 1146 ELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALK 1183
Cdd:smart00787 250 ELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
997-1213 |
3.39e-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: 380155 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 997 RQKLQLEKVTAEAKIKKMEEEillLE--DQNskflkekKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERL 1074
Cdd:NF012221 1571 RQRLEQEKQQQLAAISGSQSQ---LEstDQN-------ALETNGQAQRDAILEESRAVTKELTTLAQGLDALDSQATYAG 1640
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1075 KKEEKTRQELekAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARgDEEAVQKNnalkvirelQAQIAEL 1154
Cdd:NF012221 1641 ESGDQWRNPF--AGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAK-SEAGVAQG---------EQNQANA 1708
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1155 QEDLESekaSRNKAEKQKRD-LSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKA 1213
Cdd:NF012221 1709 EQDIDD---AKADAEKRKDDaLAKQNEAQQAESDANAAANDAQS--RGEQDASAAENKAN 1763
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1076-1183 |
3.39e-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: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1076 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALAR--GDEEAVQK-------NNALKVIRE 1146
Cdd:cd22656 104 ADATDDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAleTLEKALKDlltdeggAIARKEIKD 183
|
90 100 110
....*....|....*....|....*....|....*...
gi 45382679 1147 LQAQIAELQEDLESE-KASRNKAEKQKRDLSEELEALK 1183
Cdd:cd22656 184 LQKELEKLNEEYAAKlKAKIDELKALIADDEAKLAAAL 221
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1551-1686 |
3.58e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1551 KDDVGKNVHELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVR 1630
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1631 ELEAELEDERKQRALAVAAKkkmemDLKDLEGQIEAANKARDEAIKQLRKLQAQMK 1686
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1422-1653 |
3.66e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227278 [Multi-domain] Cd Length: 420 Bit Score: 42.02 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1422 EENKKKLLKDMESLSQRLEEKAMAYDKLEKTKNRLQQELDDLmvdlDHQ-RQIVSNLEKKQKKFDQMLAEEKNISARYAE 1500
Cdd:COG4942 37 DKQLKQIQKEIAALEKKIREQQDQRAKLEKQLKSLETEIASL----EAQlIETADDLKKLRKQIADLNARLNALEVQERE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1501 ERDRAEA---------------------EAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVH 1559
Cdd:COG4942 113 QRRRLAEqlaalqrsgrnpppallvspeDAQRSVRLAIYYGALNPARAERIDALKATLKQLAAVRAEIAAEQAELTTLLS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1560 ELEKSKRTLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKKRMLVKQVRELEAELEDE 1639
Cdd:COG4942 193 EQRAQQAKLAQLLEERKKTLAQLNSELSADQKKLEELRANESRLKNEIASAEAAAAKAREAAAAAEAAAARARAAEAKRT 272
|
250
....*....|....
gi 45382679 1640 RKQRALAVAAKKKM 1653
Cdd:COG4942 273 GETYKPTAPEKMLI 286
|
|
| TolA |
COG3064 |
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1008-1195 |
3.81e-03 |
|
Membrane protein involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 225606 [Multi-domain] Cd Length: 387 Bit Score: 41.86 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1008 EAKIKKMEEEILLLEDQNSKFLKEKKLME-DRIAECTSQLAEEEEKAKN---LAKLKNKQEMMITDLEERLKKEEKTRQE 1083
Cdd:COG3064 71 QSSAKKGEQQRKKKEEQVAEELKPKQAAEqERLKQLEKERLKAQEQQKQaeeAEKQAQLEQKQQEEQARKAAAEQKKKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1084 LEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAAlARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKA 1163
Cdd:COG3064 151 AAKAKAAAEAAKLKAAAEAKKKAEEAAKAAEEAKAKAEAAAAK-KKAEAEAKAAAEKAKAEAEAKAKAEKKAEAAAEEKA 229
|
170 180 190
....*....|....*....|....*....|..
gi 45382679 1164 SRNKAEKQKRDLSEELEALKTELEDTLDTTAA 1195
Cdd:COG3064 230 AAEKKKAAAKAKADKAAAAAKAAERKAAAAAL 261
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1172-1339 |
3.81e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1172 KRDLSEELEALKTELEDTLDttAAQQELRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKA 1251
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILE--EAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1252 NLEKNKQGLESDNKELACEVKVLQQVKAESEHKRKKLDAQVQELT------AKVTEGERLRVELAEKANKLQNELDnvss 1325
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISgltaeeAKEILLEKVEEEARHEAAVLIKEIE---- 179
|
170
....*....|....
gi 45382679 1326 llEEAEKKGIKFAK 1339
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 ... |
1661-1762 |
3.81e-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: 39.34 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1661 EGQIEAANKARDEAIKQLrklqaqmKDYQRELEEARASRDEIFAQSKESEKKLKglEAEILQLQEEFAAS-ERARRHAEQ 1739
Cdd:cd06503 36 AESLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEIIEEARKEAEKIK--EEILAEAKEEAERIlEQAKAEIEQ 106
|
90 100
....*....|....*....|...
gi 45382679 1740 ERDELADEIANSASGKSALLDEK 1762
Cdd:cd06503 107 EKEKALAELRKEVADLAVEAAEK 129
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1391-1758 |
4.05e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 227608 [Multi-domain] Cd Length: 1213 Bit Score: 42.22 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1391 KNLEKQMLALQAQLAEAKKKVDDDLGTIEGLEENKKKLLKDMESLSQRLEEKAMAYDKLEKTknrlQQELDDLMVDLDHQ 1470
Cdd:COG5283 32 KDSTQFWKMLEKQQKLTKDGLSASKGKYEGLSEAMEKQKKAYEDLKQEVKEVNRATQASKKA----YQEYNAQYTQAENK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1471 RQIVS-------NLEKKQKKFDQMLAEEKNISARYAEERDRAEAEAREKETKALSlaraleEALEAKEEFERQNKQLRAD 1543
Cdd:COG5283 108 LRSLSgqfgvasEQLMLQQKEIQRLQYAISTLNKSMAAQARLLEQTGNKFGTADA------KVVGLRESFGRQTEALNKQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1544 MEDLMSSKDDVGKNvheLEKSKRTLEQQVEEMRTQLEELEDELQATEDAK-LRLEVNMQAMKAQfeRDLQARDEQNEEKK 1622
Cdd:COG5283 182 LERTKKVADALTYV---LDEAQQKLSQALSARLERLQESRTQMSQSSGQLgKRLETDKAGAGAL--GLLGAALAGSFAAI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1623 RMLVKQVRELEAELEDERKQRALAVAAKKKMEMDLKDLEGQIEaankardeaikqlrKLQAQMKDYQRELEEARASRdEI 1702
Cdd:COG5283 257 GAAVRRTAQMNGELMDKTKQVKGARDNLGKVTSQGEEMSDAIQ--------------ETAEHIKDSGRELSKAAAIG-AA 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45382679 1703 FAQSKESEKKLKGLEAeILQLQEEFAASERARRHAEQERDELADEIA-----------NSASGKSAL 1758
Cdd:COG5283 322 AAMGVAAGKFPTGQEA-KPTLKEMARVAALTATAFNLPADELNDNLAkwagelkfpasDAISGGSLL 387
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1674-1917 |
4.22e-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: 41.24 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1674 AIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEE-----------FAASERARRHAEqerd 1742
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtlakaqqvNAESERTLGHAK---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1743 ELADEIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNERFRKTTLQVDTLnselagERSAAQKSENa 1817
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEA------ELKAAQDLLS- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1818 rqQLERQNKELKAKLQELEGSVKSKfkatISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEDERRHAD 1897
Cdd:pfam06008 159 --RIQTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKN 232
|
250 260
....*....|....*....|
gi 45382679 1898 QYKEQMEKANARMKQLKRQL 1917
Cdd:pfam06008 233 QLEETLKTARDSLDAANLLL 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1498-1747 |
4.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 41.21 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1498 YAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRTLeqqvEEMRT 1577
Cdd:COG1340 39 LAEKRDELNAKVRELREKAQELREERDEINEEVQELKEKRDEINAKLQELRKEYRELKEKRNEFNLGGRSI----KSLER 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1578 QLEELEdELQATEDAKLRLEVNMQAMKAQFERDLQARDEQNEEKkrmlvKQVRELEAELEDERKQRalavaakKKMEMDL 1657
Cdd:COG1340 115 EIERLE-KKQQTSVLTPEEERELVQKIKELRKELEDAKKALEEN-----EKLKELKAEIDELKKKA-------REIHEKI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1658 KDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQ-EEFAASERARRH 1736
Cdd:COG1340 182 QELANEAQEYHEEMIKLFEEADELRKEADELHEEFVELSKKIDELHEEFRNLQNELRELEKKIKALRaKEKAAKRREKRE 261
|
250
....*....|.
gi 45382679 1737 AEQERDELADE 1747
Cdd:COG1340 262 ELKERAEEIYE 272
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1556-1955 |
5.05e-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.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1556 KNVHELEKSKRTLEQQVEEMRTQLEELEDElqateDAKLRLEVNmQAMK--AQFERDLQARDEQNEEKKRMLVKQVRELE 1633
Cdd:pfam06160 86 KALDEIEELLDDIEEDIKQILEELDELLES-----EEKNREEVE-ELKDkyRELRKTLLANRFSYGPAIDELEKQLAEIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1634 AELE--DERKQRALAVAAKK---KMEMDLKDLEGQIEAA----NKARDEAIKQLRKLQA---QMKDYQRELEEarasrDE 1701
Cdd:pfam06160 160 EEFSqfEELTESGDYLEAREvleKLEEETDALEELMEDIpplyEELKTELPDQLEELKEgyrEMEEEGYALEH-----LN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1702 IFAQSKESEKKLKGLEAEILQLqeEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1781
Cdd:pfam06160 235 VDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKE 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1782 NMELLNERFrkttlqvdTLNselAGERSAAQKSENARQQLERQNKELKAKLQELEG---SVKSKFK---ATISTLEAKIA 1855
Cdd:pfam06160 313 ELERVQQSY--------TLN---ENELERVRGLEKQLEELEKRYDEIVERLEEKEVaysELQEELEeilEQLEEIEEEQE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1856 QLEEQLEQEAKERAAANKLVRRTEKKLKEVFMQVEdeRRH----ADQYKEQMEKANARMKQLKRQLeeaeeeatraNASR 1931
Cdd:pfam06160 382 EFKESLQSLRKDELEAREKLDEFKLELREIKRLVE--KSNlpglPESYLDYFFDVSDEIEDLADEL----------NEVP 449
|
410 420
....*....|....*....|....*..
gi 45382679 1932 ---RKLQRELDDATEANEGLSREVSTL 1955
Cdd:pfam06160 450 lnmDEVNRLLDEAQDDVDTLYEKTEEL 476
|
|
| EVC2_like |
pfam12297 |
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. ... |
1575-1836 |
5.30e-03 |
|
Ellis van Creveld protein 2 like protein; This family of proteins is found in eukaryotes. Proteins in this family are typically between 571 and 1310 amino acids in length. There are two conserved sequence motifs: LPA and ELH. EVC2 is implicated in Ellis van Creveld chondrodysplastic dwarfism in humans. Mutations in this protein can give rise to this congenital condition. LIMBIN is a protein which shares around 80% sequence homology with EVC2 and it is implicated in a similar condition in bovine chondrodysplastic dwarfism.
Pssm-ID: 432462 [Multi-domain] Cd Length: 429 Bit Score: 41.58 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1575 MRTQLEELEDELQATEDAKLRlEVNMQAMK---AQFERDLQARDEQNEE-KKRMLV---KQVRELEAELEDERKQRALAV 1647
Cdd:pfam12297 145 MYQALENLEIATLIRADADLE-ACRIQIMKdiiAMLLGNLTSRGHLSPQaEKRLSSvfnKQFLAMEGRLQEEYGRKMAAL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1648 AAKKKMEMDlKDLEGQIEAANKARDEAIKQLRKLQaqmkdyQRELEEARASRDEIFAQSKESEKKLKGL--EAEILQLQE 1725
Cdd:pfam12297 224 AAECNLETR-EKMEAQHQKEMAEKEEAEELLQHAS------EQEALECSSLLDKLHKLEQEHLQRSLLLkqEEEFAKARR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1726 EFAASERARRHAEQ--------ERDELADEIANS--------ASGKSALLDE-----KRRLEARIAQLEEELEEEQSNME 1784
Cdd:pfam12297 297 QLAVKRRVELHKIFfeqlkeatRKGELKEEAAKRllhdyskiQDTIEELMDFfqanqRYHLEERFAQREYLVKSLQSLET 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 45382679 1785 LLNERFRKTTLQVDTLNSELagERSAAQKSENARQQLERQNKELKAKLQELE 1836
Cdd:pfam12297 377 HISALLNTAATQLTSLIQKL--ERAGYLDEEQMEMLLERAQKEVLSVKQKLD 426
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1094-1173 |
5.50e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1094 ETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKR 1173
Cdd:PRK11448 136 PPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1065-1340 |
5.78e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 224259 [Multi-domain] Cd Length: 294 Bit Score: 40.82 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1065 MMITDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVI 1144
Cdd:COG1340 6 DKLDELELKRKQLKEEIEELKEKRDELRKEASELAEKRDELNAKVRELREKAQELREERDEINEEVQELKEKRDEINAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1145 RELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ-EVAELKKAIEEETKNHEA 1223
Cdd:COG1340 86 QELRKEYRELKEKRNEFNLGGRSIKSLEREIERLEKKQQTSVLTPEEERELVQKIKELRKElEDAKKALEENEKLKELKA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1224 QIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQglesdnkelacevkvlqqvkaESEHKRKKLDAQVQELTAKVTEGE 1303
Cdd:COG1340 166 EIDELKKKAREIHEKIQELANEAQEYHEEMIKLFE---------------------EADELRKEADELHEEFVELSKKID 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 45382679 1304 RLRVELAEKANKLqNELDNVSSLLEEAEKKGIKFAKD 1340
Cdd:COG1340 225 ELHEEFRNLQNEL-RELEKKIKALRAKEKAAKRREKR 260
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
882-1169 |
5.82e-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 characteristic 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: 41.21 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 882 EEELQAKDEELMKVKEKQTKVEAELEEMERKHQQL---LEEKNILAEQLqaETELFAEAEEMRA------RLAAKKQELE 952
Cdd:pfam19220 75 TRRLSAAEGELEELVARLAKLEAALREAEAAKEELrieLRDKTAQAEAL--ERQLAAETEQNRAleeenkALREEAQAAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 953 EILHDLESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEIL-----------LL 1021
Cdd:pfam19220 153 KALQRAEGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAaeqaereraeaQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1022 EDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKEEKTRQELEkakRKLDGETTDLQDQ 1101
Cdd:pfam19220 233 EEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLE---RRLAGLEADLERR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1102 IAELQaQIEELKIQLAKKEEELQAALARGD---EEAVQKNNAL------------KVIRELQAQIAELQEDLESEKASRN 1166
Cdd:pfam19220 310 TQQFQ-EMQRARAELEERAEMLTKALAAKDaalERAEERIASLsdriaeltkrfeVERAALEQANRRLKEELQRERAERA 388
|
...
gi 45382679 1167 KAE 1169
Cdd:pfam19220 389 LAQ 391
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
1013-1188 |
5.84e-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: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1013 KMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEE-----EKAKNLAKLKNK-QEMMITDLEErlkKEEKTRQELEk 1086
Cdd:COG5192 525 KSSESDLVVQDEPEDFFDVSKVANESISSNHEKLMESEfeelkKKWSSLAQLKSRfQKDATLDSIE---GEEELIQDDE- 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1087 akrklDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAvQKNNALKviRELQAQIaELQEDLESEKASRN 1166
Cdd:COG5192 601 -----KGNFEDLEDEENSSDNEMEESRGSSVTAENEESADEVDYETER-EENARKK--EELRGNF-ELEERGDPEKKDVD 671
|
170 180
....*....|....*....|..
gi 45382679 1167 KAEKQKRDLSEELEALKTELED 1188
Cdd:COG5192 672 WYTEEKRKIEEQLKINRSEFET 693
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1121-1278 |
5.94e-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: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1121 EELQAALARGDEEAVQ--KNNALKVIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaqqE 1198
Cdd:cd22656 98 ELIDDLADATDDEELEeaKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTD-----E 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1199 LRTKREQEVAELKKAIEEETKNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKELACEVKVLQQVK 1278
Cdd:cd22656 173 GGAIARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPALEKLQ 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1006-1231 |
5.96e-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: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1006 TAEAKIKKMEEEILLLEDQNSKFLKEKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQEmmitdlEERLKKEEKTRQELE 1085
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAE------EKQKQAEEAKAKQAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1086 KAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKEEELQAALARGDEEAVQKNNALKVIRELQAQIAELQEDLESEKASR 1165
Cdd:TIGR02794 131 EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45382679 1166 NKAEKQKRdLSEELEALKTELEDTLDTTAAQQELRTKREQEVAElKKAIEEETKNHEAQIQEIRQR 1231
Cdd:TIGR02794 211 AKAEAEAA-AAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR-GAAAGSEVDKYAAIIQQAIQQ 274
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
884-1182 |
6.52e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 41.80 E-value: 6.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 884 ELQAKDEELMKVKEKQTKVEAELEE-------MERKHQQLLEEKNILAEQLQAEtELFAEAEEMRARLAAKKQELEEILH 956
Cdd:COG3096 294 ELYTSRQQLAAEQYRHVDMSRELAElngaegdLEADYQAASDHLNLVQTALRQQ-EKIERYQADLEELTIRLEEQNEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 957 DLESRVEEEEERNQILQNEKKKM--------------QGHIQDLEEQLDEEEGARQKLQLEKVTAE----------AKIK 1012
Cdd:COG3096 373 EANERQEENEARAEAAELEVDELksqladyqqaldvqQTRAIQYQQAIAALERAKELCHLPDLTADsaeewletfqAKEE 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1013 KMEEEILLLEDQ-------NSKFLKEKKLM--------EDRIAECTSQLAEEEEKAKNLAKLKNKQEMMITDLEERLKKE 1077
Cdd:COG3096 453 EATEKLLSLEQKmsmaqaaHSQFEQAYQLVvaiagelaRSEAWDVARELLREGPDQRHLAEQVQPLRMRLSELEQRLRQQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1078 EKTRQEL----EKAKRKLDGETtdLQDQIAELQAQIEEL----------KIQLAKKEEELQAALARGDEEA---VQKNNA 1140
Cdd:COG3096 533 QSAERLLadfcKRQGKNLDAEE--LEALHQELEALIESLsdsvsnareqRMALRQEQEQLQSRIQSLMQRApvwLAAQNA 610
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1141 LKVIREL--------QAQIAELQEDLESEKA---SRNKAEKQKRDLSEELEAL 1182
Cdd:COG3096 611 LEQLSEQsgeeftdsQDVTEYMQQLLEREREatvERDELGARKNALDEEIERL 663
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
877-1017 |
6.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 877 QVTRQEEELQAKDEelmkVKEKQTKVEAELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 952
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45382679 953 EILHDLEsrveeeeernQILQNEKKKMQgHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEE 1017
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEE 181
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
891-1373 |
6.75e-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: 428520 [Multi-domain] Cd Length: 660 Bit Score: 41.25 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 891 ELMKVKEKQTKVEAELEEMERKHQqllEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQ 970
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHK---RARIELERKASALARQLERESDRNQELQKRIRLLEKREAEAEEALREQAELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 971 ILqneKKKMQGHIQDLEEQLDEEEGARQ-KLQLEKVTAEAKIKKMEEEILLLEDQNSKF-LKEKKLMEDRIAECTSQLAE 1048
Cdd:pfam05557 80 LK---KKNLEALNKKLNEKESQLADAREvISCLKNELSELRRQIQRQELELSSTNSELEeLQERLDLQKAKAQEAEQLRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1049 EEEKAKNLAKLKNKQemmITDLEERLKKEEKTRQELEKAKRKLdGETTDLQDQIAELQAQIEEL------KIQLAKKEEE 1122
Cdd:pfam05557 157 NLEAQQSSLAEAEQR---IKELEFEIQSQEQDSEIVKNSKSEL-ARIPELERELERLREHNKHLnenienKLLLKEEVED 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1123 LQAALARgdeeavqknnalkvIRELQAQIAELQEDLESEKASRNKAEKQKRDLSEEL---EALKTELEDTLDTTAAQQEL 1199
Cdd:pfam05557 233 LKRKLER--------------EEGYREELATLELEKEKLEQELKSWEKLAQDTGLNLrspEDLSRRIEQLQQREITLKEE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1200 RTKREQEVAELKKAI---EEETKNHEAQIQEIRQRhataLEELSEQLE--QAKRFKANLEKN--KQGLESDNKELACE-- 1270
Cdd:pfam05557 299 NSSLTSSARQLEKAQrelEQELAQYLKNIEDLNKK----LKRHKALVRrlQRRVLLLTKERDgmRAILESYDKELTPSny 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1271 -----------VKVLQQVKAESEHKRKKLDAQVQELTAKVTEGERLRVELaeKANKLQNELDNVSSLLEEAEkkgikfak 1339
Cdd:pfam05557 375 spqllerieeaEDMTQDMQAHNEEMEAQLSVAEEELGGYKQQATTLEREL--QALRQQESLADPSYSKEEVD-------- 444
|
490 500 510
....*....|....*....|....*....|....
gi 45382679 1340 daaSLESQLQDTQELLQEETRQKLNLSSRIRQLE 1373
Cdd:pfam05557 445 ---SLRRKLETLEAERQRLREQKNELEMELERRC 475
|
|
| PrfA |
COG0216 |
Protein chain release factor A [Translation, ribosomal structure and biogenesis]; |
1032-1149 |
7.37e-03 |
|
Protein chain release factor A [Translation, ribosomal structure and biogenesis];
Pssm-ID: 223294 [Multi-domain] Cd Length: 363 Bit Score: 40.66 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1032 KKLMEDRIAECTSQLAEEEEK------AKNLAKLK--NKQEMMITDLEERLKKEEKTRQELEKAKRKLDGETtdLQDQIA 1103
Cdd:COG0216 2 KPSLLEKLESLLERYEELEALlsdpevISDPDEYRklSKEYAELEPIVEKYREYKKAQEDLEDAKEMLAEEK--DPEMRE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 45382679 1104 ELQAQIEELKIQLAKKEEELQAALARGDEeavqkNNALKVIRELQA 1149
Cdd:COG0216 80 MAEEEIKELEAKIEELEEELKILLLPKDP-----NDDKNIILEIRA 120
|
|
| COG4913 |
COG4913 |
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown]; |
834-1120 |
7.53e-03 |
|
Uncharacterized protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 227250 [Multi-domain] Cd Length: 1104 Bit Score: 41.55 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 834 RKAFAKKQQQLSALKILQRncaaylklRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKH 913
Cdd:COG4913 643 QGEYIKLQEQANALAHIQA--------LNFASIDLPSAQRQIAELQARLERLTHTQSDIAIAKAALDAAQTRQKVLERQY 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 914 QQLLEEKNILAEQLQAetelfAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQghiqdleeqldee 993
Cdd:COG4913 715 QQEVTECAGLKKDLKR-----AAMLSRKVHSIAKQGMTGALQALGAAHFPQVAPEQHDDIVDIERIE------------- 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 994 egARQKLQLEKVTAEAKIKKMEEEILlledqnskflkekKLMEDRIAECTSQLAEEEekaKNLAKLKNKQEMMITDLEER 1073
Cdd:COG4913 777 --HRRQLQKRIDAVNARLRRLREEII-------------GRMSDAKKEDTAALSEVG---AELDDIPEYLARLQTLTEDA 838
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 45382679 1074 LKKEEKTRQEL--EKAKRKLDGETTDLQDQIAELQAQIEELKIQLAKKE 1120
Cdd:COG4913 839 LPEFLARFQELlnRSSDDGVTQLLSHLDHERALIEERIEAINDSLRRVD 887
|
|
| HlyD |
pfam00529 |
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin ... |
1623-1765 |
7.60e-03 |
|
HlyD membrane-fusion protein of T1SS; HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD and HlyB are inner-membrane proteins and specific components of the transport apparatus of alpha-haemolysin. 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: 7.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1623 RMLVKQVRELEAELEDERKQRALAVAAKKKMEMdlkdLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEAR------ 1696
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarr 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45382679 1697 ---ASRDEIFAQSKESEKKL-KGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRL 1765
Cdd:pfam00529 130 rvlAPIGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| ERM |
pfam00769 |
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at ... |
1671-1771 |
7.68e-03 |
|
Ezrin/radixin/moesin family; This family of proteins contain a band 4.1 domain (pfam00373), at their amino terminus. This family represents the rest of these proteins.
Pssm-ID: 425860 [Multi-domain] Cd Length: 247 Bit Score: 40.31 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1671 RDEAIKQLRKLQAQMKDYQRELEEARasrdeifAQSKESEKKLKGLEAEILQLQEEFAASERARRHAEQERDELADEIAN 1750
Cdd:pfam00769 1 REEAEREKQELEERLKQYEEETRKAQ-------EELEESEETAELLEEKLRVAEEEAELLEQKAQEAEEEKERLEESAEM 73
|
90 100
....*....|....*....|.
gi 45382679 1751 SASGKSALLDEKRRLEARIAQ 1771
Cdd:pfam00769 74 EAEEKEQLERELREAQEEVAR 94
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ... |
883-1480 |
7.85e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 225638 [Multi-domain] Cd Length: 1480 Bit Score: 41.41 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 883 EELQAKDEE----LMKVKEKQTKVEAELEEMERKHQQLleeKNILAEQLQAET-----ELFAEAEEMRaRLAAKKQELEE 953
Cdd:COG3096 445 ETFQAKEEEatekLLSLEQKMSMAQAAHSQFEQAYQLV---VAIAGELARSEAwdvarELLREGPDQR-HLAEQVQPLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 954 ILHDLESRVEEEEERNQILQNEKKKmqgHIQDLEEQLDEEEGARQKLQLEKVTAEAKiKKMEEEILLLEDQNSKFLKEKK 1033
Cdd:COG3096 521 RLSELEQRLRQQQSAERLLADFCKR---QGKNLDAEELEALHQELEALIESLSDSVS-NAREQRMALRQEQEQLQSRIQS 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1034 LMEDRIAECTSQLAEEEEKAKNLAKLKNKQEMMiTDLEERLKKEEKT---RQELEKAKRKLDGETTDL------QDQIAE 1104
Cdd:COG3096 597 LMQRAPVWLAAQNALEQLSEQSGEEFTDSQDVT-EYMQQLLEREREAtveRDELGARKNALDEEIERLsqpggsEDQRLN 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1105 LQAQ------IEELKIQLAKKEEELQAALARGDEEAVQKNNaLKVIRELQAQIAELQEDL------------------ES 1160
Cdd:COG3096 676 ALAErfggvlLSEIYDDVTIEDAPYFSALYGPSRHAIVVPD-LSQVKEHLEGLTDCPEDLyliegdpqsfddsvfsvdEL 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1161 EKASRNK-AEKQKR-------------DLSEELEALKTELEDTLDTTAAQ-------QELRTKREQEVA-ELKKAIEeet 1218
Cdd:COG3096 755 EKAVVVKiADRQWRysrfpeiplfgraAREQRLESLHAERDVLSERHATLsfdvqktQRLHQAFSRFIGsHLAVAFE--- 831
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1219 KNHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQGLESDNKeLACEVKVL--QQVKAESEHKRKKLDaQVQELT 1296
Cdd:COG3096 832 ADPEAEIRQLNSRRNELERALSNHENDNQQQRIQFDQAKEGVTALNR-LIPQLNLLadESLADRVEEIRERLD-EAQEAA 909
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1297 AKVTEGERLRVELAEKANKLQNELDNVSSL---LEEAEKKGIKFAKDAASLESQLQDTQELLQEETRQKLNLSSRIRqlE 1373
Cdd:COG3096 910 RFIQQHGNTLSKLEPIASVLQSDPEQFEQLkedYAQAQQMQRQARQQAFALTEVVQRRAHFSYSDSAEMLSENSDLN--E 987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1374 EEKNNLQEQQEEEEEARKNLEKQmlalQAQLAEAKKKvdddLGTIEGLEENKKKLLKDmesLSQRLEEKAMAYDklEKTK 1453
Cdd:COG3096 988 KLRQRLEQAEAERTRAREQLRQH----QAQLSQYNQV----LASLKSSYDTKKELLNE---LQQELQDIGVRAD--SGAE 1054
|
650 660
....*....|....*....|....*..
gi 45382679 1454 NRLQQELDDLMVDLDHQRQIVSNLEKK 1480
Cdd:COG3096 1055 ERARIRRDELHAQLSTNRSRRNQLEKQ 1081
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1070-1258 |
7.99e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 224755 [Multi-domain] Cd Length: 225 Bit Score: 39.99 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1070 LEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE---LQAQIEELKIQLAKKEEELQAALARGDEEAVQKnnALKVIRE 1146
Cdd:COG1842 19 LDKAEDPEKMLEQAIRDMESELAKARQALAQAIARqkqLERKLEEAQARAEKLEEKAELALQAGNEDLARE--ALEEKQS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1147 LQAQIAELQEDLESEKASRNKAEKQKRDLS---EELEALKTELEDTLDTTAAQQELRTKR----EQEVAELKKAIEEETK 1219
Cdd:COG1842 97 LEDLAKALEAELQQAEEQVEKLKKQLAALEqkiAELRAKKEALKARKAAAKAQEKVNRSLgggsSSSAMAAFERMEEKIE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 45382679 1220 NHEAQIQEIRQRHATALEELSEQLEQAKRFKANLEKNKQ 1258
Cdd:COG1842 177 EREARAEAAAELAEGSGDDLDKEFAQAGAQSAVDSRLAA 215
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1650-1880 |
8.84e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1650 KKKMEMDLKDLEGqieAANKARDEAIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE-----SE 1710
Cdd:PRK10929 25 EKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEprsvpPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1711 KKLKGLEAEILQLQEEFAasERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEEQSNMEL 1785
Cdd:PRK10929 102 MSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1786 LNERFRKTTLQVDTLnsELAgersaaQKSENARQQLERQNKEL-KAKLQELEGSvkskfkatistLEAKIAQLEEQLEQE 1864
Cdd:PRK10929 178 LQAESAALKALVDEL--ELA------QLSANNRQELARLRSELaKKRSQQLDAY-----------LQALRNQLNSQRQRE 238
|
250
....*....|....*.
gi 45382679 1865 AkERAaanklVRRTEK 1880
Cdd:PRK10929 239 A-ERA-----LESTEL 248
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1632-1960 |
9.16e-03 |
|
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: 429718 [Multi-domain] Cd Length: 488 Bit Score: 40.64 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1632 LEAELEDERKQRALAVaakKKMEMDLKDLEGQIEAANKARDEAIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEK 1711
Cdd:pfam07888 32 LQNRLEECLQERAELL---QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKVEEL-------EE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1712 KLKGLEAEILQLQEEFAASERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNERFR 1791
Cdd:pfam07888 102 KYKELSRSGEELAEEKDALLAQRAESEARIRELEEDIKTLTQRVLERETELERMKERVKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1792 KTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLqelegsvkskfkatiSTLEAKIAQLEEQLEQ--EAKERA 1869
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---------------TTAHRKEAENEALLEElrSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1870 AANKlvrRTEKKLKEVF--MQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANaSRRKLQRELDDATEANEG 1947
Cdd:pfam07888 247 NASE---RKVEGLGEELssMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQ-ERETLQQSAEADKDRIEK 322
|
330
....*....|...
gi 45382679 1948 LSREVSTLKNRLR 1960
Cdd:pfam07888 323 LSAELQRLEERLQ 335
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1700-1961 |
9.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1700 DEIFAQSKESEKKLKgleaEILQLQEEFAASERA---RRHAEQERDELADEIANSASGKSALLDEKRRLEA------RIA 1770
Cdd:PRK03918 138 DAILESDESREKVVR----QILGLDDYENAYKNLgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlreinEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1771 QLEEELEEEQSNMELLNERFRKTTLQVDTLNSELAGERSAAQKSENARQQLERQNKELKAKLQELEGSVK---------- 1840
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkelkekae 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1841 ---------SKFKATISTLEAKIAQLEEQLEQEAKERAAANKLVRRTEkKLKEVFMQVEDERRHADQYKEQMEKANARMK 1911
Cdd:PRK03918 294 eyiklsefyEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKE 372
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 45382679 1912 QLKRqleeaeEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:PRK03918 373 ELER------LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1663-1765 |
9.59e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1663 QIEAANKARDEAIKQLRKLQAQMKD-YQRELEEARASRDEIFAQSKESEKKLKGLEAEILQLQEEFAASERARRhaeQER 1741
Cdd:PRK11448 142 NLLHALQQEVLTLKQQLELQAREKAqSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK---QKR 218
|
90 100
....*....|....*....|....*.
gi 45382679 1742 DELADEIAnsasgKSALLDEK--RRL 1765
Cdd:PRK11448 219 KEITDQAA-----KRLELSEEetRIL 239
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
874-1132 |
9.59e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 40.70 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 874 PLLQVTRQEE-ELQAKDEELMKVKEKQTKVEAELEEMERKHQQLLEEKNILAEQLQAETELfAEAEEMrARLAAKKQELE 952
Cdd:PRK05035 426 PLVQYYRQAKaEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAKDKD-AVAAAL-ARVKAKKAAAT 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 953 EILHDLESrvEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEILLLEDQNSKFLKEK 1032
Cdd:PRK05035 504 QPIVIKAG--ARPDNSAVIAAREARKAQARARQAEKQAAAAADPK-KAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKA 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1033 KL---MEDRIAECTSQLAEEEEKAKNLAKLKNKQEmMITDLEERLKKEEKTRQELEKAKRKLDgettdlqDQIAELQAQI 1109
Cdd:PRK05035 581 AVaaaIARAKAKKAAQQAASAEPEEQVAEVDPKKA-AVAAAIARAKAKKAEQQANAEPEEPVD-------PRKAAVAAAI 652
|
250 260
....*....|....*....|...
gi 45382679 1110 EELKIQLAKKEEELQAALARGDE 1132
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDP 675
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
878-1108 |
9.94e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 225288 [Multi-domain] Cd Length: 652 Bit Score: 40.84 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 878 VTRQEEELQAKDEELMKVKEKQTKVEAELEEMERKhqqlLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 957
Cdd:COG2433 410 EEEERREITVYEKRIKKLEETVERLEEENSELKRE----LEELKREIEKLESELERFRREVRDKVRKDREIRARDRRIER 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 958 LESRVEEEEERNQILQNEKKKMQGHIQDLEEQLDEEEGARQKLQLE-KVTAEAKIKKMEEEILLLED------QNSKFLK 1030
Cdd:COG2433 486 LEKELEEKKKRVEELERKLAELRKMRKLELSGKGTPVKVVEKLTLEaIEEAEEEYGIKEGDVILVEDpsgggaRTAEELI 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45382679 1031 EKKLMEDRIAECTSQLAEEEEKAKNLAKLKNKQ-------EMMITDLEERLKKEEKTRQELEKAKRKldGETTDLQDQIA 1103
Cdd:COG2433 566 DKKPRAIIRGEEMSHAAAEEFFKNEIPVLPEGDvqiirldEFAVVDSEELRRAIEEWKKRFEERERR--QKEEDILRIIE 643
|
....*
gi 45382679 1104 ELQAQ 1108
Cdd:COG2433 644 EYRRE 648
|
|
|