|
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: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 1491.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 879 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 958
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 959 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1038
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1039 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1118
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1119 KEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE 1198
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1199 LRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVK 1278
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1279 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE 1358
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1359 TRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQR 1438
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1439 LEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALS 1518
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1519 LARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEV 1598
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1599 NMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1678
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1679 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAL 1758
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1759 LDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGA 1838
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1839 VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLE 1918
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1907083610 1919 EAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
99-802 |
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: 1433.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI----------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14920 151 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14920 231 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14920 311 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14920 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVG 658
Cdd:cd14920 471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKD---------------------VDRIVG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14920 530 LDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 1323.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespkpvKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESG---------KKKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYR-FLSNGYIPIPGQQDKDNFQ 337
Cdd:cd01377 152 HFGSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYfFLSQGELTIDGVDDAEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01377 232 LTDEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd01377 312 VTKGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK-FQKP 576
Cdd:cd01377 391 NHHMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 577 RQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQtiqrasfydsvsglheppvdri 656
Cdd:cd01377 469 KPKKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEE---------------------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 657 vgldqvtgmtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 736
Cdd:cd01377 527 ----------SGGGGGKKKKKGGSFRTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVL 596
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 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: 1225.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQS------SIALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14932 155 NFDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14932 235 TMEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14932 315 QKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14932 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVG 658
Cdd:cd14932 475 LKDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKD---------------------VDRIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTGMTETAFGsAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14932 534 LDKVAGMGESLHG-AFKTRKGMFRTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEG 612
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 1196.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKD-------------QGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14919 148 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14919 228 TMEAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14919 308 QKAQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14919 388 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVG 658
Cdd:cd14919 468 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKD---------------------VDRIIG 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14919 527 LDQVAGMSETALPGAFKTRKGMFRTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 1185.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIpqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI----------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14921 151 NFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14921 231 TLEAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14921 311 QKAQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14921 391 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQ 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVG 658
Cdd:cd14921 471 LKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKD---------------------VDRIVG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14921 530 LDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEG 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 1175.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQN------SLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd15896 155 NFDVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd15896 235 TMEAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd15896 315 QKAQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd15896 395 HTMFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVG 658
Cdd:cd15896 475 LKDEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKD---------------------VDRIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTGMTEtaFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd15896 534 LDKVSGMSE--MPGAFKTRKGMFRTVGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEG 611
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 1168.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14911 160 NFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14911 240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14911 320 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKpRQ 578
Cdd:cd14911 400 HTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiqrasfydsvsglheppvdRIVG 658
Cdd:cd14911 476 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA----------------------EIVG 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTgMTETAFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14911 534 MAQQA-LTDTQFGA--RTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 1131.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPqespkpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQdKDNFQE 338
Cdd:cd14930 151 NFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14930 230 TLESLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14930 310 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQ 578
Cdd:cd14930 390 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfydsvsglheppVDRIVG 658
Cdd:cd14930 470 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKD---------------------VEGIVG 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 LDQVTGMTETAFGSayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd14930 529 LEQVSSLGDGPPGG--RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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 [Multi-domain] Cd Length: 674 Bit Score: 1100.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 87 VEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML 166
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 167 QDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKN 246
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGN--------------VGRLEEQILQSNPILEAFGNAKTVRN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 247 DNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYI 325
Cdd:pfam00063 147 NNSSRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCY 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 326 PIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:pfam00063 227 TIDGIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:pfam00063 307 LCKRRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLC 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:pfam00063 387 INYVNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 566 EQGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRAsfydsv 645
Cdd:pfam00063 464 TFSKHPHFQKPRL-QGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAA------ 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 646 sglheppvdrivgldqvtgMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 725
Cdd:pfam00063 537 -------------------ANESGKSTPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSL 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 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: 1012.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 80 NPPKFSKVEDMAELTCLNEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISE 159
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 160 SAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpQGELERQLLQANPILESFG 239
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTE----------------VGSVEDQILESNPILEAFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 240 NAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRF 319
Cdd:smart00242 145 NAKTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 320 LSNG-YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENT-VAQKLCHLLGM 397
Cdd:smart00242 225 LNQGgCLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 398 NVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFE 477
Cdd:smart00242 305 DPEELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 478 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDK 557
Cdd:smart00242 384 VNSFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQ 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 558 TFVEKLVQEQGSHSKFQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiq 637
Cdd:smart00242 461 TFLEKLNQHHKKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVSN-- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 638 rasfydsvsglheppvdrivgldqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:smart00242 538 -------------------------------------AGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKK 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQS 797
Cdd:smart00242 581 PGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKT 660
|
730
....*....|....*..
gi 1907083610 798 KIFFRAGVLAHLEEERD 814
Cdd:smart00242 661 KVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
36-1492 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 912.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 36 VWIPSERHGFEAASIKEERGDEVMVELA---ENGKKAMVNKDDIQ--KMNPPKFSKVEDMAELTCLNEASVLHNLKDRYY 110
Cdd:COG5022 12 CWIPDEEKGWIWAEIIKEAFNKGKVTEEgkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 111 SGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKK 190
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 191 VIQYLAHVASSHKGRKdhnipqespkpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGAN 270
Cdd:COG5022 172 IMQYLASVTSSSTVEI---------------SSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 271 IETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-IPGQQDKDNFQETMEAMHIMGFS 349
Cdd:COG5022 237 IETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGID 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 350 HEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADF 429
Cdd:COG5022 317 EEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 430 AVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEY 509
Cdd:COG5022 396 IRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEY 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 510 QREGIEWNFIDFgLDLQPCIDLIERpANPPGVLALLDEECWFPKATDKTFVEKLVQ--EQGSHSKFQKPRQLKDKadFCI 587
Cdd:COG5022 475 VKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQrlNKNSNPKFKKSRFRDNK--FVV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 588 IHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppvdrivgldqvtgmte 667
Cdd:COG5022 551 KHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENI-------------------------------- 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 668 tafgsaykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFP 747
Cdd:COG5022 599 --------ESKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFP 670
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 748 NRIVFQEFRQRYEILTPNA----IPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFRAGVLAHLEEERDLKITDIIIF 823
Cdd:COG5022 671 SRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATR 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 824 FQAVCRGYLARKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEEL--LKVKEKQTK 901
Cdd:COG5022 751 IQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIikLQKTIKREK 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 902 VEGELEEMERKHQqlleeknilAEQLQAETELFAEAEEMRARLaaKKQELEEilhdlesrveeeeernQILQNEKKKMQA 981
Cdd:COG5022 831 KLRETEEVEFSLK---------AEVLIQKFGRSLKAKKRFSLL--KKETIYL----------------QSAQRVELAERQ 883
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 982 HIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSS--QLAEEEEKAKNLAKI 1059
Cdd:COG5022 884 LQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPsiEYVKLPELNKLHEVE 963
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1060 RNKQEVmISDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKV---------QLTKKEEELQGAL 1127
Cdd:COG5022 964 SKLKET-SEEYEDLLKKSTILVREGNKANSELKNfkkELAELSKQYGALQESTKQLKElpvevaelqSASKIISSESTEL 1042
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1128 ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQK--RDLSEELEALKTELEDT-------LDTTAAQQE 1198
Cdd:COG5022 1043 SILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEVTNRnlvkpanVLQFIVAQM 1122
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1199 LRTKREQEVAELKKALEDETKNHEAQIQ------DMRQRHATALEELS-----EQLEQAKRFKANLEKNKQGLETDNKEL 1267
Cdd:COG5022 1123 IKLNLLQEISKFLSQLVNTLEPVFQKLSvlqlelDGLFWEANLEALPSpppfaALSEKRLYQSALYDEKSKLSSSEVNDL 1202
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1268 ACEVK-VLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDN--VSTLLEEAEKKGIKFAKDA--- 1341
Cdd:COG5022 1203 KNELIaLFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNekLLSLLNSIDNLLSSYKLEEevl 1282
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1342 -AGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQsQLADTKKKVDDDLGTIes 1420
Cdd:COG5022 1283 pATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCREFEISDVDEELEELI-QAVKVLQLLKDDLNKL-- 1359
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1421 leeakKKLLKDVEALSQRLEEKVLA-YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK--QKKFDQLLAEEK 1492
Cdd:COG5022 1360 -----DELLDACYSLNPAEIQNLKSrYDPADKENNLPKEILKKIEALLIKQELQLSLEGKDetEVHLSEIFSEEK 1429
|
|
| 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 [Multi-domain] Cd Length: 633 Bit Score: 859.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSS-----------ASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL-----SNGYIPIPGQQD 332
Cdd:cd00124 150 LQFDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 333 KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT--DQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd00124 230 AEEFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ-GASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd00124 310 IKVGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGS 569
Cdd:cd00124 390 NEKLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 570 HSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdeiqtiqrasfydsvsglh 649
Cdd:cd00124 467 HPRFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 650 eppvdrivgldqvtgmtetafgsayktkkgmfrtvgqlYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 729
Cdd:cd00124 519 --------------------------------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQ 560
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 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: 783.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKdhniPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPG----KKAQFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKsDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14927 157 HFGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQ-DMLLVSMNpyDYHFCSQGVTTVDNMDDGEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14927 236 MATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14927 316 YVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQK 575
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 576 PR---QLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfyDSVSglhepp 652
Cdd:cd14927 472 PRpdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYENYVGS-------DSTE------ 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 653 vdrivglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14927 539 -------DPKSGVKEK------RKKAASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRC 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 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: 767.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATGDLAKK--------KDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPEL-IELLLITTNpyDYPFISQGEILVASIDDAEELL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14913 233 ATDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKP 576
Cdd:cd14913 392 NHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrasfYDSVSGlheppvd 654
Cdd:cd14913 469 KVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYAT----------FATADA------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 655 rivgldqvtgmtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14913 532 ------------DSGKKKVAKKKGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNG 599
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 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: 746.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipqeSPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKK----------TDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14909 151 HFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14909 231 LTDQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14909 311 VTQGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKP 576
Cdd:cd14909 390 NHHMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 577 RQLK---DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppv 653
Cdd:cd14909 467 KPPKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAGQ------------------ 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 drivgldqvTGMTETAFGSAYKtKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14909 529 ---------SGGGEQAKGGRGK-KGGGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCN 598
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 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: 737.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRKDHnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG------------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHL-KSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14934 149 HFGTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELiESLLLVPNPKEYHWVSQGVTVVDNMDDGEELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14934 229 ITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14934 309 VQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKP 576
Cdd:cd14934 388 NHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 577 RQLKDK---ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdRFVAELWKDEiqtiqrasfydsvsglheppv 653
Cdd:cd14934 465 KGGKGKgpeAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSS-LGLLALLFKE--------------------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 drivgldqvtgmtETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14934 523 -------------EEAPAGSKKQKRGsSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLAC 589
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 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: 716.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSG-LIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqESpkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--------ET--------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01380 146 LFDKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGgSPVIDGVDDAAEFE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd01380 226 ETRKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd01380 306 IVKPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 497 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK--FQ 574
Cdd:cd01380 386 FNQHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 KPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhqssdrfvaelwkdeiqtiqRASfydsvsglheppvd 654
Cdd:cd01380 462 KPRFSNTA--FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVL--------------------KAS-------------- 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 655 rivgldqvtgmtetafgsayKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd01380 506 --------------------KNRK---KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACG 562
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 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: 711.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASShkgrkdhnipqesPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAM-------------IESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlKSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14929 148 HFGARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKE--LRDLLLVSANpsDFHFCSCGAVAVESLDDAEEL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14929 226 LATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14929 306 YVTRSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQK 575
Cdd:cd14929 385 FNQHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQK 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglheppv 653
Cdd:cd14929 462 PKPDKKKfeAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYIST------------------ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 drivgldqvtgMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14929 524 -----------DSAIQFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCN 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 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: 703.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDhnipqESPKpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKD-----QTPG----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14917 153 HFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPEL-LDMLLITNNpyDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 417 YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 497 FNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQK 575
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 576 PRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglhEPPV 653
Cdd:cd14917 468 PRNIKGKpeAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGA--------------DAPI 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 DRIVGldqvtgmtetafgsayKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14917 534 EKGKG----------------KAKKGsSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRC 597
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 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: 688.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGES 180
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 181 GAGKTENTKKVIQYLAHVASSHKGRKDHNipqespkpVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 260
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEES--------GKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 261 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQET 339
Cdd:cd14918 155 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMAT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 340 MEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14918 235 DSAIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14918 315 KGQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 500 TMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPRQ 578
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 LKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqraSFYDSVSGlheppvdri 656
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLF----------STYASAEA--------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 657 vgldqvtgmtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVL 736
Cdd:cd14918 532 ----------DSGAKKGAKKKGSSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVL 601
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 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: 686.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ-------QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFN--NYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14923 155 FGATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNpfDFPFVSQGEVTVASIDDSEELL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14923 234 ATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14923 314 VTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKP 576
Cdd:cd14923 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYdQHLGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRASFYDSVSGlheppvd 654
Cdd:cd14923 470 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAGAEAGDSGGSKKGG------- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 655 rivgldqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14923 543 --------------------KKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNG 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14923 603 VLEGIRICRKGFPSRILYADFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 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: 685.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnipqESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEITSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14912 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLItTNPYDYPFVSQGEISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLV-QEQGSHSKFQKPR 577
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYeQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 578 QLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvSGLHeppvdr 655
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF----------------SGAQ------ 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 656 ivgldqvTGMTETAFGSAYK--TKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14912 530 -------TAEGASAGGGAKKggKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRC 602
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14912 603 NGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| 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: 685.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVAS-SHKGRKDHnipqespkPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKEN--------PNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEgfNN---YRFLSNGYIPIPGQQDKDN 335
Cdd:cd14916 154 HFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVT--NNpydYAFVSQGEVSVASIDDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14916 232 LLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGN 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14916 312 EYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 496 LFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQ 574
Cdd:cd14916 391 FFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 KPRQLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrASFYDSVSGlhepp 652
Cdd:cd14916 468 KPRNVKGKqeAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF---------STYASADTG----- 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 653 vdrivgldqvtgmtETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14916 534 --------------DSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRC 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14916 600 NGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| 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: 680.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnipqESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEATSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLL-EGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14910 156 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLItTNPYDYAFVSQGEITVPSIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd14910 236 TDSAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd14910 316 TKGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKPR 577
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 578 QLKDK--ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvSGlheppvdr 655
Cdd:cd14910 472 PAKGKveAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF----------------SG-------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 656 ivgldQVTGMTETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14910 528 -----AAAAEAEEGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNG 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 735 VLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKG-FMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14910 603 VLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| 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 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGRKdhnipqESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKK------EEAASGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLkSDLLLEGFNNYRF--LSNGYIPIPGQQDKDNFQ 337
Cdd:cd14915 156 FGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL-IEMLLITTNPYDFafVSQGEITVPSIDDQEELM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDY 417
Cdd:cd14915 235 ATDSAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 418 VQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 497
Cdd:cd14915 315 VTKGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 498 NHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQ-GSHSKFQKP 576
Cdd:cd14915 394 NHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 577 RQLKDKAD--FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvSGLHeppvd 654
Cdd:cd14915 471 KPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLF----------------SGGQ----- 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 655 rivgldqvTGMTETAFGSAYKTKKG-MFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14915 530 --------TAEAEGGGGKKGGKKKGsSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCN 601
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 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: 640.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-------------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--HLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14883 143 FDASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK-ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14883 223 DHLRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGaSFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14883 303 NVTEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQK 575
Cdd:cd14883 382 FFNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 576 PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfydsvsglhEPPVDR 655
Cdd:cd14883 459 PDRRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFT-------------------YPDLLA 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 656 IVGLDQVTGMTETAFGsaykTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGV 735
Cdd:cd14883 520 LTGLSISLGGDTTSRG----TSKGK-PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGM 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 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: 639.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGRKDHnipqespkpVKpqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESEVER---------VK------DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY-IPIPGQQDKDNFQE 338
Cdd:cd01378 147 FDFKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG---R 415
Cdd:cd01378 227 VLNAMKVIGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd01378 306 SVYEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 496 LFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFP-KATDKTFVEKLVQEQGSHSKFQ 574
Cdd:cd01378 386 IFIELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 KPRQLKD--KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglhepp 652
Cdd:cd01378 463 CPSGHFElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDL----------------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 653 vdrivgldqvtgmtetafgsaykTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd01378 526 -----------------------DSKKRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKY 582
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 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: 638.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRgkKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-------------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQE 338
Cdd:cd01383 141 FDAAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYV 418
Cdd:cd01383 221 LKEALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 419 QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 498
Cdd:cd01383 301 VKKLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFN 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 499 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRq 578
Cdd:cd01383 381 RHLFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER- 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 579 lkDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVAELwkdeiqtiqrasfYDSVSGLHeppvdrivg 658
Cdd:cd01383 457 --GGA-FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQL-------------FASKMLDA--------- 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 659 lDQVTGMTETAFGSAyktkkGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEG 738
Cdd:cd01383 511 -SRKALPLTKASGSD-----SQKQSVATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEV 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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: 605.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKgrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISGQHS-------------------WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01381 142 HFNKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01381 222 DIRSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS--FIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd01381 302 ETVVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLI-ERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 572
Cdd:cd01381 382 QQFFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKN 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 573 FQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglhepp 652
Cdd:cd01381 458 YLKPKSDLNTS-FGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM----------------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 653 vdrivgldqvtgMTETAFGSAyktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd01381 520 ------------GSETRKKSP---------TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRY 578
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 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: 601.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVAsshkGRKDHNIpqespKPVkpqgelERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEG-----RSV------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYiPIPGQQDKDN 335
Cdd:cd01384 146 IQFDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLnqSKCF-ELDGVDDAEE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAiLTPRIK 412
Cdd:cd01384 225 YRATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDA-LCKRVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 413 VGRD-YVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01384 304 VTPDgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 571
Cdd:cd01384 383 KLQQHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 572 KFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvsglheP 651
Cdd:cd01384 460 RFSKPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLF---------------------P 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 652 PVDRivgldqvtgmteTAFGSAYKtkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 731
Cdd:cd01384 517 PLPR------------EGTSSSSK-----FSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLR 579
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 732 CNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAiPKGFMDGKQACERMIRALELDPnlYRIGQSKIFFR 802
Cdd:cd01384 580 CGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| 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: 568.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-------------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgeHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd14872 142 HFDNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP--DPASRGGWGSSAAYGYLSlSGCIEVEGVDDVADFE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQAS---MPENTVAQKLCHLLGMNVMEFTRAILTPRIKV- 413
Cdd:cd14872 220 EVVLAMEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVSgstVANRDVLKEVATLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 494 QQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 573
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTF 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 574 QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvsglhePPV 653
Cdd:cd14872 457 VYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLF---------------------PPS 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 DrivgLDQVTGMTetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14872 516 E----GDQKTSKV----------------TLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYA 575
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILtPNAIPKGFM-DGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14872 576 GVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| 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: 568.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG------------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNyrflsngyipipgqqDKDNFQ 337
Cdd:cd01382 143 IHFNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDPLLD---------------DVGDFI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNT-------DQASMPENTVAQKlchLLGMNVMEF-----TRA 405
Cdd:cd01382 208 RMDKAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYAAE---LLGLDQDELrvsltTRV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqGASFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd01382 285 MQTTRGGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFC 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQ 565
Cdd:cd01382 363 INYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 566 EQGSHSKFQKPRQ--------LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiq 637
Cdd:cd01382 440 KHKNHFRLSIPRKsklkihrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESS----- 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 638 rasfydsvsglheppvdrivgldqvtgmTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:cd01382 515 ----------------------------TNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMT 566
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfMDGKQACERMIRALELDPNLYRIGQS 797
Cdd:cd01382 567 SHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLT 644
|
....*
gi 1907083610 798 KIFFR 802
Cdd:cd01382 645 KVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
99-802 |
1.77e-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: 552.46 E-value: 1.77e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQ----DREDQS 173
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 174 ILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 254 KFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 334 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD--QASMPENTVAqKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTvlEDATTLQSLK-LAAELLGVNEDALEKALLTRQL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 412 KVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14890 320 FVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYANE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE-RPANPPGVLALLDeECWFPKAT--DKTFVEKLVQ--- 565
Cdd:cd14890 399 KLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLD-DCWRFKGEeaNKKFVSQLHAsfg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 566 ----------EQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdeiQT 635
Cdd:cd14890 477 rksgsggtrrGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------RS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 636 IQRASfydsvsglheppvdrivgldqvtgmtetafgsayktkkgmfrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHE 715
Cdd:cd14890 544 IREVS-------------------------------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNET 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 716 KRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipkgfMDGKQACERMIRALELDPNLYRIG 795
Cdd:cd14890 581 KAPGKFDGLDCLRQLKYSGMMEAIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIG 655
|
....*..
gi 1907083610 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 |
1.04e-172 |
|
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: 542.04 E-value: 1.04e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVAsshkgrkdhnipqesPKPVKPQGElerQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN---------------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQQDKDNFQ 337
Cdd:cd01387 143 FFE-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQ---ASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd01387 222 RLLAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHGqegVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINkALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd01387 302 RERIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQ 574
Cdd:cd01387 381 YYFNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYS 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 KPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRAsfydsvsglheppvd 654
Cdd:cd01387 458 KPRM--PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRAQTDKA--------------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 655 rivgldqvtgmTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd01387 521 -----------PPRLGKGRFVTMKPRTPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSG 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 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 |
3.30e-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: 536.19 E-value: 3.30e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLahVASSHKGrkdHNipqespkpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG---YG------------SGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNFQ 337
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKER-NTDQASMPENT-VAQKLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASfIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 571
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 572 KFQKPrQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL----------WKdeiqtIQRAsF 641
Cdd:cd01385 460 YYEKP-QVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWA-----VLRA-F 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 642 YDSVSGLHEPPVDRIVGLDQVTGM----TETAFGSAYKTKKGMfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:cd01385 532 FRAMAAFREAGRRRAQRTAGHSLTlhdrTTKSLLHLHKKKKPP--SVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKK 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGFMDGKQACERMIRALELDPNLYRIGQS 797
Cdd:cd01385 610 PLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKT 685
|
....*
gi 1907083610 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 |
9.38e-167 |
|
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: 525.88 E-value: 9.38e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIpqespkpvkpqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG---GLNDSTI---------------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLsgAGEHLKSDLLLEGFNNYRFL-SNGYIPIPGQQDKDNF 336
Cdd:cd14903 143 LQFDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGMSDRKHF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM--PENTVAQKLCHLLGMNVMEFTRAILTPRIKVG 414
Cdd:cd14903 221 ARTKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQgASFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14903 301 GDVYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQ 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKLVqeqGSHSKFQ 574
Cdd:cd14903 380 QKFTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQ 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 K----PRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiQRASFYDSVSglhe 650
Cdd:cd14903 453 DviefPR--TSRTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK------EKVESPAAAS---- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 651 ppvdrivgldqvtgMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 730
Cdd:cd14903 521 --------------TSLARGARRRRGGALTTTTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQL 586
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 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 |
5.83e-165 |
|
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: 520.89 E-value: 5.83e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMY------RGKKRHEMPPHIYAISESAYRCMLQDRE-- 170
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 171 --DQSILCTGESGAGKTENTKKVIQYLAHVaSSHKGRKDHNIPQESpkpvkpqgeLERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASV-SSATTHGQNATEREN---------VRDRVLESNPILEAFGNARTNRNNN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIP 326
Cdd:cd14901 151 SSRFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 327 IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF-KKERNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14901 231 RDGVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAS-FIGILDIAGFEIFELNSFEQL 484
Cdd:cd14901 311 LCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 485 CINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgldlqP----CIDLIErpANPPGVLALLDEECWFPKATDKTFV 560
Cdd:cd14901 391 CINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PnndaCVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 561 EKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdeiqtiqras 640
Cdd:cd14901 464 NKYYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 641 fydsvsglheppvdrivgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGK 720
Cdd:cd14901 531 ------------------------------------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSE 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 721 LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRA------LELDPNLYrI 794
Cdd:cd14901 569 FDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-V 647
|
....*.
gi 1907083610 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 |
2.57e-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: 513.86 E-value: 2.57e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRgKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS---------------LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVT---------GYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIP-- 326
Cdd:cd14888 145 LQFSKLkskrmsgdrGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 327 ----------------------IPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE 384
Cdd:cd14888 225 idmssfephlkfryltksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 385 NTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG 461
Cdd:cd14888 305 ASCTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 462 ASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGV 541
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 542 LALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSS 621
Cdd:cd14888 462 FCMLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 622 DRFVaelwkdeiqtiqrasfydsvSGLHEPPVDRIVGLdqvtgmtetafgsayKTKKGMFRTVGQLYKESLTKLMATLRN 701
Cdd:cd14888 540 NPFI--------------------SNLFSAYLRRGTDG---------------NTKKKKFVTVSSEFRNQLDVLMETIDK 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 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 |
7.72e-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: 509.34 E-value: 7.72e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDhnipqespkpVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSL----------KEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPGQQDKDNF 336
Cdd:cd14873 151 LNICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerNTDQASMPENTVAQKLCHLLGMNVMEFTRAiLTPRIKVGR- 415
Cdd:cd14873 231 REVITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRg 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKLQ 494
Cdd:cd14873 307 EEILTPLNVQQAVDSRDSLAMALYARCFEWVIKKINS---RIKGKEDfKSIGILDIFGFENFEVNHFEQFNINYANEKLQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 495 QLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQ 574
Cdd:cd14873 384 EYFNKHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 KPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfYDSVSGLHEPPvd 654
Cdd:cd14873 460 KPRVAVN--NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLFE-----------HVSSRNNQDTL-- 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 655 rivgldqvtgmtetafGSAYKTKKGmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNG 734
Cdd:cd14873 525 ----------------KCGSKHRRP---TVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSG 585
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 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 |
2.55e-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: 2.55e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASShkgrkdhnipqespkpvkPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKA------------------NNRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGagehLKSDLLLEGFN-------NYRFLSNGYIPIPGQQD 332
Cdd:cd01379 144 FTSTGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAG----LAEDKKLAKYKlpenkppRYLQNDGLTVQDIVNNS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 333 --KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENTVA-QKLCHLLGMNVMEFTRAi 406
Cdd:cd01379 220 gnREKFEEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTeveSNHQTDKSSRISNPEAlNNVAKLLGIEADELQEA- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd01379 299 LTSHSVVTRgETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQ 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCID-LIERPAnppGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd01379 379 LCINIANEQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEK 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 563 LvqEQGSHSKFQKpRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdeiqtiqrasfy 642
Cdd:cd01379 455 F--HNNIKSKYYW-RPKSNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 643 dsvsglheppvdrivgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLD 722
Cdd:cd01379 517 ----------------------------------------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFD 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 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 |
4.13e-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: 4.13e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKK-RHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASSHkgrkdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSD------------------DSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD----- 332
Cdd:cd14897 143 LHFTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDseele 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 333 --KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14897 223 yyRQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14897 303 NTIRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14897 383 NLSNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKY 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 567 QGSHSKFQKPrqLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfydsvs 646
Cdd:cd14897 460 CGESPRYVAS--PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 647 glheppvdrivgldqvtgmtetafgsayktkkgmfrtvgQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLV 726
Cdd:cd14897 522 ---------------------------------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELV 562
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 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 |
1.43e-154 |
|
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: 492.35 E-value: 1.43e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEM---PPHIYAISESAYRCMLQDR----ED 171
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhniPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKG------ASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNG-YIPIPGQ 330
Cdd:cd14892 155 FGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGnCVEVDGV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 331 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQ----ASMPENTVAQKLCHLLGMNVMEFTRAI 406
Cdd:cd14892 235 DDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRF--EENADDedvfAQSADGVNVAKAAGLLGVDAAELMFKL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 407 LTPRIKVGRDYV-QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ---------GASFIGILDIAGFEIF 476
Cdd:cd14892 313 VTQTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 477 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPanPPGVLALLDEECWFP-KAT 555
Cdd:cd14892 393 PTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTT 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 556 DKTFVEKLVQEQ-GSHSKFQKPRQLKDkaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwkdeiq 634
Cdd:cd14892 470 DKQLLTIYHQTHlDKHPHYAKPRFECD--EFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 635 tiqrasfydsvsglheppvdrivgldqvtgmtetafgsayktkkgmFRTvgqlykeSLTKLMATLRNTNPNFVRCIIPNH 714
Cdd:cd14892 536 ----------------------------------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNN 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 715 EKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN-AIPKGFMDGKQACERM-----IRALELD 788
Cdd:cd14892 563 LKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALE 642
|
730
....*....|....
gi 1907083610 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 |
1.76e-146 |
|
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: 468.63 E-value: 1.76e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY-----------RGKKRHEMPPHIYAISESAYRCM-- 165
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 166 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVAsshkgrkDHNIPQESPKPVKPQGeLERQLLQANPILESFGNAKT 243
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAG-------DNNLAASVSMGKSTSG-IAAKVLQTNILLESFGNART 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 244 VKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEhlksdlllegfnnyrflsng 323
Cdd:cd14900 154 LRNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASE-------------------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 324 yipipGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQK-------LCHLLG 396
Cdd:cd14900 214 -----AARKRDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGAS-FIGILDIAG 472
Cdd:cd14900 289 VDATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 473 FEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP 552
Cdd:cd14900 369 FEVFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMP 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 553 KATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNmdplndnvatllhqssdrfvaelwKDE 632
Cdd:cd14900 446 KGSDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKN------------------------KDV 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 633 iqtiqrasfydsvsgLHEPPVDrivgldqvtgmtetafgsayktkkgMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIP 712
Cdd:cd14900 502 ---------------LHQEAVD-------------------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKP 540
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1907083610 713 NHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 762
Cdd:cd14900 541 NDLCKAGIYERERVLNQLRCNGVMEAVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
99-765 |
4.73e-145 |
|
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: 466.43 E-value: 4.73e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH--------EMPPHIYAISESAYRCMLQDR 169
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 170 EDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPV-KPQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATsKSTKSIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 249 SSRFGKFIRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE----GFNNYRFLSNG 323
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKnqlsGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 324 YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFK-KERNTDQASMPENT-VAQKLCHLLGMNVME 401
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 402 FTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL-------DRTKRQGASFIGILDIAGFE 474
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIE--WNFIDFgLDLQPCIDLIERPanPPGVLALLDEECWFP 552
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEdyLNQLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 553 KATDKTFVEKLVQEQGSHSKFQKPRQLKdKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDE 632
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKIN-KDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 633 IQTIQRASFYDSVSglheppvdrivgldqvtgmtetafgsaYKTKKgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIP 712
Cdd:cd14907 557 DGSQQQNQSKQKKS---------------------------QKKDK----FLGSKFRNQMKQLMNELMQCDVHFIRCIKP 605
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 713 NHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 765
Cdd:cd14907 606 NEEKKADLFIQGYVLNQIRYLGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN 658
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
101-802 |
2.17e-144 |
|
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276854 Cd Length: 659 Bit Score: 464.38 E-value: 2.17e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 101 VLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCML----QDREDQSILC 176
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 177 TGESGAGKTENTKKVIQYLAHVAsshkgrkdhnipqespkpvKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC-------------------RGNSQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 257 RINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKSDLLLEGFnnYRFLSNGYipipGQQD-- 332
Cdd:cd14889 144 QLRFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGisAEDRENYGLLDPGK--YRYLNNGA----GCKRev 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 333 ---KDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFkkERNTDQASMPENTVAQKL---CHLLGMNVMEFTRAi 406
Cdd:cd14889 217 qywKKKYDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEALKVENDSNGWLkaaAGQFGVSEEDLLKT- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 407 LTPRIKVGR-DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQG--ASFIGILDIAGFEIFELNSFEQ 483
Cdd:cd14889 294 LTCTVTFTRgEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQ 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 484 LCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKL 563
Cdd:cd14889 374 ACINLANEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 564 VQEQGSHSKFQKPRQLKDKadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKdeiQTIQRASFYD 643
Cdd:cd14889 451 NIHFKGNSYYGKSRSKSPK--FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFT---ATRSRTGTLM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 644 SVSGLhePPVdrivgldqvtgmTETAFGSAYKtkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDP 723
Cdd:cd14889 526 PRAKL--PQA------------GSDNFNSTRK------QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDS 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 724 HLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL--TPNaIPKgfmdGKQACERMIRALELDPnlYRIGQSKIFF 801
Cdd:cd14889 586 KYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFF 658
|
.
gi 1907083610 802 R 802
Cdd:cd14889 659 K 659
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
99-802 |
3.63e-140 |
|
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: 451.81 E-value: 3.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRyySGLI----YTYSGLFCVVINPYKNLPiysENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE---D 171
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 252 FGKFIRINFDVTGY-IVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLS-NGYIPIPG 329
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 330 QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKErNTDQASMPENTVAQK-----LCHLLGMNVMEFTR 404
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEE-DTSEGEAEIASESDKealatAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 405 AILTPRIkVGRDYVQKAQ-TKEQADFAVEALAKATYERLFRWLVHRINKALDRtKRQGASFIGILDIAGFEIFEL-NSFE 482
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 483 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEK 562
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIA--SKPNGILPLLDNEARNPNPSDAKLNET 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 563 LVQEQGSHSKFQKPRQlKDKAD-FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSsdrfvaelwkdeiqtiqrASF 641
Cdd:cd14891 470 LHKTHKRHPCFPRPHP-KDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS------------------AKF 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 642 YDSVSGLheppVDrivgldqvtgmtetafgsayktkkgmfrtvgqlykesltklmaTLRNTNPNFVRCIIPNHEKRAGKL 721
Cdd:cd14891 531 SDQMQEL----VD-------------------------------------------TLEATRCNFIRCIKPNAAMKVGVF 563
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 722 DPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQA-CERMIRALELDPNLYRIGQSKIF 800
Cdd:cd14891 564 DNRYVVDQLRCSGILQTCEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVF 643
|
..
gi 1907083610 801 FR 802
Cdd:cd14891 644 FR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
99-802 |
3.43e-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: 3.43e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLahvASSHKGRKDHNIpqespkpvkpqgeleRQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL---SSLYQDQTEDRL---------------RQPEDVLPILESFGHAKTILNANASRFGQVLRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQDKDNFQ 337
Cdd:cd14896 143 HLQ-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGAcRLQGKEDAQDFE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQ--ASMPENTVAQKLCHLLGMNVmEFTRAILTPRIKV-G 414
Cdd:cd14896 222 GLLKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPP-ERLEGAVTHRVTEtP 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 415 RDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGA-SFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14896 301 YGRVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 494 QQLFNHTMFILEQEEYQREGIEWNFIDfGLDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 573
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSY 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 574 QKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiQRAsfyDSVSGLHEPPV 653
Cdd:cd14896 458 AKPQL--PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLF-------QEA---EPQYGLGQGKP 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 drivgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14896 526 -----------------------------TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQA 576
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 734 GVLEGIRICRQGFPNRIVFQEFRQRYEILTpNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 802
Cdd:cd14896 577 GILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
99-802 |
1.90e-133 |
|
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: 433.21 E-value: 1.90e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASshkGRKDHNIPQespkpvkpqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIAK---------------VIDVNPLLESFGNAKTTRNDNSSRFGKFTQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNGYIPIPGQQDKDN 335
Cdd:cd14904 143 LQFDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQkLCHLLGMNVMEFTRAILTPRIKVGR 415
Cdd:cd14904 223 FASTQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 416 DYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQ 495
Cdd:cd14904 302 ESVTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 496 LFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSK 572
Cdd:cd14904 382 KFTTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNES 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 573 FQKPRQlkDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWkdeiqtiqrasfydsvsglhepp 652
Cdd:cd14904 458 IDFPKV--KRTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELF----------------------- 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 653 vdrivglDQVTGMTETAFGSAYKTKKGMfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14904 513 -------GSSEAPSETKEGKSGKGTKAP-KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRS 584
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGfmDGKQACERMIRAL-ELDPNLYRIGQSKIFFR 802
Cdd:cd14904 585 AGVIEAIRITRSGYPSRLTPKELATRYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
99-802 |
1.40e-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: 1.40e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR--GKKRHE-------MPPHIYAISESAYRCMLQD- 168
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQEspkpvkpQGELERQLLQANPILESFGNAKTVKNDN 248
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELG-------KLSIMDRVLQSNPILEAFGNARTLRNDN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 249 SSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGE--------HLKSDLLLEGFNNYRFL 320
Cdd:cd14908 154 SSRFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEeehekyefHDGITGGLQLPNEFHYT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 321 SNGYIPIPGQ-QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPE---NTVAQKLCHLLG 396
Cdd:cd14908 234 GQGGAPDLREfTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIAEegnEKCLARVAKLLG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 397 MNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL--DRTKRQGASfIGILDIAGFE 474
Cdd:cd14908 314 VDVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 475 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFP-K 553
Cdd:cd14908 393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 554 ATDKTFVEKLV--------QEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLM-KNmdplndnvatllhqssdrf 624
Cdd:cd14908 470 GSDANYASRLYetylpeknQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKN------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 625 vaelwKDEIQtiqrasfydsvsglheppvdrivgldqvtgmtetafgsayKTKKGMFRTvGQLYKESLTKLMATLRNTNP 704
Cdd:cd14908 531 -----KDEIP----------------------------------------LTADSLFES-GQQFKAQLHSLIEMIEDTDP 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 705 NFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnAIPK--------------- 769
Cdd:cd14908 565 HYIRCIKPNDAAKPDLVTRKRVTEQLRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEvvlswsmerldpqkl 643
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907083610 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 |
1.40e-130 |
|
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: 427.39 E-value: 1.40e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYR--------GKKRHEMPPHIYAISESAYRCMLQ-D 168
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 169 REDQSILCTGESGAGKTENTKKVIQYLAHVASshkgrkdhniPQES-PKPVKPQGELERQLLQANPILESFGNAKTVKND 247
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGR----------DQSStEQEGSDAVEIGKRILQTNPILESFGNAQTIRND 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 248 NSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLsNGYIP- 326
Cdd:cd14902 151 NSSRFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELL-NSYGPs 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 327 ---IPGQQDKDN--FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---CHLLGMN 398
Cdd:cd14902 230 farKRAVADKYAqlYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 399 VMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD--------RTKRQGASFIGILDI 470
Cdd:cd14902 310 VDKLETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 471 AGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECW 550
Cdd:cd14902 390 FGFESLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 551 FPKATDKTFVEKLVQEQGSHSKFqkprqlkdkadfCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDrfvaelwk 630
Cdd:cd14902 467 MPKGSNQALSTKFYRYHGGLGQF------------VVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSN-------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 631 deiqtiqrasfydsvsglhepPVDRIVGLDQVTGMTETAFGSAYKTKKGMFRT--VGQLYKESLTKLMATLRNTNPNFVR 708
Cdd:cd14902 527 ---------------------EVVVAIGADENRDSPGADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVR 585
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 709 CIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTP 764
Cdd:cd14902 586 CLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
97-855 |
2.46e-128 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 424.83 E-value: 2.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 97 NEASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHE-MPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 176 CTGESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIPQespkpvkpqgelerQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMDLKIQN--------------AIMAANPVLEAFGNAKTIRNNNSSRFGRF 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 256 IRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:PTZ00014 251 MQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKD 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASM--PEN-TVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:PTZ00014 331 FEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIegKEEGGLTDAAAisDESlEVFNEACELLFLDYESLKKELTVKV 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsFIGILDIAGFEIFELNSFEQLCINYTN 490
Cdd:PTZ00014 411 TYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITN 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 491 EKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSH 570
Cdd:PTZ00014 490 EMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNN 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 571 SKFQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiQTIQRAsfydsvsglhe 650
Cdd:PTZ00014 567 PKYKPAKVDSNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEG--VEVEKG----------- 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 651 ppvdrivgldqvtgmtetafgsayKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQL 730
Cdd:PTZ00014 633 ------------------------KLAKGQL--IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQL 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 731 RCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR---AGVLA 807
Cdd:PTZ00014 687 HSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELT 766
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 1907083610 808 HLEEERDLKITDIIIFFQAVCRGYLARKAFAKKqqqlsaLKVLQRNCA 855
Cdd:PTZ00014 767 QIQREKLAAWEPLVSVLEALILKIKKKRKVRKN------IKSLVRIQA 808
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
100-763 |
6.89e-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: 419.36 E-value: 6.89e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPiyseniiEMYRGKKRHE-------MPPHIYAISESAYRCMLQ----- 167
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 168 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSHKGRKDHNIPQEspkpvkpqgelerQLLQANPILESFGNA 241
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS-------------ELLSANPILESFGNA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 242 KTVKNDNSSRFGKFIRINF-----DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN- 315
Cdd:cd14895 142 RTLRNDNSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 316 -NYRFLSNG--YIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD-------------- 378
Cdd:cd14895 222 qEFQYISGGqcYQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrl 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 379 -QASMPENTVAQKL---CHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL 454
Cdd:cd14895 302 aSASPSSLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSAS 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 455 DRTK----------RQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLD 524
Cdd:cd14895 382 PQRQfalnpnkaanKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 525 lQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRqlKDKAD--FCIIHYAGKVDYKADEWL 602
Cdd:cd14895 462 -SVCLEMLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFC 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 603 MKNMDPLNDNVATLLHQSSDRFVAELWKdeiqtiqrasfydsvsglhepPVDRIVGLDQVTGMTETAFGSAYKTKKGmfr 682
Cdd:cd14895 537 EKNKDQPNAELFSVLGKTSDAHLRELFE---------------------FFKASESAELSLGQPKLRRRSSVLSSVG--- 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 683 tVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 762
Cdd:cd14895 593 -IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL 671
|
.
gi 1907083610 763 T 763
Cdd:cd14895 672 V 672
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
99-800 |
1.83e-124 |
|
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: 407.84 E-value: 1.83e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRH-EMPPHIYAISESAYRCMLQDREDQSILCT 177
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAhvaSSHKGRKDHNIpQESpkpvkpqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMDLRI-QTA-------------IMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQ 337
Cdd:cd14876 144 LDVASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 338 ETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPEN---TVAQKLCHLLGMNVMEFTRAILTPRIK 412
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKItgKTEQGVDDAAAISNeslEVFKEACSLLFLDPEALKRELTVKVTK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 413 VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDrtKRQG-ASFIGILDIAGFEIFELNSFEQLCINYTNE 491
Cdd:cd14876 304 AGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 492 KLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppGVLALLDEECWFPKATDKTFVEKLVQEQGSHS 571
Cdd:cd14876 382 MLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 572 KFqKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTiqrasfydsvsglhep 651
Cdd:cd14876 459 KF-KPAKVDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVE---------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 652 pvdrivgldqvtgmtetafgsAYKTKKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLR 731
Cdd:cd14876 522 ---------------------KGKIAKGSL--IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLH 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 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 |
1.63e-120 |
|
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: 397.84 E-value: 1.63e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHVASSHKGRkdhnipqespkpvkpqgeLERQLLQA-NPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV------------------LSVEKLNAaLTVLEAFGNVRTALNGNATRFSQLFS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLE--GFNNYRFLSNGYIPIPGQQDKDN 335
Cdd:cd01386 143 LDFDQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIVPLQKPEDKQKAAAA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 336 FQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAI--------- 406
Cdd:cd01386 223 FSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 407 ---LTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASfIGILDIAGFEIFELN---- 479
Cdd:cd01386 303 qqsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqr 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 480 --SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERP---ANPP---------GVLALL 545
Cdd:cd01386 382 gaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 546 DEECWFPKATDKTFVEKLVQEQG--SHSKFQKPRQLKDKA-DFCIIHYAGK--VDYKADEWLMK-NMDPLNDNVATLLHQ 619
Cdd:cd01386 462 DEEALYPGSSDDTFLERLFSHYGdkEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQE 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 620 SSDRFVAelwkdeiqtiqrasfydsvsglheppvdrivgldqvtgmtetafgsayKTKKGMFRTVgqlyKESLTKLMATL 699
Cdd:cd01386 542 SQKETAA------------------------------------------------VKRKSPCLQI----KFQVDALIDTL 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 700 RNTNPNFVRCIIPNH--EKRAGK----------LDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 767
Cdd:cd01386 570 RRTGLHFVHCLLPQHnaGKDERStsspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLT 649
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907083610 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 |
2.25e-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: 2.25e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDRE--DQSI 174
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 175 LCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQEspkpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGK 254
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER----------IEQRILNSNPVMEAFGNACTLRNNNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 255 FIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGyipiPGQQDKD 334
Cdd:cd14880 151 FIQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNP----ERNLEED 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 335 NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTV---AQKLCHLLGMNVMEFTRAILTPRI 411
Cdd:cd14880 227 CFEVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 412 KVGRDYV--QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYT 489
Cdd:cd14880 307 RAGKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 490 NEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQEQGS 569
Cdd:cd14880 387 NEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAQLQTRIESALA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 570 HSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiQRASFYDSVSGLH 649
Cdd:cd14880 464 GNPCLGHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPAN----PEEKTQEEPSGQS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 650 EPPVdrivgldqvtgmtetafgsayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQ 729
Cdd:cd14880 540 RAPV----------------------------LTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQ 591
|
650 660 670
....*....|....*....|....*....|....*
gi 1907083610 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 |
4.32e-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: 383.18 E-value: 4.32e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKR-HEMPPHIYAISESAYRCMLQDREDQSILC 176
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 177 TGESGAGKTENTKKVIQYLAHVASShKGRKDHNIPQESPKpvkpqgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFI 256
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSS-NQQQNNNNNNNNNS-------IEKDILTSNPILEAFGNSRTTKNHNSSRFGKFL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 257 RINFDVTGYIV-GANIETYLLEKSR-AVRQAKDERTFHIFYQLLSGAGehlKSDLLLEGFNN----YRFL---------- 320
Cdd:cd14906 153 KIEFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGAS---KDERSKWGLNNdpskYRYLdarddvissf 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 321 ----SNGYIPIPGQQDKD-NFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKL---C 392
Cdd:cd14906 230 ksqsSNKNSNHNNKTESIeSFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTASLesvS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 393 HLLGMNVMEFTRAILTPRIKV-GRDYVQ-KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDR----------TKRQ 460
Cdd:cd14906 310 KLLGYIESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 461 GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPANppG 540
Cdd:cd14906 390 NNLFIGVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--G 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 541 VLALLDEECWFPKATDKTFVEKLVQEQgsHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQS 620
Cdd:cd14906 467 ILSLLDDECIMPKGSEQSLLEKYNKQY--HNTNQYYQRTLAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLAS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 621 SDRFVAELWKdeiqtiqrasfydsvsglheppvdrivglDQVTGMTETafgsayKTKKGMFRTVGQLYKESLTKLMATLR 700
Cdd:cd14906 545 SNFLKKSLFQ-----------------------------QQITSTTNT------TKKQTQSNTVSGQFLEQLNQLIQTIN 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 701 NTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPN 765
Cdd:cd14906 590 STSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDM 654
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
99-802 |
6.42e-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: 366.44 E-value: 6.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYS-GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRG-KKRHEMPPHIYAISESAYRCM-LQDREDQSIL 175
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhNIPQESPKpvkpqGELERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSS----NTSQRSIA-----DKIDENLKWSNPVMESFGNARTVRNDNSSRFGKY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 256 IRINFD-VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDL-LLEGFNNYRFLSNGYI----PIPG 329
Cdd:cd14875 152 IKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTfvrrGVDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 330 Q--QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtDQASMPENTVAQKLCHLLGMNVMEFTRAIL 407
Cdd:cd14875 232 KtlDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 408 tprIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD-RTKRQGASFIGILDIAGFEIFELNSFEQLCI 486
Cdd:cd14875 311 ---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 487 NYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIErpANPPGVLALLDEECWFPKATDKTFVEKLVQE 566
Cdd:cd14875 388 NYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 567 QGSHSK-FQKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRAsfydsv 645
Cdd:cd14875 465 WANKSPyFVLPKSTIPN-QFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRK------ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 646 sglheppvdrivgldqvtgmtetafgsayktkkgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHL 725
Cdd:cd14875 538 ------------------------------------QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLL 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 726 VLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGK--QACERMIRALE-----LDPNlYRIGQSK 798
Cdd:cd14875 582 VGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTK 660
|
....
gi 1907083610 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 |
1.66e-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: 364.98 E-value: 1.66e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRH-----EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 173 SILCTGESGAGKTENTKKVIQYLAHVASSHkgrkdhnipqespkpvkpQGELERQLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTS------------------STDVQSLILGSNPLLESFGNAKTLRNNNSSRF 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 253 GKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYI-PIPGQQ 331
Cdd:cd14886 143 GKFIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGID 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 332 DKDNFQETMEAMHIMgFSHEEILSMLKVVSSVLQFGNISFKKERN--TDQASMPENTVA-QKLCHLLGMNVMEFTRAILT 408
Cdd:cd14886 223 DQKEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIIT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 409 PRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRqgasFIGILDIAGFEIFELNSFEQLC 485
Cdd:cd14886 302 KVVVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfdADARP----WIGILDIYGFEFFERNTYEQLL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 486 INYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIERPANppGVLALLDEECwfpkatdktfvekLVQ 565
Cdd:cd14886 378 INYANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQC-------------LIQ 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 566 eQGSHSKFQKPRQLKDKAD-----------FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiq 634
Cdd:cd14886 442 -TGSSEKFTSSCKSKIKNNsfipgkgsqcnFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSD--- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 635 tiqrasfydsvsglheppvdrivgLDQVTGMTetafgsayktkKGMFrtVGQLYKESLTKLMATLRNTNPNFVRCIIPNH 714
Cdd:cd14886 518 ------------------------IPNEDGNM-----------KGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQ 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 715 EKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT--PNAIPKGFMDGKQACERMIRALELDPNLY 792
Cdd:cd14886 561 DKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDY 640
|
730
....*....|
gi 1907083610 793 RIGQSKIFFR 802
Cdd:cd14886 641 RIGKTKVFLR 650
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
99-759 |
5.93e-109 |
|
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276864 [Multi-domain] Cd Length: 717 Bit Score: 365.57 E-value: 5.93e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMY----------RGKKRHEMPPHIYAISESAYRCMLQ 167
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydhnsqfgdRVTSTDPREPHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 168 DREDQSILCTGESGAGKTENTKKVIQYLAhVASSHKGRKDHNIPQESPKPVKPQGELERQLLQANPILESFGNAKTVKND 247
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFA-VHCGTGNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRND 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 248 NSSRFGKFIRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-----AGEHLKSDLLLEGFNNYRFLS 321
Cdd:cd14899 160 NSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 322 NGYIPI--PGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKK--ERNTDQASMPENTVAQ-------- 389
Cdd:cd14899 240 QSLCSKrrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 390 --KLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRT---------- 457
Cdd:cd14899 320 ftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 458 ----KRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCIDLIE 533
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 534 RpaNPPGVLALLDEECWFPKATDKTFVEKL---VQEQGSHSKFQKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLN 610
Cdd:cd14899 479 H--RPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFC 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 611 DNVATLLHQSSDRFvaelwkdeIQTIQRASFYDSVSGLHEppVDRIVGLDQVTGMTETAFGSayktkkgmfrtVGQLYKE 690
Cdd:cd14899 557 ESAAQLLAGSSNPL--------IQALAAGSNDEDANGDSE--LDGFGGRTRRRAKSAIAAVS-----------VGTQFKI 615
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 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 |
7.37e-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: 324.68 E-value: 7.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYS--------GLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDRE 170
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 171 DQSILCTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpVKPQGeLERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHG-------------ADSQG-LEARLLQSGPVLEAFGNAHTVLNANSS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 251 RFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFlsngyipipgq 330
Cdd:cd14887 147 RFGKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPEST----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 331 qDKDNFQETMEAMHIMGFSHEEIlsmLKVVSSVLQFGNISFKKERNTDQASMPENT--------VAQKLCHLL------- 395
Cdd:cd14887 216 -DLRRITAAMKTVGIGGGEQADI---FKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclss 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 396 GMNVMEFTRAILT--------PRIKVGRDYV------------QKAQTKEQADFAVEALAKATYERLFRWLVHRINKALD 455
Cdd:cd14887 292 GLKVTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 456 RTKR-------------QGASFIGILDIAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFI 519
Cdd:cd14887 372 RSAKpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQD 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 520 --DFGLDLQPCIDLIERPAN---------------------PPGVLALLDE------ECWFPKATDKTFVEKLVQEQGSH 570
Cdd:cd14887 452 csAFPFSFPLASTLTSSPSStspfsptpsfrsssafatspsLPSSLSSLSSslssspPVWEGRDNSDLFYEKLNKNIINS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 571 SKFQK--PRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLhQSSDRFVaelwkdeiqtiqrasfydsvsgl 648
Cdd:cd14887 532 AKYKNitPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYT----------------------- 587
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 649 heppvdRIVGLDQVTGMtetafgSAYKTKKgmfRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLD 728
Cdd:cd14887 588 ------RLVGSKKNSGV------RAISSRR---STLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHR 652
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 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 |
4.96e-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: 319.88 E-value: 4.96e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 96 LNEASVLHNLKDRYYSGLIYTY---SGLfcVVINPYKNLPIYSENIIEMYR-------GKKRHEMPPHIYAISESAYRCM 165
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 166 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVaSSHkgrkdhnipqeSPKPVKpqgeLERQLLQANPILESFGNAKTVK 245
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRL-SSH-----------SKKGTK----LSSQISAAEFVLDSFGNAKTLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 246 NDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFL--SNG 323
Cdd:cd14879 143 NPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasYGC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 324 Y--IPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMpENT-VAQKLCHLLGMN 398
Cdd:cd14879 223 HplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFtyDHEGGEESAVV-KNTdVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 399 VMEFtRAILTPRIK-VGRD----YVQKAQTKEQADfaveALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGF 473
Cdd:cd14879 302 PEDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGF 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 474 EIF---ELNSFEQLCINYTNEKLQ-----QLFNHTMFILEQEEYQREGIEWNfidfglDLQPCIDLIERPanPPGVLALL 545
Cdd:cd14879 377 QNRsstGGNSLDQFCVNFANERLHnyvlrSFFERKAEELEAEGVSVPATSYF------DNSDCVRLLRGK--PGGLLGIL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 546 DEEC-WFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD---FCIIHYAGKVDYKADEWLMKNMDPLndnvatllhqSS 621
Cdd:cd14879 449 DDQTrRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SP 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 622 DrFVAelwkdeiqtiqrasfydsvsglheppvdrivgldqvtgmtetafgsayktkkgMFRTVGQLyKESLTKLMATLRN 701
Cdd:cd14879 519 D-FVN-----------------------------------------------------LLRGATQL-NAALSELLDTLDR 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 702 TNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgFMDGKQACERM 781
Cdd:cd14879 544 TRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCA 617
|
730 740
....*....|....*....|
gi 1907083610 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 |
3.19e-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: 3.19e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNlpIYSENIIEMYRGKKRHeMPPHIYAISESAYRCMLQdREDQSILCTGE 179
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVASSHKgrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTT-------------------SIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDvtGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDlllegFNNYRFLSNGYIPIPgqQDKDNFQET 339
Cdd:cd14898 139 FD--GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTAGNKESIV--QLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 340 MEAMHIMGFSHeeILSMLKVVSSVLQFGNISFKKERNTDQASmpeNTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQ 419
Cdd:cd14898 210 CSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVNDGILKLQR---NESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 420 KAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTkrqGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 499
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 500 TMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLvqeqgshSKFQKPRqL 579
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKI-------KKYLNGF-I 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 580 KDKADFCII--HYAGKVDYKADEWLMKNMDplndnvatllhqssdrfvaelwkdeiqtiqrasfydsvsglheppvdriv 657
Cdd:cd14898 430 NTKARDKIKvsHYAGDVEYDLRDFLDKNRE-------------------------------------------------- 459
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 658 gldqvtGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLE 737
Cdd:cd14898 460 ------KGQLLIFKNLLINDEGSKEDLVKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILE 533
|
650 660
....*....|....*....|....*....
gi 1907083610 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 |
2.51e-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: 309.44 E-value: 2.51e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR---GKKRHEMPPHIYAISESAYRCMLQDREDQSIL 175
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 176 CTGESGAGKTENTKKVIQYLAHVASSHKGrkdhnipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSSRFGKF 255
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT------------------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 256 IRINF-DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGY----IPIPGQ 330
Cdd:cd14878 143 FELQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMredvSTAERS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 331 QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPR 410
Cdd:cd14878 223 LNREKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDI 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 411 IKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKAL---DRTKRQGASFIGILDIAGFEIFELNSFEQLCIN 487
Cdd:cd14878 303 QYFKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 488 YTNEKLQQLFNHTMFILEQEEYQREGIewnfidfgldlqpCIDLIERPAN-----------PPGVLALLDEECWFPKATD 556
Cdd:cd14878 383 MTNEKMHHYINEVLFLQEQTECVQEGV-------------TMETAYSPGNqtgvldfffqkPSGFLSLLDEESQMIWSVE 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 557 KTFVEKL--VQEQGSHSKFQKPRQ-------LKDK-ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVA 626
Cdd:cd14878 450 PNLPKKLqsLLESSNTNAVYSPMKdgngnvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVIN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 627 ELWKDEIQTIqrASfydsvsglheppvdrivgldqvtgmtetafgsayktkkgmfrtvgQLYKeSLTKLMATLRNTNPNF 706
Cdd:cd14878 530 HLFQSKLVTI--AS---------------------------------------------QLRK-SLADIIGKLQKCTPHF 561
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 707 VRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKgfmDGKQACERMIRALE 786
Cdd:cd14878 562 IHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLGE---KKKQSAEERCRLVL 638
|
730
....*....|....*...
gi 1907083610 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 |
2.04e-86 |
|
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: 297.31 E-value: 2.04e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYseniIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAhvasshkgrkdhnipqespKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRI 258
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL-------------------SGVKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKI 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 259 NFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQE 338
Cdd:cd14937 138 ELDEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 339 TMEAMHIMGFsHEEILSMLKVVSSVLQFGNISFK---KERNTDQASMPENT--VAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14937 218 LMISFDKMNM-HDMKDDLFLTLSGLLLLGNVEYQeieKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTI 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 414 GRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14937 297 ANQKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 494 QQLFNHTMFILEQEEYQREGIEWNFIDFGLDlQPCIDLIERPANppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF 573
Cdd:cd14937 376 HSIYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKY 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 574 QKPRQLKDKaDFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDeiqtiqrASFYDSVsglheppv 653
Cdd:cd14937 452 ASTKKDINK-NFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYED-------VEVSESL-------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 654 drivgldqvtgmtetafgsayktkkGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCN 733
Cdd:cd14937 516 -------------------------GRKNLITFKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSL 570
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 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 |
1.43e-78 |
|
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: 275.63 E-value: 1.43e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYRGKKRHE-------MPPHIYAISESAYRCMLQDRE 170
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 171 DQSILCTGESGAGKTENTKKVIQYLAHVasshKGRKDHNipqespkpvkpqgELERQLLQANPILESFGNAKTVKNDNSS 250
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI----QTDSQMT-------------ERIDKLIYINNILESMSNATTIKNNNSS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 251 RFGKFIRINFD---------VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG-AGEHLKSDLLLEGFNNYRFL 320
Cdd:cd14884 144 RCGRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 321 --------------------SNGYIPIPGQQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKkerntdqa 380
Cdd:cd14884 224 npdeshqkrsvkgtlrlgsdSLDPSEEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 381 smpentvaqKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQ 460
Cdd:cd14884 296 ---------AAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEK 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 461 GA-----------SFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGlDLQPCI 529
Cdd:cd14884 367 DEsdnediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTL 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 530 DLIERpanppgVLALLDE-----ECWFPKATDKTFV-----EKLVQEQGSHSK-FQKPR--------QLKDKADFCIIHY 590
Cdd:cd14884 446 IFIAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHdadgtakkQNIKKNIFFIRHY 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 591 AGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAElwkdeiqtiqrasfydsvsglheppvdrivgldqvtgmtetaf 670
Cdd:cd14884 520 AGLVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE------------------------------------------- 556
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 671 gSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRI 750
Cdd:cd14884 557 -ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKI 635
|
....
gi 1907083610 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 |
4.47e-75 |
|
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: 263.90 E-value: 4.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYknlpiyseniieMYRGKKRH-------EMPPHIYAISESAYRCMLQDREDQ 172
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTltstrssPLAPQLLKVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 173 SILCTGESGAGKTENTKKVIQYLAHVASShkgrkdhnipqespkpvKPQGELERQLLQANPILESFGNAKTVKNDNSSRF 252
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-----------------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 253 GKFIRINFdVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFN--NYRFLSNGYIPIPGQ 330
Cdd:cd14881 133 GHFIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEA 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 331 QDKDNFQETMEAMHIMGFsheEILSMLKVVSSVLQFGNISF--KKERNTDQASMPE-NTVAQklchLLGMNVMEFTRAiL 407
Cdd:cd14881 212 EDAARFQAWKACLGILGI---PFLDVVRVLAAVLLLGNVQFidGGGLEVDVKGETElKSVAA----LLGVSGAALFRG-L 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 408 TPRIK-VGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKaldrTKRQGAS--------FIGILDIAGFEIFEL 478
Cdd:cd14881 284 TTRTHnARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANS----LKRLGSTlgthatdgFIGILDMFGFEDPKP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 479 NSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNF-IDFgLDLQPCIDLIErpANPPGVLALLDEECwFPKATDK 557
Cdd:cd14881 360 SQLEHLCINLCAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAE 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 558 TFVEKLVQEQGSHSKFQKPRQLKDKAdFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSdrfvaelwkdeiqtiq 637
Cdd:cd14881 436 SYVAKIKVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN---------------- 498
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 638 rasfydsvsglheppvdrivgldqvtgmteTAFGsayktkkgmFRTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKR 717
Cdd:cd14881 499 ------------------------------CNFG---------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTET 539
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 718 AGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPKGFMDGKQACERMIR--ALELDP 789
Cdd:cd14881 540 PNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPP 613
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
100-802 |
6.97e-71 |
|
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: 252.71 E-value: 6.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLP-IYSENIIEMYrgKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAHV-ASSHKGRKDHnipqespkpvkpqgelerqLLQANPILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTdLSRSKYLRDY-------------------ILESGIILESFGHASTDSNHNSSRWGKYFE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSN-GYIPIPGQQDKDNF 336
Cdd:cd14905 141 MFYSLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNtdQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRD 416
Cdd:cd14905 221 DRLKMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 417 YVQKAqtkeqadfavEALAKATYERLFRWLVHRINKALDRTkrQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQL 496
Cdd:cd14905 299 AVENR----------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQI 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 497 FNHTMFILEQEEYQREGIEW-NFIDFGlDLQPCIDLIERpanppgVLALLDEECWFPKATDKTFVEKLVQEQGSHSKF-Q 574
Cdd:cd14905 367 YLQTVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK------IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFgK 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 575 KPRQlkdkadFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVaeLWKDEIQTIQRA-----SFYDSVSGLH 649
Cdd:cd14905 440 KPNK------FGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL--FSRDGVFNINATvaelnQMFDAKNTAK 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 650 EPPVDRIVGL--------DQVTGMTETAFGSAYKTKKGMFRTVGQLYKESLTKLMATLRNTNPN--FVRCIIPNHEKRAG 719
Cdd:cd14905 512 KSPLSIVKVLlscgsnnpNNVNNPNNNSGGGGGGGNSGGGSGSGGSTYTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHL 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 720 KLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAipKGFMD-GKQACERMIRALELDPNLYRIGQSK 798
Cdd:cd14905 592 TFDVKSVNEQIKSLCLLETTRIQRFGYTIHYNNKIFFDRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVGNTK 669
|
....
gi 1907083610 799 IFFR 802
Cdd:cd14905 670 IFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
99-767 |
3.62e-69 |
|
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: 246.32 E-value: 3.62e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 99 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYrgkkrhemppHIYAISESAYRCMLQDRED-QSILCT 177
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 178 GESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQEspkpvkpqgelerqllqanpILESFGNAKTVKNDNSSRFGKFIR 257
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAIES--------------------VFKSFGCAKTLKNDEATRFGCSID 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 258 INFDvTGYIVGANIE-TYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNF 336
Cdd:cd14874 131 LLYK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHF 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 337 QETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTD-QASMPE--NTVAQKLCHLLGMNVMEFTRAILTPRIKV 413
Cdd:cd14874 210 KHLEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNvEQDVVEigNMSEVKWVAFLLEVDFDQLVNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 414 GrdyvqKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGAsfIGILDIAGFEIFELNSFEQLCINYTNEKL 493
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 494 QQLFNHTMFILEQEEYQREGIEWNF-IDFGLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSK 572
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 573 FQKPRQlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQrasfydsvsglhepp 652
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTS--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 653 vDRIVgldqvtgmtetafgsayktkkgmfrTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRC 732
Cdd:cd14874 505 -DMIV-------------------------SQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKN 558
|
650 660 670
....*....|....*....|....*....|....*
gi 1907083610 733 NGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 767
Cdd:cd14874 559 LLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
102-801 |
5.14e-67 |
|
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: 242.95 E-value: 5.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 102 LHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKR----------HEMPPHIYAISESAYRCMLQDRED 171
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 172 QSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKpqgeleRQLLQANPILESFGNAKTVKNDNSSR 251
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPDSEGASGVLHPIG------QQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 252 FGKFIRINFDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAgEH---LKSDLLL-EGFNNYRFLSNGyIPI 327
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGV-QHdptLRDSLEMnKCVNEFVMLKQA-DPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 328 PGQ--QDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISF--KKERNTDQASMPENTVAQ-KLCHL-------L 395
Cdd:cd14893 236 ATNfaLDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpDPEGGKSVGGANSTTVSDaQSCALkdpaqilL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 396 GMNVMEFTRAILTPRIKVGRDYVQ---------KAQTKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQG- 461
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQFFSKdgnktvsslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNi 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 462 ---ASFIGILDIAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWNFIDFGLDLQPCI 529
Cdd:cd14893 396 vinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 530 DLIERPanPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKAD------------FCIIHYAGKVDYK 597
Cdd:cd14893 476 QLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYN 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 598 ADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQTIQRASFYDSVSGlheppvdrivgldqvTGMTETAFG----SA 673
Cdd:cd14893 554 GKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGAAQMAAASSEKAAKQTEE---------------RGSTSSKFRksasSA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 674 YKTKKGMFRTVGQLYKESlTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQ 753
Cdd:cd14893 619 RESKNITDSAATDVYNQA-DALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYG 697
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 754 EFRQRYeiltpnaipKGFMDGKQACERMIRALE----LDPNLYRIGQSKIFF 801
Cdd:cd14893 698 HFFRRY---------KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKVYL 740
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
100-762 |
1.03e-61 |
|
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: 224.62 E-value: 1.03e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGE 179
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 180 SGAGKTENTKKVIQYLAHVasshkGRKDHNIPQespkpvkpqgelerQLLQANPILESFGNAKTVKNDNSSRFGKFIRIN 259
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATG--------------RVESSIKAILALVNAGTPLNADSTRCILQYQLT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 260 FDVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSG--AGEHLKsDLLLEGFNNYRFLSngyIP--IPG------ 329
Cdd:cd14882 143 FGSTGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLR---IPpeVPPsklkyr 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 330 ----QQDKDNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKerNTDQASMPENTVAQKLCHLLGMNVMEFTRA 405
Cdd:cd14882 219 rddpEGNVERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 406 ILTPRIKVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKrqgASF-----IGILDIAGFEIFELNS 480
Cdd:cd14882 297 LTNYCLIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 481 FEQLCINYTNEKLQQLFNHTMFI---LEQEEYQREGIEWNFIDFGLDLQPCIdlierpANPPGVLALLDEECwfPKATDK 557
Cdd:cd14882 374 LEQLMVNTLNEQMQYHYNQRIFIsemLEMEEEDIPTINLRFYDNKTAVDQLM------TKPDGLFYIIDDAS--RSCQDQ 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 558 TFVEKLVQEQgsHSKFQKPrqlKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEiqtiq 637
Cdd:cd14882 446 NYIMDRIKEK--HSQFVKK---HSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNS----- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 638 rasfydsvsglheppvdrivgldQVTGMtetafgsayKTKKGMFRTVgqlykeSLTKLMATLRNTNP---NFVRCIIPNH 714
Cdd:cd14882 516 -----------------------QVRNM---------RTLAATFRAT------SLELLKMLSIGANSggtHFVRCIRSDL 557
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907083610 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 |
6.60e-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: 6.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 121 FCVVINPYKNLPIYSEN-IIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 199
Cdd:cd01363 1 VLVRVNPFKELPIYRDSkIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 200 SSHKGRKDHNIpqeSPKPVKPQGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGY 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 |
2.99e-59 |
|
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: 218.94 E-value: 2.99e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 100 SVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYR-GKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 178
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 179 ESGAGKTENTKKVIQYLAH-VASSHKGRKDHNIPQESPKPV----KPQGELERQLLQANPILESFGNAKTVKNDNSSRFG 253
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYqVKGSRRLPTNLNDQEEDNIHNeentDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 254 KFIRINFDvTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDK 333
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 334 DNFQETMEAMHIMGFSHEEILSMLKVVSSVLQFGNI----SFKKE----------------------RNTDQASMPENTV 387
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkAFRKKsllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 388 AQKL-CHLLGMNVMEFTRAILTPRIkVGRDYVQKAQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKR--QGASF 464
Cdd:cd14938 321 NLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 465 IGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANppGVLAL 544
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE--GSLFS 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 545 LDEECWFPKATDKTFVEKLVQEQGSHSKF--QKPRQLKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSD 622
Cdd:cd14938 478 LLENVSTKTIFDKSNLHSSIIRKFSRNSKyiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSEN 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 623 RFVAELwkdeiqtiqrASFYDSVSGLHEPPVDRIVGLDQVTGMtetaFGSAYKTKKGMFRTvgqLYKESLTKLMATLRNT 702
Cdd:cd14938 558 EYMRQF----------CMFYNYDNSGNIVEEKRRYSIQSALKL----FKRRYDTKNQMAVS---LLRNNLTELEKLQETT 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 703 NPNFVRCIIPNHEKRA-GKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPnaipkgfmDGKQACERM 781
Cdd:cd14938 621 FCHFIVCMKPNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEAL 692
|
730
....*....|....*....
gi 1907083610 782 IRALELDPNLYRIGQSKIF 800
Cdd:cd14938 693 IKSYQISNYEWMIGNNMIF 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1036-1892 |
1.35e-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: 148.67 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1036 EDRIAECSSQL------AEEEEKAKNL-AKIRNKQ-EVMISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQA 1107
Cdd:TIGR02168 192 EDILNELERQLkslerqAEKAERYKELkAELRELElALLVLRLEELREELEELQEELKEAEEELE----ELTAELQELEE 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1108 QVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1187
Cdd:TIGR02168 268 KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1188 DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATaLEELSEQLEQAKRFKANLEKNKQGLETDNkel 1267
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEI--- 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1268 acevkvlqqvkaeSEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDaaglESQ 1347
Cdd:TIGR02168 424 -------------EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1348 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVdddlgTIESLEEAKKk 1427
Cdd:TIGR02168 487 LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAV-----VVENLNAAKK- 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1428 llkDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAeekGISARYAEERDRAEA 1507
Cdd:TIGR02168 561 ---AIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALS---YLLGGVLVVDDLDNA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1508 EAREKETKAL---------------SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1572
Cdd:TIGR02168 635 LELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1573 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQnEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1652
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL-EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1653 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1732
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1733 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSA-- 1810
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtl 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1811 ------AQKSDNARQQLERQNKELKAKLQELeGAVKSKFKATISALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEK 1880
Cdd:TIGR02168 954 eeaealENKIEDDEEEARRRLKRLENKIKEL-GPVNLAAIEEYEELKERYDFLTAQKEdlTEAKEtlEEAIEEIDREARE 1032
|
890
....*....|..
gi 1907083610 1881 KLKEIFMQVEDE 1892
Cdd:TIGR02168 1033 RFKDTFDQVNEN 1044
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1162-1917 |
5.37e-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: 146.74 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1162 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ----QELRTKREQE--------VAELKKALE--DETKNHEAQ 1224
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEdilNELERQLKSLERQaekaERYKELKAELrelelallVLRLEELREelEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1225 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDR 1304
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1305 LRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQE------ETRQKLN-LSSRIRQLEEEKN 1377
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETlrskvaQLELQIAsLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1378 SLQE-----QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKkkllkdvEALSQRLEEKVLAYDKLEKT 1452
Cdd:TIGR02168 411 RLEDrrerlQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL-------EELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1453 KNRLQQELDDLTVDLDHQRQI---VSNLEKKQKKF--------DQLLAEEKGISARYAEERDRAEAEAREKETKAL---- 1517
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGYEAAIEAALGGRLQAVVVENLNAAKkaia 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1518 SLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL--- 1594
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrp 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1595 ---------------------RLEVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1652
Cdd:TIGR02168 644 gyrivtldgdlvrpggvitggSAKTNSSILERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1653 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1732
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1733 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNdrfrkttLQVDTLNTELAAERSAAQ 1812
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA-------AEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1813 KSDNARQQLERQNKELKAKLQELEGAVKSKFKAtISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1892
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESK-RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
810 820
....*....|....*....|....*.
gi 1907083610 1893 -RRHADQYKEQMEKANARMKQLKRQL 1917
Cdd:TIGR02168 956 aEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1036-1889 |
1.12e-30 |
|
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: 132.50 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1036 EDRIAECSSQLAEEEEKAKNLAKIRNKQEvMISDLEERLKKEE-----KTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1110
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1111 ELKVQLTKKEEELQGALARGDDETLHKNNALKVA-RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDT 1189
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1190 LDTTAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELS---EQLEQAKRFKANLEKNKQGLETDNKE 1266
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDL----RAELEEVDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1267 LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1346
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1347 QLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearknlEKQVLALQSQLADTKKK--VDDDLGTIESLEEA 1424
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----------ERYATAIEVAAGNRLNNvvVEDDAVAKEAIELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1425 KKKLL-----------KDVEALSQRLEEKV---LAYDKLE---KTKNRLQQELDDLTV--DLDHQRQIVSN--------- 1476
Cdd:TIGR02169 568 KRRKAgratflplnkmRDERRDLSILSEDGvigFAVDLVEfdpKYEPAFKYVFGDTLVveDIEAARRLMGKyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1477 -LEKKQKKFDQLLAEEKGISaRYAEERDRAEAEAREKEtkalSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG 1555
Cdd:TIGR02169 648 lFEKSGAMTGGSRAPRGGIL-FSRSEPAELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1556 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErdlQTRDEQNEEKKRLLLKQVRELEAE 1635
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH---KLEEALNDLEARLSHSRIPEIQAE 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1636 LEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKS 1715
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-------EEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1716 LEAEILQLQEELAsserarrHAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttl 1795
Cdd:TIGR02169 873 LEAALRDLESRLG-------DLKKERDELEAQL-------RELERKIEELEAQIEKKRKRLSELKAKLEALEEE------ 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1796 qvdtlNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE--GAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1873
Cdd:TIGR02169 933 -----LSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRalEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
890
....*....|....*.
gi 1907083610 1874 LVRRTEKKLKEIFMQV 1889
Cdd:TIGR02169 1008 RIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1216-1965 |
3.68e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 130.95 E-value: 3.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1216 DETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA--NLEKNKQG--LETDNKELACEVKVLQQVKAESEHKRKKLDAQ 1291
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKElkAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1292 VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQ 1371
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1372 LEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK 1451
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1452 TKNRLQQELDDLTVDLDHQR--QIVSNLEKKQKKFDQLLAEEKGISARYAE---ERDRAEAEAREKETKALSLARALEEA 1526
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAEleELEEELEELQEELERLEEALEELREELEEaeqALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1527 LEAKEEFERQNKQ----------------------------LRADMEDL-MSSKDDVGKNVHELEKS---KRALEQQVEE 1574
Cdd:TIGR02168 502 EGFSEGVKALLKNqsglsgilgvlselisvdegyeaaieaaLGGRLQAVvVENLNAAKKAIAFLKQNelgRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1575 MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTR----------DEQNEEKKRLLLkqvRELEAELEDER---- 1640
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvvddlDNALELAKKLRP---GYRIVTLDGDLvrpg 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1641 ----KQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1716
Cdd:TIGR02168 659 gvitGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARL 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1717 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQleeeleeEQSNMELLNDRFRKTTLQ 1796
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-------LKEELKALREALDELRAE 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1797 VDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSkFKATISALEAKIGQLEEQLEQEAKERAAANKLVR 1876
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES-LAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1877 RTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANAS-RRKLQRELDDA-------TEANEGL 1948
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAealenkiEDDEEEA 970
|
810
....*....|....*..
gi 1907083610 1949 SREVSTLKNRLRRGGPI 1965
Cdd:TIGR02168 971 RRRLKRLENKIKELGPV 987
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1085-1729 |
1.03e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.29 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1085 EKAKRKLDGETTDL---QDQIAELQAQVDELKVQ---------LTKKEEELQGALargddetlhknnALKVARELQAQIA 1152
Cdd:COG1196 175 EEAERKLEATEENLerlEDILGELERQLEPLERQaekaeryreLKEELKELEAEL------------LLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1153 ELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknheaqiQDMRQRH 1232
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRREL 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1233 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1312
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1313 ANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKN 1392
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1393 LEKQVLALQSQLADtkkkvdddlgtieslEEAKKKLLKDVEALSQRLEEKVLAYDKLEKtKNRLQQELDDLTVDldhqrq 1472
Cdd:COG1196 475 LEAALAELLEELAE---------------AAARLLLLLEAEADYEGFLEGVKAALLLAG-LRGLAGAVAVLIGV------ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1473 ivsnlekkQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD 1552
Cdd:COG1196 533 --------EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1553 DVgKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVREL 1632
Cdd:COG1196 605 AS-DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVT-LEGEGGSAGGSLTGGSRRELLAALLEAEAELE 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1633 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEiFAQSKESEKK 1712
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE-ALEELPEPPD 761
|
650
....*....|....*..
gi 1907083610 1713 LKSLEAEILQLQEELAS 1729
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
880-1723 |
7.40e-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: 126.71 E-value: 7.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 880 RQEEELQakdeeLLKVKEKQTKVEGELEEMERKhQQLLEEKNILAEQLQaetELFAEAEEMRARLAAK-KQELEEILHDL 958
Cdd:TIGR02168 174 RKETERK-----LERTRENLDRLEDILNELERQ-LKSLERQAEKAERYK---ELKAELRELELALLVLrLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 959 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR 1038
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1039 IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTK 1118
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1119 KEEELQGALARgdDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQE 1198
Cdd:TIGR02168 405 LEARLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE------EAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1199 LRTKREQEvaelkkaleDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNK-ELACE------- 1270
Cdd:TIGR02168 477 LDAAEREL---------AQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyEAAIEaalggrl 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1271 ----VKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLqnelDNVSTLLEEAEKKGIKFAKDAAGLES 1346
Cdd:TIGR02168 548 qavvVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNI----EGFLGVAKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1347 Q------LQDTQELLQEETRQ---------------------------KLNLSSRIrqleeeknslqeqqeeeeearKNL 1393
Cdd:TIGR02168 624 GvlvvddLDNALELAKKLRPGyrivtldgdlvrpggvitggsaktnssILERRREI---------------------EEL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1394 EKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL-DHQRQ 1472
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELtELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1473 IVSNLEKKQKKFDQLLAEEKGIsARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD 1552
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1553 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAmkAQFERDLQTRDEQNEEKKRlllkqvREL 1632
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL--LRSELEELSEELRELESKR------SEL 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1633 EAELEDERKQralavaskkkmeidLKDLEAQIEAANKARDEVIKQLRklqaqmKDYQRELEEARASRDEIFAQSKESEKK 1712
Cdd:TIGR02168 914 RRELEELREK--------------LAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRR 973
|
890
....*....|.
gi 1907083610 1713 LKSLEAEILQL 1723
Cdd:TIGR02168 974 LKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1198-1889 |
1.10e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 125.82 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1198 ELRTKREQevAELKkaLEdETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKA------NLEKNKQGLETDNKELacEV 1271
Cdd:COG1196 169 KYKERKEE--AERK--LE-ATEENLERLEDILGELERQLEPLERQAEKAERYRElkeelkELEAELLLLKLRELEA--EL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1272 KVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDT 1351
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1352 QELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKD 1431
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1432 VEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEARE 1511
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE---ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1512 KETKALSLARaleealeakeefERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRaLEQQVEEMRTQLEELEDELQATED 1591
Cdd:COG1196 479 LAELLEELAE------------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRG-LAGAVAVLIGVEAAYEAALEAALA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1592 AKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR 1671
Cdd:COG1196 546 AALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1672 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANS 1751
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1752 ASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKsdnARQQLERQNKEL--- 1828
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER---ELERLEREIEALgpv 782
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1829 --KAkLQELEgavkskfkatisALEAKIGQLEEQLE--QEAKE--RAAANKLVRRTEKKLKEIFMQV 1889
Cdd:COG1196 783 nlLA-IEEYE------------ELEERYDFLSEQREdlEEAREtlEEAIEEIDRETRERFLETFDAV 836
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1067-1948 |
2.96e-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: 118.25 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1067 ISDLEERLKKEEKTRQELEKAKRKLDgettdlqdqiaELQAQVDELKVQLTKKEEElqgalargddetlhKNNALKvare 1146
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIE-----------RLDLIIDEKRQQLERLRRE--------------REKAER---- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1147 LQAQIAELQEDFESEKASR-NKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQI 1225
Cdd:TIGR02169 213 YQALLKEKREYEGYELLKEkEALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLEELNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1226 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETdnkelacevkvlQQVKAESEhkRKKLDAQVQELHAKVSEGDRL 1305
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEE------------RLAKLEAE--IDKLLAEIEELEREIEEERKR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1306 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1385
Cdd:TIGR02169 352 RDKLTEEYAELKEELEDLRAELEEVDKE-------FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1386 EEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDdltv 1465
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALE-------IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA---- 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1466 DLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEarEKETKALSLAraleealeakeeferqnkqLRADME 1545
Cdd:TIGR02169 494 EAEAQARASEERVRGGRAVEEVL--KASIQGVHGTVAQLGSVG--ERYATAIEVA-------------------AGNRLN 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1546 DLMSSKDDVGKNVHELEKSK---RALEQQVEEMRTQLEELEdelQATEDAKLRLEVNMQAMKAQFE-------RDlqTRD 1615
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagRATFLPLNKMRDERRDLS---ILSEDGVIGFAVDLVEFDPKYEpafkyvfGD--TLV 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1616 EQNEEKKRLLLKQVR--ELEAELEDE--------RKQRALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1685
Cdd:TIGR02169 626 VEDIEAARRLMGKYRmvTLEGELFEKsgamtggsRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRL 704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1686 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1765
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1766 EARIAQLEEELEEEQsnMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV------ 1839
Cdd:TIGR02169 785 EARLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIenlngk 862
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1840 KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRqLEE 1919
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIED-PKG 941
|
890 900
....*....|....*....|....*....
gi 1907083610 1920 AEEEATRANASRRKLQRELDDATEANEGL 1948
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1352-1917 |
1.36e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.80 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1352 QELLQEETRQKLNLSS-RIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1430
Cdd:COG1196 216 RELKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1431 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1510
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1511 EKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATE 1590
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-------RLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1591 DAKLRLEvnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKA 1670
Cdd:COG1196 449 EEEAELE--------EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1671 RdeVIKQLRKLQAQMKDYQRELEEARASR--------DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERD 1742
Cdd:COG1196 521 G--LAGAVAVLIGVEAAYEAALEAALAAAlqnivvedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1743 ELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLE 1822
Cdd:COG1196 599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1823 RQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQ 1902
Cdd:COG1196 679 AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPE 758
|
570
....*....|....*...
gi 1907083610 1903 M---EKANARMKQLKRQL 1917
Cdd:COG1196 759 PpdlEELERELERLEREI 776
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
875-1737 |
9.98e-25 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 113.24 E-value: 9.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 875 LLQVTRQEEELQAKDEEllkVKEKQTKVEGELEEMERkHQQLLEEKNILA--EQLQAETELFAEAEEMRARLAAKKQELE 952
Cdd:TIGR02169 179 LEEVEENIERLDLIIDE---KRQQLERLRREREKAER-YQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 953 EILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGarqKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEK 1032
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG---ELEAEIASLERSIAEKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1033 KLMEDRIAECSSQLAEEE-EKAKNLAKIRNKQEVM---ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQ 1108
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERkRRDKLTEEYAELKEELedlRAELEEVDKEFAETRDELKDYREKLE----KLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1109 VD---ELKVQLTKKEEELQGALARGDDetlhKNNALKVARE-LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1184
Cdd:TIGR02169 408 LDrlqEELQRLSEELADLNAAIAGIEA----KINELEEEKEdKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1185 ELE------DTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALE----------------ELSEQ 1242
Cdd:TIGR02169 484 ELSklqrelAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvaagnrlnnvvveddaVAKEA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1243 LEQAKRFKAN----LEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQN 1318
Cdd:TIGR02169 564 IELLKRRKAGratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF------GDTLVVEDIEAARRLMG 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1319 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklNLSSRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVL 1398
Cdd:TIGR02169 638 KYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ-----RLRERLEGLKRELSSLQSE-------LRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1399 ALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1478
Cdd:TIGR02169 706 ELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1479 KKQKKFDQLLAEEKGISARyaEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNV 1558
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQ--AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1559 HELEKSKRALEQQVEEMRTQLEELEDELQatedaklrlevnmqamkaqferDLQTRDEQNEEKKRLLLKQVRELEAELED 1638
Cdd:TIGR02169 857 ENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1639 ERKQRALAVASKKKMEIDLKDLEAQIeAANKARDEVIKQLRKLQAQMKDYQRELEE-------ARASRDEIFAQSKESEK 1711
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPK-GEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKE 993
|
890 900
....*....|....*....|....*.
gi 1907083610 1712 KLKSLEAEILQLQEELASSERARRHA 1737
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
838-1480 |
1.56e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 112.34 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 838 AKKQQQLSA-LKVLQrncaAYLKLRHWQWWRvftkvkplLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQL 916
Cdd:COG1196 212 AERYRELKEeLKELE----AELLLLKLRELE--------AELEELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 917 LEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdlesrveeeeeRNQILQNEKKKMQAHIQDLEEQLDEEEGA 996
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--------------RLEELEEELAELEEELEELEEELEELEEE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 997 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK 1076
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1077 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQE 1156
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1157 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAL 1236
Cdd:COG1196 506 FLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1237 EELSEQLEQAKRFKANLeknkqGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKL 1316
Cdd:COG1196 586 AALAAALARGAIGAAVD-----LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1317 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQ 1396
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1397 VLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALsqrleEKV--LA---YDKLEKTKNRLQQELDDLTVDLDHQR 1471
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL-----GPVnlLAieeYEELEERYDFLSEQREDLEEARETLE 815
|
....*....
gi 1907083610 1472 QIVSNLEKK 1480
Cdd:COG1196 816 EAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
890-1771 |
1.63e-24 |
|
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: 112.47 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 890 EELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEmrarlAAKKQELEEILHDLEsrVEEEEERN 969
Cdd:TIGR02169 160 DEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREK-----AERYQALLKEKREYE--GYELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 970 QILQNEKKKMQAHIqdleeqldeeegARQKLQLEKVTAE--AKIKKMEEEVLLLEDQNSKFikeKKLMEDRIAECSSQLA 1047
Cdd:TIGR02169 233 EALERQKEAIERQL------------ASLEEELEKLTEEisELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1048 EEEEKAKNLAKIrnkqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1127
Cdd:TIGR02169 298 ELEAEIASLERS-------IAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1128 ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEV 1207
Cdd:TIGR02169 371 AELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE---AKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1208 AELKKAlEDETKNHEAQIQDMRQRH---ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLqqvkaesEHK 1284
Cdd:TIGR02169 448 LEIKKQ-EWKLEQLAADLSKYEQELydlKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVL-------KAS 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1285 RKKLDAQVQELhAKVSEGDRLRVELAekankLQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLN 1364
Cdd:TIGR02169 520 IQGVHGTVAQL-GSVGERYATAIEVA-----AGNRLNNVVVEDDAVAKEAIELLK-----RRKAGRATFLPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1365 LSSRIRqleeeknslqeqqeeeeearknlEKQVLALQSQLADTKKK-------VDDDLGTIESLEEAKKKL--------- 1428
Cdd:TIGR02169 589 DLSILS-----------------------EDGVIGFAVDLVEFDPKyepafkyVFGDTLVVEDIEAARRLMgkyrmvtle 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1429 ----------------LKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK----QKKF 1484
Cdd:TIGR02169 646 gelfeksgamtggsraPRGGILFSRSEPAELQRLrerlEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEI 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1485 DQLLAEEKGISARYAEERDRAEAEAREKETKALSLARaleeALEAKEEFERQNKQLRADMEDLMSSKDDVGknVHELEKS 1564
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE----LEARIEELEEDLHKLEEALNDLEARLSHSR--IPEIQAE 799
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1565 KRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRA 1644
Cdd:TIGR02169 800 LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1645 LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE------SEKKLKSLEA 1718
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQA 958
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1719 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:TIGR02169 959 ELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1137-1912 |
3.78e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 111.36 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1137 KNNALKVARELQAQIAELQEDFESekaSRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALED 1216
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNE---SNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1217 ETKNHEAQiqdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD--NKELACEVKVLQQVKAESEHKR--------- 1285
Cdd:pfam15921 150 TVHELEAA----KCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIlvDFEEASGKKIYEHDSMSTMHFRslgsaiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1286 -KKLDAQVQELHAKV-SEGDRLRVELAEKANK----LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ---LQDTQELLQ 1356
Cdd:pfam15921 226 lRELDTEISYLKGRIfPVEDQLEALKSESQNKiellLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1357 EETRQKLnlSSRIRQLEEeknslqeqqeeeeearknLEKQVLALQSQLADTKKKVDDdlgTIESLEeaKKKLLKDVEALS 1436
Cdd:pfam15921 306 EQARNQN--SMYMRQLSD------------------LESTVSQLRSELREAKRMYED---KIEELE--KQLVLANSELTE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1437 QRLEEkvlayDKLEKTKNRLQQELDDLTVDLdHQRQIVSNLEKKQKKfdQLLAEEKGISARYAEERdraeaeaREKETKA 1516
Cdd:pfam15921 361 ARTER-----DQFSQESGNLDDQLQKLLADL-HKREKELSLEKEQNK--RLWDRDTGNSITIDHLR-------RELDDRN 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1517 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1596
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1597 EVNMQAMKAqferdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKD-----LEAQIE-----A 1666
Cdd:pfam15921 506 QEKERAIEA-------TNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDkvieiLRQQIEnmtqlV 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1667 ANKARDEVIKQLRK--LQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1744
Cdd:pfam15921 579 GQHGRTAGAMQVEKaqLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1745 ADEIANSASGKSALLDEkrrleariaqleeeleeeqsnMELLNDRFRKTTLQVDT----LNTELAAERSAAQKSDNARQQ 1820
Cdd:pfam15921 659 LNEVKTSRNELNSLSED---------------------YEVLKRNFRNKSEEMETttnkLKMQLKSAQSELEQTRNTLKS 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1821 LERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERaaanKLVRRTEKKLKEIFMQVEDERRHADQYK 1900
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAK-RGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKNKLSQELSTVATEKNKMAGEL 792
|
810
....*....|..
gi 1907083610 1901 EQMEKANARMKQ 1912
Cdd:pfam15921 793 EVLRSQERRLKE 804
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
105-743 |
1.17e-23 |
|
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: 109.45 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 105 LKDRYYSGLIYTYSGLFCV-VINPYKNL------PIYSENIIEMYRGKKRHE--MPPHIYAISE---------------- 159
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 160 ----SAYRCMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPQESPKPVKPQGEL----------- 224
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPALSKGSEETCKVSGSTRQPKIKLftsstkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 225 ----------------------------------------------------------------ERQL------------ 228
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyeklehledEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 229 ----LQANPILESFGNAKTVKNDNSSRFGKF--IRINFDVTGY---IVGANIETYLLEKSRAVRQA------KDERTFHI 293
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 294 FYQLLSGAGEH-----LKSDLLLEGFN--NYRFLSNGYIPIPG--------QQDKDNFQETMEAMHIMGFSHEEILSMLK 358
Cdd:cd14894 326 LYAMVAGVNAFpfmrlLAKELHLDGIDcsALTYLGRSDHKLAGfvskedtwKKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 359 VVSSVLQFGNISFKKERNTDQASMPEN---TVAQKLCHLLGMNVME-FTRAILTPRIKV--GRDYVQKAQTKEQADFAVE 432
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGSVEkLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 433 ALAKATYERLFRWLVHRINKAL-------DRTKRQ---------GASFIGILDIAGFEIFELNSFEQLCINYTNEKLQql 496
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 497 fnhtmfileQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKAT----------DKTFVEKLVQE 566
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 567 QGSHSKfQKPRQLKDKA----------DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDEIQti 636
Cdd:cd14894 635 NSSRLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSQ-- 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 637 qrasfydsvsglheppvdrivgLDQVTGMTETAFGSAYKTKKGMFRTVGQlYKESLTKLMATLRNTNPNFVRCIIPNHEK 716
Cdd:cd14894 712 ----------------------LGWSPNTNRSMLGSAESRLSGTKSFVGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKK 768
|
810 820
....*....|....*....|....*..
gi 1907083610 717 RAGKLDPHLVLDQLRCNGVLEGIRICR 743
Cdd:cd14894 769 QPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
877-1575 |
2.93e-23 |
|
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: 108.61 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 956
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 957 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ-----LEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1031
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1032 KKLMEDRIAECSSQLAEEEEK----AKNLAKIRNKQEvMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI---AE 1104
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQAldaaERELAQLQARLD-SLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIsvdEG 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1105 LQAQVDelkvqlTKKEEELQGALARGDD------ETLHKNNALKVA---------RELQAQIAELQEDFESEKASRNKAE 1169
Cdd:TIGR02168 535 YEAAIE------AALGGRLQAVVVENLNaakkaiAFLKQNELGRVTflpldsikgTEIQGNDREILKNIEGFLGVAKDLV 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1170 KQKRDLSEELEAL--KTELEDTLDTTAAQQEL-------------------------------RTKREQEVAELKKALEd 1216
Cdd:TIGR02168 609 KFDPKLRKALSYLlgGVLVVDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIE- 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1217 ETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELH 1296
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1297 AKVSEGDRLRVELAEKANKLQNELDNVSTLLEEaekkgikfakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEK 1376
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKA--------------LREALDELRAELTLLNEEAANLRERLESLERRI 833
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1377 NSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL 1456
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEEL-------IEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1457 QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFER 1535
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGP 986
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1907083610 1536 QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1575
Cdd:TIGR02168 987 VNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1162-1771 |
1.07e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.56 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1162 KASRNKAEKQKRDLSEELEALK---TELEDTLDTTAAQ-------QELRTKREQEVAELKKALEDETKNHEAQIQDMRQR 1231
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEdilGELERQLEPLERQaekaeryRELKEELKELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1232 HATALEELSEQLEQAkrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1311
Cdd:COG1196 251 LEAELEELEAELAEL---EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1312 KANKLQNELDNVSTL----------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQE 1381
Cdd:COG1196 328 LEEELEELEEELEELeeeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1382 QQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1461
Cdd:COG1196 408 AEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1462 DLTVDLDHQRQIVSNLEKKQK--KFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA----RALEEALEAKEEFER 1535
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEgvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALqnivVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1536 QNKQLRA------DMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER 1609
Cdd:COG1196 568 AAKAGRAtflpldKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1610 DLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1689
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1690 RELEEARASRDEIFAQSK----ESEKKLKSLEAEILQLQEELASSERARRH-------AEQERDELADEIANSASGKSAL 1758
Cdd:COG1196 728 EQLEAEREELLEELLEEEelleEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDL 807
|
650
....*....|...
gi 1907083610 1759 LDEKRRLEARIAQ 1771
Cdd:COG1196 808 EEARETLEEAIEE 820
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1345-1961 |
3.20e-21 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 101.79 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1345 ESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEeeeeARKNLEKQVLALQSQLADTKKKVDDDLGTIES---- 1420
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETELCAEAEEMRARLAARKQELEEILHELESrlee 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1421 -------LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEekg 1493
Cdd:pfam01576 87 eeersqqLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISE--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1494 isaryaeerdrAEAEAREKETKALSLARALEealeakeeferQNKQLRADMEDLMSSKDdvgKNVHELEKSKRALEQQVE 1573
Cdd:pfam01576 164 -----------FTSNLAEEEEKAKSLSKLKN-----------KHEAMISDLEERLKKEE---KGRQELEKAKRKLEGEST 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1574 EMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKM 1653
Cdd:pfam01576 219 DLQEQIAELQAQIAELRAQLAKKEEELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1654 EIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELE-EARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1732
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEeETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1733 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQ 1812
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1813 KSDNARQQLERQNKELKAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDE 1892
Cdd:pfam01576 458 KLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1893 RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1751 |
5.58e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.37 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 880 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEleEILHDLE 959
Cdd:PTZ00121 1115 RKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE--EVRKAEE 1192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 960 SRVEeeeernqilQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRI 1039
Cdd:PTZ00121 1193 LRKA---------EDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1040 AECSSQLAEEEEKAKNLAKIRNKQEVMISDleERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKK 1119
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKAD--EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK----KK 1337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1120 EEELQGALARGDDETLHKNNALKVARElQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQEL 1199
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEE-KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA 1416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1200 RTKREqevaELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelACEVKVLQQVKA 1279
Cdd:PTZ00121 1417 KKKAD----EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK--AEEAKKADEAKK 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1280 ESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNEldnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET 1359
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA--------EEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1360 RQKlnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK----KKVDDDLGTIESLEEAKKKlLKDVEAL 1435
Cdd:PTZ00121 1563 KKK---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKIKAEELKKAEEE-KKKVEQL 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1436 SQRLEEKVLAYDKLEKTknrlqqelddltvdlDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETK 1515
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKA---------------EEENKIKAAEEAKKAEEDKKKAEE----AKKAEEDEKKAAEALKKEAE 1699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1516 AlslARALEEALEAKEEFERQNKQLRADMEDLMSskddvgkNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLR 1595
Cdd:PTZ00121 1700 E---AKKAEELKKKEAEEKKKAEELKKAEEENKI-------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1596 LEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEidlkdleaqieaankarDEVI 1675
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEME-----------------DSAI 1832
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1676 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSleaEILQLQEELASSERARRHAEQERDELADEIANS 1751
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNK---EKDLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1627-1917 |
1.58e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.24 E-value: 1.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1627 KQVRELEAELEdeRKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQS 1706
Cdd:COG1196 213 ERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA-------ELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1707 KESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELL 1786
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1787 NDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAK 1866
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1867 ERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQL 1917
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
878-1747 |
9.50e-20 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 96.96 E-value: 9.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 878 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRArlAAKKQELEEILHD 957
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLY--LDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 958 LESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegarQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1037
Cdd:pfam02463 242 LQELLRDEQEEIESSKQEIEKEEEKL--------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1038 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKrkldgettDLQDQIAELQAQVDELKVQLT 1117
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEE--------EELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1118 KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDF-ESEKASRNKAEKQKRDLSEELEALKTELEDTLDTtaaq 1196
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLlKEEKKEELEILEEEEESIELKQGKLTEEKEELEK---- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1197 QELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ 1276
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1277 VKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ 1356
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1357 EETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALS 1436
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEIL 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1437 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerdrAEAEAREKETKA 1516
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEE------------EEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1517 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRL 1596
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1597 EVNMQAMKAQFE-RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVI 1675
Cdd:pfam02463 844 EEQKLEKLAEEElERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERI 923
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1676 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKsleaEILQLQEELASSERARRHAEQERDELADE 1747
Cdd:pfam02463 924 KEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN----KRLLLAKEELGKVNLMAIEEFEEKEERYN 991
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
867-1487 |
1.77e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.91 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 867 RVFTKVKPLLQVTRQEEELqaKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQL-QAETELFAEAEEM----- 940
Cdd:TIGR02169 266 RLEEIEQLLEELNKKIKDL--GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLaKLEAEIDKLLAEIeeler 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 941 --------RARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIK 1012
Cdd:TIGR02169 344 eieeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1013 KMEEEVLLLEDQNSKFIKEKKLMEDRIaecssqlAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLD 1092
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEI-------KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1093 GETTDLQDQIAELQAQVDELK----------VQLTKKEEELQGALargddETLHKNNALKVARELQAQIAELQEDFESEK 1162
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKasiqgvhgtvAQLGSVGERYATAI-----EVAAGNRLNNVVVEDDAVAKEAIELLKRRK 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1163 ASR------NKAEKQKRDLSEELE-------------------ALKTELEDTL---DTTAAQQELRTKR----EQEVAE- 1209
Cdd:TIGR02169 572 AGRatflplNKMRDERRDLSILSEdgvigfavdlvefdpkyepAFKYVFGDTLvveDIEAARRLMGKYRmvtlEGELFEk 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1210 ----------------LKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKV 1273
Cdd:TIGR02169 652 sgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1274 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEkkgikfakdAAGLESQLQDTQE 1353
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE----LEEDLHKLEEALNDLE---------ARLSHSRIPEIQA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1354 LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVE 1433
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1434 ALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-EKKQKKFDQL 1487
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1325-1961 |
1.60e-18 |
|
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: 92.81 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1325 TLLEEAekKGI-KFAKDAAGLESQLQDTQELLQeetRQKLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEKQVLALQ 1401
Cdd:TIGR02168 159 AIFEEA--AGIsKYKERRKETERKLERTRENLD---RLEDILNELERQLKslERQAEKAERYKELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1402 sqLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTvdldhqrQIVSNLEKKQ 1481
Cdd:TIGR02168 234 --LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-------NEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1482 KKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL 1561
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1562 EKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDERK 1641
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERL-----------------QQEIEELLKKLEEAELKELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1642 QRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK--LKSLEAE 1719
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgILGVLSE 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1720 ILQLQE--ELASSERARRHAEQ---ERDELADEI----ANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRF 1790
Cdd:TIGR02168 528 LISVDEgyEAAIEAALGGRLQAvvvENLNAAKKAiaflKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1791 RKTTLQ--------------VDTLNTELAAERS-----------------------AAQKSDNARQQLERQNKELKAKLQ 1833
Cdd:TIGR02168 608 VKFDPKlrkalsyllggvlvVDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1834 ELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQL 1913
Cdd:TIGR02168 688 ELEEKIAEL-EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1907083610 1914 KRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
881-1451 |
2.03e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 92.43 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 881 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEqLQAETElfaEAEEMRARLAAKKQELEEILHDLES 960
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE-LEKELE---SLEGSKRKLEEKIRELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 961 RVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARqKLQLEKVTAEAKIKKMEEEVLLLEDQNSkfikEKKLMEDRIA 1040
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELR-EIEKRLSRLEEEINGIEERIKELEEKEE----RLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1041 ECSSQLAEEEEKAKNLAKIRNKQEVMisdleERLKKEEKTR---------QELEKAKRKLDGETTDLQDQIAELQAQVDE 1111
Cdd:PRK03918 349 ELEKRLEELEERHELYEEAKAKKEEL-----ERLKKRLTGLtpeklekelEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKvqltKKEEELQGAlargddetlhKNNALKVARELQAQiaELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:PRK03918 424 LK----KAIEELKKA----------KGKCPVCGRELTEE--HRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1192 TTAAQQELRtkREQEVAELKKALEDETKNHEAQiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETD---NKELA 1268
Cdd:PRK03918 488 VLKKESELI--KLKELAEQLKELEEKLKKYNLE----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKElekLEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1269 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKfakdaagLESQL 1348
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK-------LEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1349 QDTQELLQEETRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1423
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREK 708
|
570 580 590
....*....|....*....|....*....|
gi 1907083610 1424 AKKKLLKDVEALS--QRLEEKVLAYDKLEK 1451
Cdd:PRK03918 709 AKKELEKLEKALErvEELREKVKKYKALLK 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
876-1515 |
5.27e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 91.36 E-value: 5.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 876 LQVTRQEEELQaKDEELLKVKEKQTKVEGELEEMERKHQQLLE-EKNILAEQLQAETELFAEAEEmrARLAAKKQELEEI 954
Cdd:PTZ00121 1178 AEAARKAEEVR-KAEELRKAEDARKAEAARKAEEERKAEEARKaEDAKKAEAVKKAEEAKKDAEE--AKKAEEERNNEEI 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 955 LHDLESRVEEEEERNQILQNEKKKM-----QAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----IKKMEEEVLLLEDQN 1025
Cdd:PTZ00121 1255 RKFEEARMAHFARRQAAIKAEEARKadelkKAEEKKKADEAKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKKADAA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1026 SKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKK--EEKTRQELEKAKRKLDGETTDLQDQIA 1103
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1104 ELQAQVDEL--KVQLTKKEEEL--QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS--RNKAEKQKRDlSE 1177
Cdd:PTZ00121 1415 AAKKKADEAkkKAEEKKKADEAkkKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAeeAKKADEAKKK-AE 1493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1178 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataleelSEQLEQAKRFKANLEKNK 1257
Cdd:PTZ00121 1494 EAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK--------ADELKKAEELKKAEEKKK 1565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1258 qgleTDNKELACEVKVLQQVKAESEHKRKKldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTllEEAEKKGIKF 1337
Cdd:PTZ00121 1566 ----AEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEEKKKVEQ 1637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1338 AKDAAglESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlalQSQLADTKKKVdddlgt 1417
Cdd:PTZ00121 1638 LKKKE--AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA-----LKKEAEEAKKA------ 1704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1418 iESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISAR 1497
Cdd:PTZ00121 1705 -EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
650
....*....|....*...
gi 1907083610 1498 YAEERDRAEAEAREKETK 1515
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1008-1607 |
9.46e-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: 89.69 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1008 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKA 1087
Cdd:TIGR04523 67 EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1088 KRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEEL---QGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKAS 1164
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1165 RNKAEKQKRDLSEELEALKTELEDT----LDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRqrhaTALEELS 1240
Cdd:TIGR04523 227 NNQLKDNIEKKQQEINEKTTEISNTqtqlNQLKDEQNKIKKQLSEKQKELEQN-NKKIKELEKQLNQLK----SEISDLN 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1241 EQLEQ--AKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKkldaqvqELHAKVSEGDRLRVELAEKANKLQN 1318
Cdd:TIGR04523 302 NQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK-------ELTNSESENSEKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1319 ELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1398
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQIND----LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1399 ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLE 1478
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1479 KKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKALSLaraleeaLEAKEEFERQNKQLRADMEDLMSSKDDVGK 1556
Cdd:TIGR04523 531 SEKKEKESKISdlEDELNKDDFELKKENLEKEIDEKNKEIEEL-------KQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1557 NVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF 1607
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETI 654
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1234-1953 |
1.17e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 89.97 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1234 TALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKAESEhKRKKLDAQVQELHAkvsEGDRLRVELAE-K 1312
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAE-RYAAARERLAELEY---LRAALRLWFAQrR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1313 ANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLS-SRIRQLEEEKNSLQEQQEEEEEARK 1391
Cdd:COG4913 290 LELLEAELEELRAELARLEAE-------LERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1392 NLEKQVLALQSQLADTKkkvdddlgtiESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1471
Cdd:COG4913 363 RLEALLAALGLPLPASA----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1472 QIVSNLEKKQKKFDQLLAEEKGISA---RYA------EERDRAEAEAREKE--TKALSLARALEEALEAKEEFERQNKQL 1540
Cdd:COG4913 433 RRKSNIPARLLALRDALAEALGLDEaelPFVgelievRPEEERWRGAIERVlgGFALTLLVPPEHYAAALRWVNRLHLRG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1541 RADMEdlmsskdDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedaklRLEVNMQAMKAQFERDLQTrdeqneE 1620
Cdd:COG4913 513 RLVYE-------RVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA------ELGRRFDYVCVDSPEELRR------H 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1621 KKRL----LLKQVRELeAELEDERKQRALAV----ASKKkmeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1692
Cdd:COG4913 574 PRAItragQVKGNGTR-HEKDDRRRIRSRYVlgfdNRAK-----LAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1693 EEARAsrdeiFAQSKESEKKLKSLEAEILQLQEELASSERAR---RHAEQERDELADEIANSASGKSALLDEKRRLEARI 1769
Cdd:COG4913 648 EALQR-----LAEYSWDEIDVASAEREIAELEAELERLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKEL 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1770 AQLEEELEEEQSNMELLNDRFRK-TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV---KSKFKA 1845
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARLeLRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMrafNREWPA 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1846 TISALEAKIGQLEE------QLEQE---AKERAAANKLVRRTEKKLKEIFMQVEDERRHAdqyKEQMEKANARMKQLK-- 1914
Cdd:COG4913 803 ETADLDADLESLPEylalldRLEEDglpEYEERFKELLNENSIEFVADLLSKLRRAIREI---KERIDPLNDSLKRIPfg 879
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1907083610 1915 --RQLeeAEEEATRANASRRKLQRELDDATEANEGLSREVS 1953
Cdd:COG4913 880 pgRYL--RLEARPRPDPEVREFRQELRAVTSGASLFDEELS 918
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1427 |
1.29e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 90.20 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 859 KLRHWQWWRVFTKVKPLLQVTRQ---EEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQAETELFA 935
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQaaiKAEEARKADELKKAEEKKKADEAKKAEEKKK----ADEAKKKAEEAKKADEAKK 1322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 936 EAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAK----- 1010
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKkkaee 1402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1011 IKKMEEEVLLLEDQNSKFIKEKKLMED-RIAECSSQLAEEEEKAKNLAKirnKQEVMISDLEERLKKEEKTRQELEKAKR 1089
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1090 KLDGETTDLQDQIAELQAQVDELK--VQLTKKEEELQGALARGDDETLHKNNALKVARELQaQIAELQEDFESEKASRNK 1167
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1168 AEKQKRdlseELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATAlEELSEQLEQAK 1247
Cdd:PTZ00121 1559 KAEEKK----KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA-EELKKAEEEKK 1633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1248 RF----KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQElhakvsEGDRLRVELAEKANKLQNELDNV 1323
Cdd:PTZ00121 1634 KVeqlkKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE------EDEKKAAEALKKEAEEAKKAEEL 1707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1324 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1403
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKK----AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
570 580 590
....*....|....*....|....*....|...
gi 1907083610 1404 LADTK---------KKVDDDLGTIESLEEAKKK 1427
Cdd:PTZ00121 1784 ELDEEdekrrmevdKKIKDIFDNFANIIEGGKE 1816
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
886-1586 |
2.18e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 88.97 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 886 QAKDEELLKVKEKQTKVEGE---LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH---DLE 959
Cdd:PRK03918 134 QGEIDAILESDESREKVVRQilgLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEIS 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 960 SRVEEEEERNQILQNEKKKMQAHiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEVllledqnskfikekKLMEDRI 1039
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEEL-----------KEEIEELEKELESLEGSKRKLEEKI--------------RELEERI 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1040 AECSSQLAEEEEKAKNLAKIRNKQEVMISdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvQLTKK 1119
Cdd:PRK03918 269 EELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLE-ELKKK 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1120 EEELQGALARgdDETLHKnnALKVARELQAQIAELqedfeSEKASRNKAEKQKRDLsEELEALKTELEDTLDTTAAQqel 1199
Cdd:PRK03918 347 LKELEKRLEE--LEERHE--LYEEAKAKKEELERL-----KKRLTGLTPEKLEKEL-EELEKAKEEIEEEISKITAR--- 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1200 RTKREQEVAELKKALEdetknheaQIQDMRQRHATALEELSEqlEQAKRFKAnleknkqgletdnkELACEVKVLQQVKA 1279
Cdd:PRK03918 414 IGELKKEIKELKKAIE--------ELKKAKGKCPVCGRELTE--EHRKELLE--------------EYTAELKRIEKELK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1280 ESEHKRKKLDAQVQELHAKVSEGDRLRV--ELAEKANKLQNELDNVStlLEEAEKKGIKFakdaaglesqlqdtqellqE 1357
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKLKKYN--LEELEKKAEEY-------------------E 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1358 ETRQKLN-LSSRIRQLEEEKNSLQEQQEEeeeaRKNLEKQVLALQSQLADTKKKvdddlgtiesLEEAKKKLLKDVEALS 1436
Cdd:PRK03918 529 KLKEKLIkLKGEIKSLKKELEKLEELKKK----LAELEKKLDELEEELAELLKE----------LEELGFESVEELEERL 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1437 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEErdraeaEAREKETKA 1516
Cdd:PRK03918 595 KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE------EYEELREEY 668
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1517 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEqQVEEMRTQLEELEDEL 1586
Cdd:PRK03918 669 LELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALL 737
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
973-1904 |
3.66e-17 |
|
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: 88.49 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 973 QNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKME-------EEVLLLEDQNSKFIKEKKLmedriaecSSQ 1045
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLkekleleEEYLLYLDYLKLNEERIDL--------LQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1046 LAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLdgettdLQDQIAELQAQVDELKVQLTKKEEELQG 1125
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL------LAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1126 ALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQ 1205
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1206 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEqakrfKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR 1285
Cdd:pfam02463 399 LKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-----SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1286 KKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNL 1365
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1366 SSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLA 1445
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1446 YDKLEKTKNRLQQELDDlTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEE 1525
Cdd:pfam02463 634 LTKLKESAKAKESGLRK-GVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1526 ALEAKEEFERQNKQLRADMEDLmsskddvgknvhelekSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1605
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKI----------------NEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1606 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQaqm 1685
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAE--- 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1686 kdyqrelEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIansasgkSALLDEKRRL 1765
Cdd:pfam02463 854 -------EELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL-------NLLEEKENEI 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1766 EARIAQLEEELeeeqsnmellndrfrkttLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1845
Cdd:pfam02463 920 EERIKEEAEIL------------------LKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIE 981
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1846 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQME 1904
Cdd:pfam02463 982 EFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYL 1040
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1418-1961 |
4.55e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.79 E-value: 4.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1418 IESLEEAKKKLLKDVEALSQRLEEKVLaYDKLektkNRLQQELDDLTVDLDHqrqivsnLEKKQKKFDQLLAEEKGISAR 1497
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKDL-HERL----NGLESELAELDEEIER-------YEEQREQARETRDEADEVLEE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1498 YAEERDRAE------AEAREK----ETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA 1567
Cdd:PRK02224 246 HEERREELEtleaeiEDLRETiaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1568 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK---AQFERDLQTRDEQNEEKKrlllKQVRELEAELEDERKQRA 1644
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRR----EEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1645 LAvaskkkmEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDE--------------IFAQSKESE 1710
Cdd:PRK02224 402 DA-------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegspHVETIEEDR 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1711 KKLKSLEAEILQLQEELASSErarrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRf 1790
Cdd:PRK02224 475 ERVEELEAELEDLEEEVEEVE--------ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRER- 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1791 rkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfkATISALEAKIGQLEEQLEqeakeraa 1870
Cdd:PRK02224 546 ------AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL--ERIRTLLAAIADAEDEIE-------- 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1871 anklvRRTEKKlkEIFMQVEDERRhadqykEQMEKANARMKQLKRQ-----LEEAEEEATRANASRRKLQRELDDATEAN 1945
Cdd:PRK02224 610 -----RLREKR--EALAELNDERR------ERLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREER 676
|
570
....*....|....*.
gi 1907083610 1946 EGLSREVSTLKNRLRR 1961
Cdd:PRK02224 677 DDLQAEIGAVENELEE 692
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1011-1826 |
6.63e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.89 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1011 IKKMEEevLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1090
Cdd:PTZ00121 1026 IEKIEE--LTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEA 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1091 LDGETTDLQDQIAELQAQV---DELKVQLTKKEEELQGAL-ARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1166
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKkaeDARKAEEARKAEDARKAEeARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARK 1183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1167 KAEKQKRDlseelEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1246
Cdd:PTZ00121 1184 AEEVRKAE-----ELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1247 KRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLQNELDNVSTL 1326
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD-EAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1327 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssrirqlEEEKNSLQEQQEEEEEARKNLEkqvlaLQSQLAD 1406
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK----------EEAKKKADAAKKKAEEKKKADE-----AKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1407 TKKKVDDdlgtIESLEEAKKKllkdVEALSQRLEEKVLAyDKLEKtKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQ 1486
Cdd:PTZ00121 1403 DKKKADE----LKKAAAAKKK----ADEAKKKAEEKKKA-DEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1487 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKE-EFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK 1565
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1566 RALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLK--QVRELEAELEDERKQR 1643
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeEAKIKAEELKKAEEEK 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1644 ALAVASKKKMEIDLKDLEA--QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK---LKSLEA 1718
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEElkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKaeeLKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1719 EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRrleaRIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1798
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK----KIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
810 820
....*....|....*....|....*...
gi 1907083610 1799 TLNTELAAERSAAQKSDNARQQLERQNK 1826
Cdd:PTZ00121 1789 DEKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1145-1752 |
3.31e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.35 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1145 RELQAQIAELQEDFESEKASRNKAEK--QKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDEtknHE 1222
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDarEQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA---EL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1223 AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE-LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSE 1301
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1302 GDRlrvELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQE 1381
Cdd:COG4913 378 SAE---EFAALRAEAAALLEALEEELEALEE-------ALAEAEAALRDLRR--------------ELRELEAEIASLER 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1382 QqeeeeeaRKNLEKQVLALQSQLADTKKKVDDDL-----------------GTIESL-----------EEAKKKLLKDVE 1433
Cdd:COG4913 434 R-------KSNIPARLLALRDALAEALGLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVN 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1434 ALSQRLE---EKVLAYDKLEKT-----------------------KNRLQQELDDLTVD----LDHQR-------QIVSN 1476
Cdd:COG4913 507 RLHLRGRlvyERVRTGLPDPERprldpdslagkldfkphpfrawlEAELGRRFDYVCVDspeeLRRHPraitragQVKGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1477 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKEtKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVG- 1555
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELE-EELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVAs 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1556 --KNVHELEKSKRALEQ---QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVR 1630
Cdd:COG4913 666 aeREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1631 ELEAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEVIKQLRKLqaqMKDYQRELEEARASRDEIFAQSKESE 1710
Cdd:COG4913 746 ELRALLEERFAAALGDAVERELRE----NLEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYL 818
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1907083610 1711 KKLKSLEAEIL-QLQEELAssERARRHAEQERDELADEIANSA 1752
Cdd:COG4913 819 ALLDRLEEDGLpEYEERFK--ELLNENSIEFVADLLSKLRRAI 859
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
997-1624 |
5.89e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.58 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 997 RQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKF-----IKEKKLMEDRIAECSSQLAEEEEKaknlakirnkqevmISDL 1070
Cdd:COG4913 249 EQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLEAE--------------LERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1071 EERLKKEEKTRQELEKAKRKLDGettdlqDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQ 1150
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGG------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1151 IAELQEDFESEKAS----RNKAEKQKRDLSEELEALKTELEdtldttaaqqELRTKR---EQEVAELKKALEDETKNHEA 1223
Cdd:COG4913 389 AAALLEALEEELEAleeaLAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEA 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1224 QIQ------DMRQRHA---TALEEL-----------SEQLEQAKRFkanLEKNKQGLETdnkelacevkVLQQVKAESEH 1283
Cdd:COG4913 459 ELPfvgeliEVRPEEErwrGAIERVlggfaltllvpPEHYAAALRW---VNRLHLRGRL----------VYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1284 -KRKKLDAQ--VQELHAKVSE-GDRLRVELAEKANKLQneLDNVSTLleEAEKKGI-----------KFAKDAagleSQL 1348
Cdd:COG4913 526 pERPRLDPDslAGKLDFKPHPfRAWLEAELGRRFDYVC--VDSPEEL--RRHPRAItragqvkgngtRHEKDD----RRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1349 QDTQELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ--SQLADTKKKVDDDLGTIESLEEAK 1425
Cdd:COG4913 598 IRSRYVLGFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1426 KKLLK---DVEALSQRLEEKVLAYDKLEKTKN-------RLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgis 1495
Cdd:COG4913 678 ERLDAssdDLAALEEQLEELEAELEELEEELDelkgeigRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER--- 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1496 aRYAEERDRAEAEAREKETKALSLARaleealeakeefeRQNKQLRADMEDLMSS-KDDVGKNVHELEKSKRALEqQVEE 1574
Cdd:COG4913 755 -FAAALGDAVERELRENLEERIDALR-------------ARLNRAEEELERAMRAfNREWPAETADLDADLESLP-EYLA 819
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1575 MRTQLEelEDEL-QATEDAKLRLEVNMQAMKAQFERDLqtRDEQNEEKKRL 1624
Cdd:COG4913 820 LLDRLE--EDGLpEYEERFKELLNENSIEFVADLLSKL--RRAIREIKERI 866
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1235-1960 |
6.01e-16 |
|
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: 84.35 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1235 ALEELSEQLEQAKRFKANLEKNKQGLET--DNKELACEVKVLQQVKAESE-----HKRKKLDAQVQELHAKVSEGDRLRV 1307
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQQLERlrREREKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1308 ELAEKANKLQNELDNVSTLLEEAEKK--------GIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1379
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1380 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1459
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1460 LDDLTVDLDHQRQIVSNLEKKQKKFDqllaeekgisaryaEERDRAEAEAREKETKALSLAraleealEAKEEFERQNKQ 1539
Cdd:TIGR02169 415 LQRLSEELADLNAAIAGIEAKINELE--------------EEKEDKALEIKKQEWKLEQLA-------ADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1540 LRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAT-----------EDAKLRLEV----NMQAMK 1604
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgERYATAIEVaagnRLNNVV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1605 AQFERDLQTRDEQNEEKKR-----LLLKQVRELEAELEDERKQRALAVAskkkmeIDLKDLEAQIEAANKA--RDEVIKQ 1677
Cdd:TIGR02169 554 VEDDAVAKEAIELLKRRKAgratfLPLNKMRDERRDLSILSEDGVIGFA------VDLVEFDPKYEPAFKYvfGDTLVVE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1678 ----LRKL--QAQMKDYQRELEE--------ARASRDEIFAQSKESEKkLKSLEAEILQLQEELASSERARRHAEQERDE 1743
Cdd:TIGR02169 628 dieaARRLmgKYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPAE-LQRLRERLEGLKRELSSLQSELRRIENRLDE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1744 LadeiansasgKSALLDEKRRLEARiaqleeeleeeQSNMELLNDRFRKttlqvdtLNTELAAERSAAQKSDNARQQLER 1823
Cdd:TIGR02169 707 L----------SQELSDASRKIGEI-----------EKEIEQLEQEEEK-------LKERLEELEEDLSSLEQEIENVKS 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1824 QNKELKAKLQELEgAVKSKFKATISALEAKIG-----QLEEQLEQEAKERAAANKLVRRTEKKLKEIFM---QVEDERRH 1895
Cdd:TIGR02169 759 ELKELEARIEELE-EDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLekeYLEKEIQE 837
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1896 ADQY----KEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELddateanEGLSREVSTLKNRLR 1960
Cdd:TIGR02169 838 LQEQridlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL-------GDLKKERDELEAQLR 899
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
875-1460 |
2.01e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.40 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 875 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELE----EMERKHQQLLEEK-NILAEQLQAETELFAEAEEMRARLAAKKQ 949
Cdd:PRK02224 158 LLQLGKLEEYRERASDARLGVERVLSDQRGSLDqlkaQIEEKEEKDLHERlNGLESELAELDEEIERYEEQREQARETRD 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 950 ELEEILHDLESRveeeEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLL-------LE 1022
Cdd:PRK02224 238 EADEVLEEHEER----REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLddadaeaVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1023 DQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI 1102
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1103 AELQAQVDELKVQLTKKEEELQGALARGDDetLHKNNA-----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSE 1177
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDE--LREREAeleatLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1178 ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAlEDETKNHEAQIQDMRQRHATALEELSEQLEQAkrfkANLEKNK 1257
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAEDLVEA-EDRIERLEERREDLEELIAERRETIEEKRERA----EELRERA 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1258 QGLEtdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNeLDNVSTLLEEAEKKGikf 1337
Cdd:PRK02224 547 AELE-----------------AEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIADAE--- 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1338 aKDAAGLESQLQDTQElLQEETRQKL-NLSSRIRQLEEEKNslQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLG 1416
Cdd:PRK02224 606 -DEIERLREKREALAE-LNDERRERLaEKRERKRELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQA 681
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1417 TIESLEEAKKKL------LKDVEALSQRLEEKVLAYDKLEKTKNRLQQEL 1460
Cdd:PRK02224 682 EIGAVENELEELeelrerREALENRVEALEALYDEAEELESMYGDLRAEL 731
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1311-1917 |
2.39e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.42 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1311 EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEAR 1390
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1391 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDVEALSQRLEEKVLAYDKLEK-------TKNRLQQELD 1461
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELKEKAEEYIKLSEfyeeyldELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1462 DLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAlslaraleealeakeeferQNKQLR 1541
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-------------------ELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1542 ADMEDLmsSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmqamKAQFERDLQTRDEQNEEK 1621
Cdd:PRK03918 379 KRLTGL--TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK------KAKGKCPVCGRELTEEHR 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1622 KRLLlkqvRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKAR--DEVIKQLRKLQAQMKDYQRE-LEEARAS 1698
Cdd:PRK03918 451 KELL----EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLEeLEKKAEE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1699 RDEIFAQSKESEKKLKSLEAEILQLQE---ELASSERARRHAEQERDELADEIANSASGKSALLDEKrrleariaqleee 1775
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEER------------- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1776 leeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1855
Cdd:PRK03918 594 ----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYL 669
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1856 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEdERRHADQYKEQMEKANARMKQLKRQL 1917
Cdd:PRK03918 670 ELSRELAGLRAELEELEKRREEIKKTLEKLKEELE-EREKAKKELEKLEKALERVEELREKV 730
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
877-1724 |
4.15e-15 |
|
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: 81.63 E-value: 4.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleeKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILH 956
Cdd:TIGR00606 232 QLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI---KALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYH 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 957 DLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfikekklme 1036
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR------------ 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1037 driaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQL 1116
Cdd:TIGR00606 377 -------LELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1117 TKKEEELQGALARGDDETLHKNNALKVARELQAQIAELqedfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ 1196
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL------SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1197 QELRTKREQEVAELKKALEDETKNHEaQIQDMRQRHATALEELSEQLEQAKRFKA---NLEKNKQGLETDNKELACEVKV 1273
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTSLLGYFPNKKQLEDwlhSKSKEINQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1274 LQQVKAESEHKRKKLDAQVQELHAKVSEgdrlrvelAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQE 1353
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSSYEDKLFD--------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTD 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1354 -------LLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1426
Cdd:TIGR00606 675 enqsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1427 KLLKDVEALSQRLEEKvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1506
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1507 AEarEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEleksKRALEQQVEEMRTQLEELEDEL 1586
Cdd:TIGR00606 831 KQ--EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQR----RQQFEEQLVELSTEVQSLIREI 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1587 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQN---EEKKRLLLKQVRELEAELED-ERKQRALAVASKKKMEIDLKDLEA 1662
Cdd:TIGR00606 905 KDAKEQDSPLETFLEKDQQEKEELISSKETSNkkaQDKVNDIKEKVKNIHGYMKDiENKIQDGKDDYLKQKETELNTVNA 984
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1663 QIEAANKARDEVIKQLRKLQAQM--KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1724
Cdd:TIGR00606 985 QLEECEKHQEKINEDMRLMRQDIdtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQ 1048
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1288-1859 |
4.28e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 81.62 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1288 LDAQVQELHAKvsegdrlrvELAEKANKLQNELDNVSTLLEEAEKKgikfaKDAAglESQLQDTQELLQ--EETRQklnl 1365
Cdd:PRK02224 192 LKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQ-----REQA--RETRDEADEVLEehEERRE---- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1366 ssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIEsLEEAkkkllkDVEALSQRLEEkvla 1445
Cdd:PRK02224 252 --ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDA------DAEAVEARREE---- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1446 ydkLEKTKNRLQQELDDLTVDL-DHQRQIvsnlekkqkkfdqllaeekgisARYAEERDRAEAEAREKETKALSLARALE 1524
Cdd:PRK02224 319 ---LEDRDEELRDRLEECRVAAqAHNEEA----------------------ESLREDADDLEERAEELREEAAELESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1525 EALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMK 1604
Cdd:PRK02224 374 EAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1605 A-------QFERDLQTRDEQNEekkrlllkQVRELEAELEDERKQRAlAVASKKKMEIDLKDLEAQIEAANKARDEVIKQ 1677
Cdd:PRK02224 454 CpecgqpvEGSPHVETIEEDRE--------RVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEEL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1678 LRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADeIANSASGKSA 1757
Cdd:PRK02224 525 IAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIAD 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1758 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQELEg 1837
Cdd:PRK02224 604 AEDEIERLREKREALAELNDERRERLAEKRER-------KRELEAEFDEARIEEARED--KERAEEYLEQVEEKLDELR- 673
|
570 580
....*....|....*....|..
gi 1907083610 1838 AVKSKFKATISALEAKIGQLEE 1859
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEE 695
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1156-1897 |
6.24e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 81.34 E-value: 6.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1156 EDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQrhata 1235
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARK----- 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1236 lEELSEQLEQAKRfkanLEKNKQGLETDNkelACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1315
Cdd:PTZ00121 1166 -AEEARKAEDAKK----AEAARKAEEVRK---AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKK 1237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1316 LQNELDNVstlleEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlSSRIRQLEEEKNSlqeqqeeeEEARKNLEK 1395
Cdd:PTZ00121 1238 DAEEAKKA-----EEERNNEEIRKFEEARMAHFARRQAAIKAEEARK---ADELKKAEEKKKA--------DEAKKAEEK 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1396 QVLALQSQLADTKKKVDDdlgTIESLEEAKKKllkdVEALSQRLEEKvlaYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1475
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADE---AKKKAEEAKKK----ADAAKKKAEEA---KKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1476 NLEKKQKKFDQllAEEKGISARYAEERDRAEAEAREK--ETKALSLARALEEALEAKEEFERQNKQLRADMEDlmSSKDD 1553
Cdd:PTZ00121 1372 KKEEAKKKADA--AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE--AKKAD 1447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1554 VGKNVHELEKSKRALEQQVEEMRT--QLEELEDELQATEDAKLRLEVNMQamKAQFERDLQTRDEQNEEKKRLLLKQVRE 1631
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKK--KADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1632 LEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1711
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEK 1605
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1712 KLKSLEA----EILQLQEELASSERARRHAEQERDELADEIANS---------ASGKSALLDEKRRLEARIAQLEEELEE 1778
Cdd:PTZ00121 1606 KMKAEEAkkaeEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAeelkkaeeeNKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1779 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQqlERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLE 1858
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE--ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
730 740 750
....*....|....*....|....*....|....*....
gi 1907083610 1859 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHAD 1897
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD 1802
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
871-1463 |
2.39e-14 |
|
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: 79.24 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 871 KVKPLLQVTRQEEELQAKDEELL-KVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFA-EAEEMRARLAA 946
Cdd:TIGR00618 291 KAAPLAAHIKAVTQIEQQAQRIHtELQSKMRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRdAHEVATSIREI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 947 KKQELEEI--LHDLESRVEEEEERNQILQNEKKKMQAhiqdLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQ 1024
Cdd:TIGR00618 371 SCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDILQR----EQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAA 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1025 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIrnkqevmisdleerLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1104
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQI--------------HLQETRKKAVVLARLLELQEEPCPLCGSCIH 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1105 LQAqvdelKVQLTKKEEELQGALARGDDETLHKNNALKVAR----ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1180
Cdd:TIGR00618 513 PNP-----ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYhqltSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1181 ALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN-----HEAQIQDMRQRHATALEELSEQL------EQAKRF 1249
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLqdvrlHLQQCSQELALKLTALHALQLTLtqervrEHALSI 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1250 KANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLdaqvQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEE 1329
Cdd:TIGR00618 668 RVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLL----RELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1330 AEKKGIKFAKDA--AGLESQLQDTQELL------QEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1401
Cdd:TIGR00618 744 SLKELMHQARTVlkARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQC 823
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1402 SQLADTKKKVDDDLgtiesleEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDL 1463
Cdd:TIGR00618 824 ETLVQEEEQFLSRL-------EEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1167-1883 |
2.61e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.95 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1167 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQRHATaLEELSEQL 1243
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEKLEKEVKE-LEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1244 EQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesEHKRKKLDAQVQELHAKVSEGDRLRvELAEKANKLqneldnv 1323
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIREL--------------EERIEELKKEIEELEEKVKELKELK-EKAEEYIKL------- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1324 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETrqklNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqVLALQSQ 1403
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLEELKKKLKELEKRLEELEERHELYEE-AKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1404 LADTKKKVdddlgTIESLEEAKKKLlkdvEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldhqRQIVSNLEKKQKK 1483
Cdd:PRK03918 374 LERLKKRL-----TGLTPEKLEKEL----EELEKAKEEIEEEISKITARIGELKKEIKEL-------KKAIEELKKAKGK 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1484 F---DQLLAEE--KGISARYAEERDRAEAEAREKETKaLSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK-N 1557
Cdd:PRK03918 438 CpvcGRELTEEhrKELLEEYTAELKRIEKELKEIEEK-ERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyN 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1558 VHELEKSKRALEQQVEEMRT---QLEELEDELQatedaklrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEA 1634
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKlkgEIKSLKKELE--------------------------KLEELKKKLAELEKKLDELEE 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1635 ELED-ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDeVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1713
Cdd:PRK03918 571 ELAElLKELEELGFESVEELEERLKELEPFYNEYLELKD-AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1714 KSLEAEIlqlqeelasSERARRHAEQERDELADEIAnsasgksalldekrRLEARIAQLEEELEEEQSNMELLNDRFrkt 1793
Cdd:PRK03918 650 EELEKKY---------SEEEYEELREEYLELSRELA--------------GLRAELEELEKRREEIKKTLEKLKEEL--- 703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1794 tlqvdtlntelaaersaaQKSDNARQQLERQNKELkAKLQELEGAVKS-KFKATISALeAKIGQLEEQLEQEAKERAAAN 1872
Cdd:PRK03918 704 ------------------EEREKAKKELEKLEKAL-ERVEELREKVKKyKALLKERAL-SKVGEIASEIFEELTEGKYSG 763
|
730
....*....|.
gi 1907083610 1873 KLVRRTEKKLK 1883
Cdd:PRK03918 764 VRVKAEENKVK 774
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1279-1959 |
2.79e-14 |
|
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: 78.96 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1279 AESEHKRKKLDAQVQELHAKVsegDRLRVEL--AEKANKLQNELDNVSTLLEEAEKKgiKFAKDAAGLESQLQDTQELLQ 1356
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQL---ERLRRERekAERYQALLKEKREYEGYELLKEKE--ALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1357 EETRQKLNLSSRIRQLEEEKNSLQEQQeeeeeaRKNLEKQVLALQSQLADTKkkvdddlGTIESLEEAKKKLLKDVEALS 1436
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKI------KDLGEEEQLRVKEKIGELE-------AEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1437 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKE--- 1513
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEERKRRD---KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklk 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1514 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1593
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1594 LRLEVNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELEAELE------------DERKQRALAVASKKKME------- 1654
Cdd:TIGR02169 479 DRVEKELSKLQRELAE-AEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvGERYATAIEVAAGNRLNnvvvedd 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1655 ---------------------------------------------IDLKDLEAQIEAANK--ARDEVIKQ----LRKL-- 1681
Cdd:TIGR02169 558 avakeaiellkrrkagratflplnkmrderrdlsilsedgvigfaVDLVEFDPKYEPAFKyvFGDTLVVEdieaARRLmg 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1682 QAQMKDYQRELEE--------ARASRDEIFAQSKESEkKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSAS 1753
Cdd:TIGR02169 638 KYRMVTLEGELFEksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1754 GKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLER-----QNKEL 1828
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsRIPEI 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1829 KAKLQELEgAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANA 1908
Cdd:TIGR02169 797 QAELSKLE-EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1909 RMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1010-1836 |
3.07e-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: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1010 KIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE----EEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELE 1085
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRT---VREKERELVDCQRELEKLN 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1086 KAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQG--------ALARGDDETLHKNNALKVARELQAQIAELQED 1157
Cdd:TIGR00606 333 KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlatrleldGFERGPFSERQIKNFHTLVIERQEDEAKTAAQ 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1158 FESEKASRNK-AEKQKRDLSEELEALKTELE-DTLDTTAAQQELRTKR---EQEVAELKKALEDETKNHEAQIQDMRQRH 1232
Cdd:TIGR00606 413 LCADLQSKERlKQEQADEIRDEKKGLGRTIElKKEILEKKQEELKFVIkelQQLEGSSDRILELDQELRKAERELSKAEK 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1233 ATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESehkRKKLDAQVQELHAKVSEGDRLRVELAEK 1312
Cdd:TIGR00606 493 NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT---KDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1313 ANK--LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL---EEEKNSLQEQQEEEE 1387
Cdd:TIGR00606 570 PNKkqLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLERLKEEIE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1388 EARKNLekQVLALQSQLADTK-KKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAY----DKLEKTKNRLQQELDD 1462
Cdd:TIGR00606 650 KSSKQR--AMLAGATAVYSQFiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLApdklKSTESELKKKEKRRDE 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1463 LTVDLDHQRQIvsnLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKET--KALSLARALEEALEAKEEFERQNKQL 1540
Cdd:TIGR00606 728 MLGLAPGRQSI---IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDV 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1541 RADMEDLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA---QFERDLQTRd 1615
Cdd:TIGR00606 805 ERKIAQQAAKLQgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRR- 883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1616 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKardevikqlrKLQAQMKDYQRELEEA 1695
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK----------KAQDKVNDIKEKVKNI 953
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1696 RASRDEIFAQSKES-EKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEE 1774
Cdd:TIGR00606 954 HGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEV 1033
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1775 ELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELE 1836
Cdd:TIGR00606 1034 EEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1001-1598 |
4.11e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 78.24 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1001 QLEKVTAEAKiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKI-----RNKQEVMISDLEERLK 1075
Cdd:pfam15921 246 QLEALKSESQ-NKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIiqeqaRNQNSMYMRQLSDLES 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1076 KEEKTRQELEKAKRKLDGettdlqdqiaelqaQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1155
Cdd:pfam15921 325 TVSQLRSELREAKRMYED--------------KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKRE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1156 EDFESEKASRNKAEKQKRDLSEELEALKTELEDtldttaaqqelrtkREQEVAELKKALedetKNHEAQIQDMRQRHATA 1235
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDD--------------RNMEVQRLEALL----KAMKSECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1236 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQ---------------------VKAESEHKRKKLDAQVQE 1294
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltaslqekeraieaTNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1295 LHAKVSEGDRLR----------VELAEKANK---LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ 1361
Cdd:pfam15921 533 LQHLKNEGDHLRnvqtecealkLQMAEKDKVieiLRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1362 KLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVlalqsqlADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE 1441
Cdd:pfam15921 613 KDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAV-------KDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRN 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1442 KVlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL-LAEEKGISARyaeerdRAEAEAREKETKALSLA 1520
Cdd:pfam15921 686 KS---EEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVaMGMQKQITAK------RGQIDALQSKIQFLEEA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1521 raLEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAK 1593
Cdd:pfam15921 757 --MTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEValdkaslQFAECQDIIQRQEQES 834
|
....*
gi 1907083610 1594 LRLEV 1598
Cdd:pfam15921 835 VRLKL 839
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1046-1747 |
6.32e-14 |
|
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: 77.70 E-value: 6.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1046 LAEEEEKAKNLAKIRNKQEV-MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQI--AELQAQVDELKvQLTKKEEE 1122
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYtQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTyhERKQVLEKELK-HLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1123 LQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEK-----QKRDLSEELEALKTELEDTLDTTAAQQ 1197
Cdd:TIGR00618 238 TQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERinrarKAAPLAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1198 ELRTKREQEVAELKKALEDETkNHEAQIQDMRQRHAtALEELSEQLEQAKRFKANLEKNKQgLETDNKELACEVKVLQQV 1277
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQS-SIEEQRRLLQTLHS-QEIHIRDAHEVATSIREISCQQHT-LTQHIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1278 KAESEHKRKKLDAQVQELHAKVSEGDRLRVELA----------EKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1347
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRDLQGQLAhakkqqelqqRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1348 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNL-------------EKQVLALQSQLADTKKKVDDD 1414
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrrmqrgEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1415 LGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdLDHQRQIV-SNLEKKQKKFDQLLAEEKG 1493
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKL---SEAEDMLAcEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1494 ISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK---RALEQ 1570
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQtllRELET 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1571 QVEEMRTQLEELEDELQATEdaklrlevnmqamkaqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASK 1650
Cdd:TIGR00618 712 HIEEYDREFNEIENASSSLG------------------SDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1651 KKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK----KLKSLEAEILQLQEE 1726
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQLLK 853
|
730 740
....*....|....*....|.
gi 1907083610 1727 LASSERARRHAEQERDELADE 1747
Cdd:TIGR00618 854 YEECSKQLAQLTQEQAKIIQL 874
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1203-1916 |
7.34e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.87 E-value: 7.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1203 REQEVAELKKALEDETK-NHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKnkqgletdnKELACEVKVLQQVKAES 1281
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKaEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEA---------FGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1282 EHKRKKldaqvqelhAKVSEGDRLRVELAEKANKLQNeldnvstlLEEAEKkgikfAKDAAGLESQLQDTQELLQEETRQ 1361
Cdd:PTZ00121 1114 ARKAEE---------AKKKAEDARKAEEARKAEDARK--------AEEARK-----AEDAKRVEIARKAEDARKAEEARK 1171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1362 klnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKqvlALQSQLADTKKKVDDdlgtIESLEEAKK-KLLKDVEALSQRLE 1440
Cdd:PTZ00121 1172 ----AEDAKKAEAARKAEEVRKAEELRKAEDARK---AEAARKAEEERKAEE----ARKAEDAKKaEAVKKAEEAKKDAE 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1441 EkvlAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE--KGISARYAEERDRAEAEAR--EKETKA 1516
Cdd:PTZ00121 1241 E---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEkkKADEAKKAEEKKKADEAKKkaEEAKKA 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1517 LSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELE---DELQATEDAK 1593
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAK 1397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1594 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKqralAVASKKKMEIDLKDLEAQIEAANKARDE 1673
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1674 VIKQLRKLQAQMKDYQRELEEARASRDEifAQSKESEKKlkslEAEILQLQEELASSERARRHAEQERdelADEIANSAS 1753
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADE--AKKAAEAKK----KADEAKKAEEAKKADEAKKAEEAKK---ADEAKKAEE 1544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1754 GKSAllDEKRRLE-ARIAQLEEELEEEQSNMELLNDRFRKTTL--QVDTLNTELAAERSAAQKSDNARQQLERQNKELKA 1830
Cdd:PTZ00121 1545 KKKA--DELKKAEeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1831 KLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTE---KKLKEIFMQVEDERRHADQYKEQMEKAN 1907
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAKKAEEDEKKAAEALKKEAEEAK 1702
|
....*....
gi 1907083610 1908 aRMKQLKRQ 1916
Cdd:PTZ00121 1703 -KAEELKKK 1710
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
885-1546 |
1.14e-13 |
|
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: 76.68 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 885 LQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEE 964
Cdd:pfam05483 115 IEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEK 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 965 eeernQILQNEKKKMQAhiqdleeqldeeEGARQKLQLEKVTAEAKIKKMEEEvllledqnskFIKEKKLMEDRIAECSS 1044
Cdd:pfam05483 195 -----MILAFEELRVQA------------ENARLEMHFKLKEDHEKIQHLEEE----------YKKEINDKEKQVSLLLI 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1045 QLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD----LQDQIAELQAQVDELKVQLTKKE 1120
Cdd:pfam05483 248 QITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTIC 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1121 EELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ---- 1196
Cdd:pfam05483 328 QLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKevel 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1197 QELRT-----------------------KREQEVAELKKALEDETKNHEAQ---IQDMRQRHATALEELSEQLEQAKRFK 1250
Cdd:pfam05483 408 EELKKilaedeklldekkqfekiaeelkGKEQELIFLLQAREKEIHDLEIQltaIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1251 ANLEKNKQGLETDNKEL-------ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNV 1323
Cdd:pfam05483 488 IELTAHCDKLLLENKELtqeasdmTLELKKHQEDIINCKKQEERMLKQIENLEEKEMN---LRDELESVREEFIQKGDEV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1324 STLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQ 1403
Cdd:pfam05483 565 KCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELE 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1404 LADTKKKVDDDLGTIESLEEAKK----KLLKDVEALSQRLEEKVlaydklektknRLQQELDdltVDLDHQ-RQIVSNLE 1478
Cdd:pfam05483 645 LASAKQKFEEIIDNYQKEIEDKKiseeKLLEEVEKAKAIADEAV-----------KLQKEID---KRCQHKiAEMVALME 710
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1479 KKQKKFDQLLAE---EKGISARYAEERDRA----EAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMED 1546
Cdd:pfam05483 711 KHKHQYDKIIEErdsELGLYKNKEQEQSSAkaalEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
875-1623 |
1.65e-13 |
|
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: 76.55 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 875 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETEL----FAEAEEMRARLAAKKQE 950
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEleikREAEEEEEEELEKLQEK 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 951 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEG-ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFI 1029
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLElARQLEDLLKEEKKEELEILEEEEESIELKQGKLT 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1030 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGettdlqdqiaeLQAQV 1109
Cdd:pfam02463 448 EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV-----------LLALI 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1110 DELKVQLTKKEEELQGALARGDDETLHKN-NALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED 1188
Cdd:pfam02463 517 KDGVGGRIISAHGRLGDLGVAVENYKVAIsTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1189 TLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1268
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELL 676
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1269 CEVKVLQQVKAES--EHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLES 1346
Cdd:pfam02463 677 EIQELQEKAESELakEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSR 756
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1347 QLQDTQEllQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKK 1426
Cdd:pfam02463 757 LKKEEKE--EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEE 834
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1427 KLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1506
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1507 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMsskddvgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1586
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE-----------EEEERNKRLLLAKEELGKVNLMAIEEF 983
|
730 740 750
....*....|....*....|....*....|....*..
gi 1907083610 1587 QATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKR 1623
Cdd:pfam02463 984 EEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
948-1724 |
1.67e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 948 KQELEEILHDLESRVEEEEER----NQILQNEKKKMQAHIQDLEEQLdeeegarQKLQLEKvTAEAKIKKME---EEVLL 1020
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRlnesNELHEKQKFYLRQSVIDLQTKL-------QEMQMER-DAMADIRRREsqsQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1021 LEDQNS--KFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQEL------------EK 1086
Cdd:pfam15921 145 NQLQNTvhELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMstmhfrslgsaiSK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1087 AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAlargddetlHKNNALKVARELQAQIAELqedfeSEKASrn 1166
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQ---------HQDRIEQLISEHEVEITGL-----TEKAS-- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1167 KAEKQKRDLSEELEALKtelEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQA 1246
Cdd:pfam15921 289 SARSQANSIQSQLEIIQ---EQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTER 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1247 KRF---KANLEKNKQGLETD----NKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1319
Cdd:pfam15921 366 DQFsqeSGNLDDQLQKLLADlhkrEKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1320 LDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQqeeeeearknlEKQVLA 1399
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK-----------ERAIEA 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1400 LQSQLADTKKKVDDDLGTIESL---EEAKKKLLKDVEALSQRLEEKvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1476
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQHLkneGDHLRNVQTECEALKLQMAEK-------DKVIEILRQQIENMTQLVGQHGRTAGA 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1477 LEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM----SSKD 1552
Cdd:pfam15921 588 MQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRN 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1553 DVGKNVHELEKSKRALEQQVEEMRT-------QLEELEDELQATEDAKLRLE-VNMQAMKAQFerDLQTRDEQNEEKKRL 1624
Cdd:pfam15921 668 ELNSLSEDYEVLKRNFRNKSEEMETttnklkmQLKSAQSELEQTRNTLKSMEgSDGHAMKVAM--GMQKQITAKRGQIDA 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1625 LLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQieaankaRDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1704
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-------KNKMAGELEVLRSQERRLKEKVANMEVALDKASL 818
|
810 820
....*....|....*....|
gi 1907083610 1705 QSKESEKKLKSLEAEILQLQ 1724
Cdd:pfam15921 819 QFAECQDIIQRQEQESVRLK 838
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1166-1834 |
2.60e-13 |
|
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: 75.44 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1166 NKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREqevaELKKALEDETKNHEAQIQDMRQrhataleelseqleq 1245
Cdd:TIGR04523 29 NKQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDE----EKINNSNNKIKILEQQIKDLND--------------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1246 akrfKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVS 1324
Cdd:TIGR04523 90 ----KLKKNKDKiNKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1325 TLLEEAEKKGIKFAKDAAGLESQLQDTQellQEETRQKLNLSSrIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQL 1404
Cdd:TIGR04523 166 KQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKLELLLSN-LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1405 ADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLT--VDLDHQRQIVSNLEKKQK 1482
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNnqKEQDWNKELKSELKNQEK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1483 KFDQL---LAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVH 1559
Cdd:TIGR04523 322 KLEEIqnqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKL-------RLEVNMQAMKAQFERDLQTRDEQNEEKKrLLLKQVREL 1632
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1633 EAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARasrDEIfaQSKESEKK 1712
Cdd:TIGR04523 481 KQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE---DEL--NKDDFELK 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1713 LKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRK 1792
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1907083610 1793 TTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQE 1834
Cdd:TIGR04523 636 IKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
998-1763 |
3.69e-13 |
|
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: 75.14 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 998 QKLQLEKVTAEAKIK----KMEEEVLLLEDQNsKFIKEKKLMEDRIaecSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1073
Cdd:pfam05483 88 EKIKKWKVSIEAELKqkenKLQENRKIIEAQR-KAIQELQFENEKV---SLKLEEEIQENKDLIKENNATRHLCNLLKET 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1074 LKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHknnalkVARELQAQIAE 1153
Cdd:pfam05483 164 CARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQH------LEEEYKKEIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1154 LQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDetknheaqIQDMRQRHA 1233
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELED--------IKMSLQRSM 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1234 TALEELSEQLEQAKRFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEK 1312
Cdd:pfam05483 310 STQKALEEDLQIATKTICQLTEEKEAqMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKK 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1313 anklqneldnvSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEEtrqklnlssriRQLEEEKNSLQEQQEEEEEARKN 1392
Cdd:pfam05483 390 -----------SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK-----------KQFEKIAEELKGKEQELIFLLQA 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1393 LEKQVLALQSQLADTKKKVDDDLGTIESLE-EAKKKLLKDVEALSQRleekvlayDKLEKTKNRLQQELDDLTVDLDHQR 1471
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEEHYLKEVEDLKtELEKEKLKNIELTAHC--------DKLLLENKELTQEASDMTLELKKHQ 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1472 QIVSNLEKKQKKFDQLLA--EEKGISARYAEERDRAEAEAREKETKAL--SLARALEEALEAKEEFERQNKQLRADMEDL 1547
Cdd:pfam05483 520 EDIINCKKQEERMLKQIEnlEEKEMNLRDELESVREEFIQKGDEVKCKldKSEENARSIEYEVLKKEKQMKILENKCNNL 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1548 MSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQatedaklRLEVNMQAMKAQFERDLQTRDEQNEEKKrlllk 1627
Cdd:pfam05483 600 KKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN-------KLELELASAKQKFEEIIDNYQKEIEDKK----- 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1628 qVRELEAELEDERKQRALAVASKKKMEIDLkdleaqieaanKARDEVIKQLRKLQAQMKDYQRELEEaRASRDEIFAQSK 1707
Cdd:pfam05483 668 -ISEEKLLEEVEKAKAIADEAVKLQKEIDK-----------RCQHKIAEMVALMEKHKHQYDKIIEE-RDSELGLYKNKE 734
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1708 ESEKKLK-SLEAEILQLQEELASSERARRHAEQERDELADEiansASGKSALLDEKR 1763
Cdd:pfam05483 735 QEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKME----AKENTAILKDKK 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
873-1288 |
4.80e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 4.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 873 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEknilAEQLQAETELFAEAEEMRARLAAK-KQEL 951
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER----HELYEEAKAKKEELERLKKRLTGLtPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 952 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ--------------LEKVTAEakIKKMEEE 1017
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPvcgrelteehrkelLEEYTAE--LKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1018 VLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNK-QEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1096
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1097 DLQdQIAELQAQVDELKVQLTKKEEELqgalarGDDETLHKNNALKVARELQAQIAELqEDFESEKASRNKAEKQKRDLS 1176
Cdd:PRK03918 547 ELE-KLEELKKKLAELEKKLDELEEEL------AELLKELEELGFESVEELEERLKEL-EPFYNEYLELKDAEKELEREE 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1177 EELEALKTELEDTLDTTA-AQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEK 1255
Cdd:PRK03918 619 KELKKLEEELDKAFEELAeTEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
410 420 430
....*....|....*....|....*....|...
gi 1907083610 1256 NKQGLETdNKELACEVKVLQQVKAESEHKRKKL 1288
Cdd:PRK03918 699 LKEELEE-REKAKKELEKLEKALERVEELREKV 730
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1308-1957 |
4.92e-13 |
|
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: 74.67 E-value: 4.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1308 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEE 1387
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1388 EARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDL 1467
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1468 DHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLradmedl 1547
Cdd:TIGR04523 197 LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQL------- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1548 msskDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLK 1627
Cdd:TIGR04523 270 ----SEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKL---EEIQNQISQNNKIISQLNE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1628 QVRELEAELEDERKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSK 1707
Cdd:TIGR04523 343 QISQLKKELTNSESE-------NSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK-------LNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1708 ESEKKLKSLEAEILQLqeelasserarrhaEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN 1787
Cdd:TIGR04523 409 QKDEQIKKLQQEKELL--------------EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1788 DRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQ--EA 1865
Cdd:TIGR04523 475 RSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNKddFE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1866 KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATranasrrKLQRELDDATEAN 1945
Cdd:TIGR04523 554 LKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS-------SLEKELEKAKKEN 626
|
650
....*....|..
gi 1907083610 1946 EGLSREVSTLKN 1957
Cdd:TIGR04523 627 EKLSSIIKNIKS 638
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
834-1480 |
5.12e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 834 RKAFAKKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEgeleemERKH 913
Cdd:PTZ00121 1372 KKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAE------EAKK 1445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 914 QQLLEEKnilAEQLQAETELFAEAEEMRARLAAKKQELEeilhdlesrveeeeernqilqnekkkmqahiqdleeqldee 993
Cdd:PTZ00121 1446 ADEAKKK---AEEAKKAEEAKKKAEEAKKADEAKKKAEE----------------------------------------- 1481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 994 egARQKLQLEKVTAEAkiKKMEEEVLLLEDQNSKFIKEKKLMEDRIAEcSSQLAEEEEKAKNLAKIRNKQEVMISDLEER 1073
Cdd:PTZ00121 1482 --AKKADEAKKKAEEA--KKKADEAKKAAEAKKKADEAKKAEEAKKAD-EAKKAEEAKKADEAKKAEEKKKADELKKAEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1074 LKKEEKTRQELEKAKRKldgETTDLQDQIAELQAQVDELKVQ----LTKKEEELQGALARGDDETLHKNNALKVARELQA 1149
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAE---EDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKK 1633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1150 QIAELQEDFESEKasrNKAEKQKRdlSEELEALKTELEdtldttaAQQELRTKREQEvaELKKALEDETKNHEAQIQDmr 1229
Cdd:PTZ00121 1634 KVEQLKKKEAEEK---KKAEELKK--AEEENKIKAAEE-------AKKAEEDKKKAE--EAKKAEEDEKKAAEALKKE-- 1697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1230 qrhatalEELSEQLEQAKRFKAnlEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE------LHAKVSEGD 1303
Cdd:PTZ00121 1698 -------AEEAKKAEELKKKEA--EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEeekkkiAHLKKEEEK 1768
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1304 RLRVELAEKANKLQNELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEET----RQKLNLSSRIRQLEEEKNSL 1379
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELD------EEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNlvinDSKEMEDSAIKEVADSKNMQ 1842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1380 QEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQE 1459
Cdd:PTZ00121 1843 LEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKD 1922
|
650 660
....*....|....*....|.
gi 1907083610 1460 lDDLTVDLDHQRQIVSNLEKK 1480
Cdd:PTZ00121 1923 -EYIKRDAEETREEIIKISKK 1942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1284-1741 |
2.06e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1284 KRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAEKKGIKFAKDAAGLEsQLQDTQELLQEETRQKL 1363
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1364 NLSSRIRQLEEEKNSLQeqqeeeeeARKNLEKQVLALQSQLADTKKKVDDDL-GTIESLEEAKKKLLKDVEALSQRLEEK 1442
Cdd:COG4717 140 ELAELPERLEELEERLE--------ELRELEEELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1443 VLAYDKLEKTKNRLQQELDDLTVDLDHQrqivsNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA-- 1520
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAA-----ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGll 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1521 --------RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATE 1590
Cdd:COG4717 287 allflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEelQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1591 DAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERK--QRALAVASKKKMEIDLKDLEAQIEAAN 1668
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK-EELEELEEQLEELLGelEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1669 KARDEVIKQLRKLQAQMKDY--QRELEEARASRDEIFAQskesekkLKSLEAEILQLQEELASSERARRHAEQER 1741
Cdd:COG4717 446 EELEELREELAELEAELEQLeeDGELAELLQELEELKAE-------LRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
871-1332 |
2.08e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 871 KVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQE 950
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKR 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 951 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIK 1030
Cdd:PRK03918 354 LEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK----KAIE 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1031 EKKLMEDRIAECSSQLAEEEEKaknlaKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT---------DLQDQ 1101
Cdd:PRK03918 430 ELKKAKGKCPVCGRELTEEHRK-----ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeseliklkELAEQ 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVQ-LTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASRNKA---EKQKRDLSE 1177
Cdd:PRK03918 505 LKELEEKLKKYNLEeLEKKAEEYEKLKEK--------------LIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEE 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1178 ELEALKTELEdtldttaaqqELRTKREQEVAELKKALEdETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNK 1257
Cdd:PRK03918 571 ELAELLKELE----------ELGFESVEELEERLKELE-PFYNEYLELKDAEKE----LEREEKELKKLEEELDKAFEEL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1258 QGLETDNKELACEVKVLQQVKAESEHKRK-----KLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1332
Cdd:PRK03918 636 AETEKRLEELRKELEELEKKYSEEEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
878-1480 |
3.41e-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: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 72.13 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 878 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNilaEQLQAETELFAEAEEMRARLaakKQELEEILHD 957
Cdd:pfam01576 515 VERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNRL---QQELDDLLVD 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 958 LESrveeeeeRNQILQNEKKKMQ-----------AHIQDLEEQLDEEEGARQK----LQLEKVTAEAKIKKME------- 1015
Cdd:pfam01576 589 LDH-------QRQLVSNLEKKQKkfdqmlaeekaISARYAEERDRAEAEAREKetraLSLARALEEALEAKEElertnkq 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1016 -----EEVLLLEDQNSKFIKE----KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEK 1086
Cdd:pfam01576 662 lraemEDLVSSKDDVGKNVHElersKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE 741
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1087 AKRKLdgettdLQDQIAELQAQVDELKVQLT-------KKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFE 1159
Cdd:pfam01576 742 EKRRQ------LVKQVRELEAELEDERKQRAqavaakkKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1160 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAEL----------KKALEDETKNHEAQIQDMR 1229
Cdd:pfam01576 816 EARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELadeiasgasgKSALQDEKRRLEARIAQLE 895
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1230 qrhatalEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkaeSEHKRKKLDAQVQELHAKVSEgdrlrvel 1309
Cdd:pfam01576 896 -------EELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQK----SESARQQLERQNKELKAKLQE-------- 956
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1310 aekanklqneldnvstlLEEAEKKgiKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEeknslqeqqeeeeea 1389
Cdd:pfam01576 957 -----------------MEGTVKS--KFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEK--------------- 1002
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1390 rknlekqvlalqsQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDH 1469
Cdd:pfam01576 1003 -------------KLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNES 1069
|
650
....*....|.
gi 1907083610 1470 QRQIVSNLEKK 1480
Cdd:pfam01576 1070 MNREVSTLKSK 1080
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
930-1658 |
3.78e-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: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 930 ETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEA 1009
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1010 KIKKMEEEVLLLEDQNSKFIKEK----KLMEDRIAECSSQLAEEEEKAK----NLAKIRNKQEVMISDLEERLKK----- 1076
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKaltgKHQDVTAKYNRRRSKIKEQNNRdiagi 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1077 EEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddETLHKNNALKVARELQAQIAELQE 1156
Cdd:pfam12128 396 KDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG----ELKLRLNQATATPELLLQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1157 DFESEKASRNKAEKQKRDLSEELEALKTELEDTLDttAAQQElrtkrEQEVAELKKALEdetknhEAQIQDMRQRHaTAL 1236
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASE--ALRQA-----SRRLEERQSALD------ELELQLFPQAG-TLL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1237 EELSEQLEQAKRFKANLEKNKQGLETDnkeLACEVkVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRvelaEKANKL 1316
Cdd:pfam12128 538 HFLRKEAPDWEQSIGKVISPELLHRTD---LDPEV-WDGSVGGELNLYGVKLDLKRIDVPEWAASEEELR----ERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1317 QNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQeetrqklNLSSRIRQLEEEKNSLQeqqeeeeearknlekq 1396
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK-------NARLDLRRLFDEKQSEK---------------- 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1397 vLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydklEKTKNRLQQELDDLTVDLDHQRQIVSN 1476
Cdd:pfam12128 667 -DKKNKALAERKDSANER---LNSLEAQLKQLDKKHQAWLEEQKE--------QKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1477 LEKKQKKFDQLLAEEKGISARYAEE-------RDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS 1549
Cdd:pfam12128 735 KAAIAARRSGAKAELKALETWYKRDlaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1550 SKDDVGKNVHELEKSkraLEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQV 1629
Cdd:pfam12128 815 QLSNIERAISELQQQ---LARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQG---SI 888
|
730 740
....*....|....*....|....*....
gi 1907083610 1630 RELEAELEDERKQRALAVASKKKMEIDLK 1658
Cdd:pfam12128 889 GERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1644-1884 |
3.78e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.18 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1644 ALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1723
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1724 QEELasserarrhaEQERDELADEIAnsasgksALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1803
Cdd:COG4942 96 RAEL----------EAQKEELAELLR-------ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1804 LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLK 1883
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
.
gi 1907083610 1884 E 1884
Cdd:COG4942 238 A 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1030-1252 |
6.75e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 6.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1030 KEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQV 1109
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1110 DEL--KVQLTKKEEELQGALARGDDETLHKNNAL--KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTE 1185
Cdd:COG4942 107 AELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1186 LedtldttAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRhATALEELSEQLEQAKRFKAN 1252
Cdd:COG4942 187 R-------AALEALKAERQKLLARLEK----ELAELAAELAELQQE-AEELEALIARLEAEAAAAAE 241
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
31-76 |
1.12e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 61.29 E-value: 1.12e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1907083610 31 TAKKLVWIPSERHGFEAASIKEERGDEVMVELaENGKKAMVNKDDI 76
Cdd:pfam02736 1 DAKKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
905-1506 |
1.89e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.56 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 905 ELEEMERKHQQLLEEKnilaEQLQAETELFAEAEEmRARLAAKKQELEEILHDLesRVEEEEERNQILQNEKKKMQAhiq 984
Cdd:COG4913 233 HFDDLERAHEALEDAR----EQIELLEPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRA--- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 985 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLmeDRIAECSSQLAEEEEKAKNLAKIRNKQE 1064
Cdd:COG4913 303 -----------ELARLEAELERLEARLDALREELDELEAQ----IRGNGG--DRLEQLEREIERLERELEERERRRARLE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1065 VMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD--DETLHK- 1137
Cdd:COG4913 366 ALLAALGLPLPASAEefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLAl 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1138 ----NNALKVARELQAQIAELQEDFESEKASRNKAEK----QKRDL--SEELEALKTELEDTLDTTAAQQELRTKREQEV 1207
Cdd:COG4913 446 rdalAEALGLDEAELPFVGELIEVRPEEERWRGAIERvlggFALTLlvPPEHYAAALRWVNRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1208 AELKKALED------ETKNHEAQ--IQD-MRQRHATALEELSEQLEQAKR-------FKANL---EKNKQGLET------ 1262
Cdd:COG4913 526 PERPRLDPDslagklDFKPHPFRawLEAeLGRRFDYVCVDSPEELRRHPRaitragqVKGNGtrhEKDDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1263 -DNKE----LACEVKVLQQVKAESEHKRKKLDAQVQEL------HAKVSEGDRLRVELAEkankLQNELDNVSTLLEEAE 1331
Cdd:COG4913 606 fDNRAklaaLEAELAELEEELAEAEERLEALEAELDALqerreaLQRLAEYSWDEIDVAS----AEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1332 KkgikFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKkv 1411
Cdd:COG4913 682 A----SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF-- 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1412 dDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlAYDKLEKTKNRLQQELDDLTVDLD------------HQRQIVSNLEK 1479
Cdd:COG4913 756 -AAALGDAVERELRENLEERIDALRARLNR---AEEELERAMRAFNREWPAETADLDadleslpeylalLDRLEEDGLPE 831
|
650 660 670
....*....|....*....|....*....|..
gi 1907083610 1480 KQKKFDQLLAEEKG-----ISARYAEERDRAE 1506
Cdd:COG4913 832 YEERFKELLNENSIefvadLLSKLRRAIREIK 863
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1566-1961 |
2.43e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.17 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1566 RALEQQVEEMRTQ---LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQ 1642
Cdd:COG4913 238 ERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1643 RALAVASKKKME--------IDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQrelEEARASRDEIFAQSKESEKKLK 1714
Cdd:COG4913 318 LDALREELDELEaqirgnggDRLEQLEREIERLERELEERERRRARLEALLAALG---LPLPASAEEFAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1715 SLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA----------------------------LLD------ 1760
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNiparllalrdalaealgldeaelpfvgeLIEvrpeee 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1761 -------------------------------EKRRLEARI-AQLEEELEEEQSNMELLNDR------FRKTTLQvDTLNT 1802
Cdd:COG4913 475 rwrgaiervlggfaltllvppehyaaalrwvNRLHLRGRLvYERVRTGLPDPERPRLDPDSlagkldFKPHPFR-AWLEA 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1803 ELAaERSAAQKSDNArQQLER------------QNKEL-------------------KAKLQELEGAVKsKFKATISALE 1851
Cdd:COG4913 554 ELG-RRFDYVCVDSP-EELRRhpraitragqvkGNGTRhekddrrrirsryvlgfdnRAKLAALEAELA-ELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1852 AKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeiFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASR 1931
Cdd:COG4913 631 ERLEALEAELDALQERREALQRLAEYSWDEID--VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510
....*....|....*....|....*....|
gi 1907083610 1932 RKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:COG4913 709 DELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1094-1863 |
3.98e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.79 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1094 ETTDLQDQIAELQAQVDELkvqltkkeEELQGALargdDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-----A 1168
Cdd:COG4913 219 EEPDTFEAADALVEHFDDL--------ERAHEAL----EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlrlwfA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1169 EKQKRDLSEELEALKTELEDTldttaaqqelrtkrEQEVAELKKALEDetknHEAQIQDMRQRHATALEELSEQLEQakr 1248
Cdd:COG4913 287 QRRLELLEAELEELRAELARL--------------EAELERLEARLDA----LREELDELEAQIRGNGGDRLEQLER--- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1249 fkanleknkqgletdnkelacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRlrvELAEKANKLQNELDNVSTLLE 1328
Cdd:COG4913 346 ---------------------EIERLERELEERERRRARLEALLAALGLPLPASAE---EFAALRAEAAALLEALEEELE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1329 EAEkkgikfaKDAAGLESQLQDTQEllqeetrqklnlssRIRQLEEEKNSLQEQqeeeeeaRKNLEKQVLALQSQLADTK 1408
Cdd:COG4913 402 ALE-------EALAEAEAALRDLRR--------------ELRELEAEIASLERR-------KSNIPARLLALRDALAEAL 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1409 KKVDDDL-----------------GTIESL-----------EEAKKKLLKDVEALSQRLEekvLAYDKLEKT-KNRLQQE 1459
Cdd:COG4913 454 GLDEAELpfvgelievrpeeerwrGAIERVlggfaltllvpPEHYAAALRWVNRLHLRGR---LVYERVRTGlPDPERPR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1460 LDDltvdldhqRQIVSNLEKKQKKFDQLLAEEkgisarYAEERDRA---EAEAREKETKALSLARaleealeakeeferq 1536
Cdd:COG4913 531 LDP--------DSLAGKLDFKPHPFRAWLEAE------LGRRFDYVcvdSPEELRRHPRAITRAG--------------- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1537 nkqlradmedLMSSkddvGKNVHELEKSKRALEQQV--EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDlqtr 1614
Cdd:COG4913 582 ----------QVKG----NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---- 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1615 deqneEKKRLLLKQVRELEAElederkqralavaskkkmEIDLKDLEAQIEAANKARDEVIK---QLRKLQAQMKDYQRE 1691
Cdd:COG4913 644 -----QERREALQRLAEYSWD------------------EIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAE 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1692 LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELassERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDA 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1772 LEEELEEEQSNMELLNDRFRKT-TLQVDTLNTELAAERSAAQKsdnaRQQLERQN-KELKAKLQELEGAVKSKFKATI-S 1848
Cdd:COG4913 778 LRARLNRAEEELERAMRAFNREwPAETADLDADLESLPEYLAL----LDRLEEDGlPEYEERFKELLNENSIEFVADLlS 853
|
810
....*....|....*
gi 1907083610 1849 ALEAKIGQLEEQLEQ 1863
Cdd:COG4913 854 KLRRAIREIKERIDP 868
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1071-1901 |
1.34e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.90 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1071 EERLKKEEKT---RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlHKN---NAL--- 1141
Cdd:COG3096 278 NERRELSERAlelRRELFGARRQLAEE----QYRLVEMARELEELSARESDLEQDYQAASD-------HLNlvqTALrqq 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1142 -KVAR------ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELED---TLDT--TAA---QQELRTKRE-Q 1205
Cdd:COG3096 347 eKIERyqedleELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADyqqALDVqqTRAiqyQQAVQALEKaR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1206 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLEtdnkelacevKVLQQVKAESEHKR 1285
Cdd:COG3096 427 ALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVC----------KIAGEVERSQAWQT 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1286 -KKLDAQVQELHAKVSEGDRLRVELAEkANKLQNELDNVSTLLEEaekkgikFAKDAAGLESQLQDTQELLQEETRQKLN 1364
Cdd:COG3096 497 aRELLRRYRSQQALAQRLQQLRAQLAE-LEQRLRQQQNAERLLEE-------FCQRIGQQLDAAEELEELLAELEAQLEE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1365 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLkdvealsQRLEE 1441
Cdd:COG3096 569 LEEQAAEAVEQRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLL-------ERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1442 KVLAYDKLEKTKNRLQQElddltvdldhqrqiVSNLEKKQKKFD---QLLAEEKG------------------ISARYAE 1500
Cdd:COG3096 642 ATVERDELAARKQALESQ--------------IERLSQPGGAEDprlLALAERLGgvllseiyddvtledapyFSALYGP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1501 ER------DraeaeareketkaLSLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEK----- 1563
Cdd:COG3096 708 ARhaivvpD-------------LSAVK-------------EQLAGLEDCPEDLYliegdpDSFDDSVFDAEELEDavvvk 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1564 -SKRAL----------------EQQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEE 1620
Cdd:COG3096 762 lSDRQWrysrfpevplfgraarEKRLEELRAERDELAEQY-----AKASFDVQkLQRLHQAFSQFVGGHlavafAPDPEA 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1621 KKRLLLKQVRELEAELEDERKQralavaskkkmeidLKDLEAQIEAANkardEVIKQLRKLQAQM------------KDY 1688
Cdd:COG3096 837 ELAALRQRRSELERELAQHRAQ--------------EQQLRQQLDQLK----EQLQLLNKLLPQAnlladetladrlEEL 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1689 QRELEEARASRDEIFAQSK---ESEKKLKSLEAEILQ---LQEELASSERARRHAEQERDELADEIANSA----SGKSAL 1758
Cdd:COG3096 899 REELDAAQEAQAFIQQHGKalaQLEPLVAVLQSDPEQfeqLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1759 LDEKRRLEARIAQLEEELEEEQSNmelLNDRFRKTTLQVDTLNTELAAERSAAqksDNARQQLerqnKELKAKLQELEGA 1838
Cdd:COG3096 979 LGENSDLNEKLRARLEQAEEARRE---AREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTL----QELEQELEELGVQ 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1839 V-----------KSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqveDERRHADQYKE 1901
Cdd:COG3096 1049 AdaeaeerarirRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYK-------QEREQVVQAKA 1115
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1661-1884 |
1.92e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.85 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1661 EAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELasserarrhaEQE 1740
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI----------EER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1741 RDELADEIA------NSASGKSALLDekrrleariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKs 1814
Cdd:COG3883 85 REELGERARalyrsgGSVSYLDVLLG---------SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1815 dnARQQLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1884
Cdd:COG3883 155 --KLAELEALKAELEAAKAELEAQQAEQ-EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1638-1960 |
2.31e-10 |
|
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: 66.24 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1638 DERKQRALAvaskkkmeiDLKDLEAQIEAANKARDEVIKQLRKLQAQ------MKDYQRELEEARASrdEIFAQSKESEK 1711
Cdd:TIGR02169 169 DRKKEKALE---------ELEEVEENIERLDLIIDEKRQQLERLRRErekaerYQALLKEKREYEGY--ELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1712 KLKSLEAEILQLQEELASSERarrhaeqERDELADEIAnsasgksALLDEKRRLEARIaqleeeleeeqsnMELLNDRFR 1791
Cdd:TIGR02169 238 QKEAIERQLASLEEELEKLTE-------EISELEKRLE-------EIEQLLEELNKKI-------------KDLGEEEQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1792 KTTLQVDTLNTELAaersaaqksdnarqQLERQNKELKAKLQELEGAVKsKFKATISALEAKIGQLEEQLEQEAKERAAA 1871
Cdd:TIGR02169 291 RVKEKIGELEAEIA--------------SLERSIAEKERELEDAEERLA-KLEAEIDKLLAEIEELEREIEEERKRRDKL 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1872 NKLVRRTEKKLKEIFMQVEDE-------RRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA 1944
Cdd:TIGR02169 356 TEEYAELKEELEDLRAELEEVdkefaetRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330
....*....|....*.
gi 1907083610 1945 NEGLSREVSTLKNRLR 1960
Cdd:TIGR02169 436 INELEEEKEDKALEIK 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1135-1852 |
3.18e-10 |
|
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: 65.63 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1135 LHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAA-QQELRTKREQeVAELKKA 1213
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQ-WKEKRDE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1214 LEDETKNHEAQIQDMRqrhatalEELSEQLEQAKRF-KANLEKNKQGLETdnkelacevkvLQQVKAESEHKRKKLDAQV 1292
Cdd:pfam12128 306 LNGELSAADAAVAKDR-------SELEALEDQHGAFlDADIETAAADQEQ-----------LPSWQSELENLEERLKALT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1293 QELHAKVSEGDRLRV----ELAEKANKLQNELDNVStllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETR-QKLNLSS 1367
Cdd:pfam12128 368 GKHQDVTAKYNRRRSkikeQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESELREQLEAGKLEFNeEEYRLKS 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1368 RIRQL----------EEEKNSLQEQQEEEEEARKNLE---KQVLALQSQLADTKKKVDddlgtiesleEAKKKLlkdvEA 1434
Cdd:pfam12128 445 RLGELklrlnqatatPELLLQLENFDERIERAREEQEaanAEVERLQSELRQARKRRD----------QASEAL----RQ 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1435 LSQRLEEkvlaydklektknrLQQELDDLTVDLDHQR-QIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEAEAREKE 1513
Cdd:pfam12128 511 ASRRLEE--------------RQSALDELELQLFPQAgTLLHFLRKEAPDWEQSIG--KVISPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1514 TKALSLARALEEALEAKEEFERQ-NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDA 1592
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDVPEWAAsEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLD 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1593 KLRLEVNMQAMKAQFERDLQTRDEQNEE--------KKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQI 1664
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERKDSANErlnsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALL 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1665 EAANKARDEVIKqlRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaEILQLQEELASSERARRHA-EQERDE 1743
Cdd:pfam12128 735 KAAIAARRSGAK--AELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE-RIAVRRQEVLRYFDWYQETwLQRRPR 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1744 LADEIANSASGKSALLDEKRRLEA----RIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTeLAAERSAAQKSDNARQ 1819
Cdd:pfam12128 812 LATQLSNIERAISELQQQLARLIAdtklRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLAT-LKEDANSEQAQGSIGE 890
|
730 740 750
....*....|....*....|....*....|....*.
gi 1907083610 1820 QLeRQNKELKAKLQELEGAVKSK---FKATISALEA 1852
Cdd:pfam12128 891 RL-AQLEDLKLKRDYLSESVKKYvehFKNVIADHSG 925
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
879-1488 |
3.95e-10 |
|
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: 65.04 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 879 TRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDL 958
Cdd:TIGR04523 64 NKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 959 ESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEdqnsKFIKEKKLMEdr 1038
Cdd:TIGR04523 144 LTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK----KKIQKNKSLE-- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1039 iaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEK----TRQELEKAKRKLDGETTDLQD---QIAELQAQVDE 1111
Cdd:TIGR04523 218 -----SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTqlnqLKDEQNKIKKQLSEKQKELEQnnkKIKELEKQLNQ 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKVQLtkkeeelqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:TIGR04523 293 LKSEI----------------SDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1192 TTAAQQELRTKREQEVAELKKALE---DETKNHEAQIQDMRQrhataleelseQLEQAKRFKANLEKNKQGLETDNKELA 1268
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQsykQEIKNLESQINDLES-----------KIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1269 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQL 1348
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1349 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQL--ADTKKKVDDDLGTIESLEEAKK 1426
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI-------SDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQK 578
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1427 KLLKDVEALSQRLeekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL 1488
Cdd:TIGR04523 579 SLKKKQEEKQELI-------DQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1664-1961 |
4.69e-10 |
|
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: 65.09 E-value: 4.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1664 IEAANKARDEVIKQLrklqAQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELassERARRHAEqERDE 1743
Cdd:TIGR02169 148 ISMSPVERRKIIDEI----AGVAEFDRKKEKALEELEEV----EENIERLDLIIDEKRQQLERL---RREREKAE-RYQA 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1744 LADEIANSASgkSALLDEKRRLEARIAQLEEELEEEQSNMEllndrfrKTTLQVDTLNTELAAersaaqksdnARQQLER 1823
Cdd:TIGR02169 216 LLKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELE-------KLTEEISELEKRLEE----------IEQLLEE 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1824 QNKELKAKLQELEGAVKSK---FKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1900
Cdd:TIGR02169 277 LNKKIKDLGEEEQLRVKEKigeLEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1901 EQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
883-1329 |
4.76e-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: 64.74 E-value: 4.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 883 EELQAKDEELLKVKEKQTKVEGE-------LEEMERKHQQLLEEK----NILAEQLQAETELFAEAEEMRARLAAKKQEL 951
Cdd:pfam05483 331 EEKEAQMEELNKAKAAHSFVVTEfeattcsLEELLRTEQQRLEKNedqlKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 952 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK- 1030
Cdd:pfam05483 411 KKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEl 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1031 ----EKKLMEDR--IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1104
Cdd:pfam05483 491 tahcDKLLLENKelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1105 LQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKT 1184
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1185 ELEDTLDTTAAQQELRTKREQEV---AELKKALEDETKNHEAQIqDMRQRHATAleelseqleqakRFKANLEKNKQGLE 1261
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKISEEKLleeVEKAKAIADEAVKLQKEI-DKRCQHKIA------------EMVALMEKHKHQYD 717
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1262 TDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAK-VSEGDRLRVELAEKANKLQNELDNVSTLLEE 1329
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAElLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1144-1937 |
4.77e-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: 65.07 E-value: 4.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1144 ARELQAQIAELQEDFESEKASRNKAEKQKRDLSE---ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKN 1220
Cdd:TIGR00606 219 ACEIRDQITSKEAQLESSREIVKSYENELDPLKNrlkEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1221 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ-QVKAESEHKRKKlDAQVQELHAkv 1299
Cdd:TIGR00606 299 TDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlQADRHQEHIRAR-DSLIQSLAT-- 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1300 segdRLRVELAEKANKLQNELDNVSTLLEEAEKKGikfAKDAAGLESQLQDTQELLQE---ETRQKLNLSSRIRQLEEEK 1376
Cdd:TIGR00606 376 ----RLELDGFERGPFSERQIKNFHTLVIERQEDE---AKTAAQLCADLQSKERLKQEqadEIRDEKKGLGRTIELKKEI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1377 nslqeqqeeeeearknLEKQvlalQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSqRLEEKVLAYDKLEKTKNRL 1456
Cdd:TIGR00606 449 ----------------LEKK----QEELKFVIKELQQLEGSSDRILELDQELRKAERELS-KAEKNSLTETLKKEVKSLQ 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1457 QQELDdltvdldhqrqivsnLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKalslaraleealeakeefERQ 1536
Cdd:TIGR00606 508 NEKAD---------------LDRKLRKLDQEMEQLN----HHTTTRTQMEMLTKDKMDK------------------DEQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1537 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqAMKAQFERDLQTRDE 1616
Cdd:TIGR00606 551 IRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-----------QNKNHINNELESKEE 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1617 QneekkrlllkqvrelEAELEDerkqRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1696
Cdd:TIGR00606 620 Q---------------LSSYED----KLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCC 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1697 ASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1776
Cdd:TIGR00606 681 PVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDI 760
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1777 EEEQSNMElLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVK----SKFKATISALEA 1852
Cdd:TIGR00606 761 QRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTvqqvNQEKQEKQHELD 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1853 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRR 1932
Cdd:TIGR00606 840 TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLE 919
|
....*
gi 1907083610 1933 KLQRE 1937
Cdd:TIGR00606 920 KDQQE 924
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1098-1884 |
4.96e-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: 64.74 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1098 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVAREL-QAQIAELQE-DFESEKASRNKAE--KQKR 1173
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIiEAQRKAIQElQFENEKVSLKLEEeiQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1174 DLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIqdmrqrhaTALEELSEQLEQAK-RFKAN 1252
Cdd:pfam05483 145 DLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMI--------LAFEELRVQAENARlEMHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1253 LEKNKQGLETDNKELACEVKvlqqvkaESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEK 1332
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEIN-------DKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1333 KGIKFAKDAAGLESQLQ---DTQELLQEETRQKlnlSSRIRQLEEEKNSlqeQQEEEEEARKNLEKQVLALQSQLADTKK 1409
Cdd:pfam05483 290 KKDHLTKELEDIKMSLQrsmSTQKALEEDLQIA---TKTICQLTEEKEA---QMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1410 KVDDDLGTIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTVDLDHQRQIVSnlekKQKKFDQLLA 1489
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILAEDEKLLD----EKKQFEKIAE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1490 EEKGisaryAEERDRAEAEAREKETKALSLarALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1569
Cdd:pfam05483 433 ELKG-----KEQELIFLLQAREKEIHDLEI--QLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1570 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKaqfERDLQTRDEqneekkrllLKQVRELEAELEDERKQRAlavas 1649
Cdd:pfam05483 506 QEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDE---------LESVREEFIQKGDEVKCKL----- 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1650 kKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAS 1729
Cdd:pfam05483 569 -DKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1730 serARRHAEQERDELADEIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellnDRFRKTTLQVDTLNTELAAERS 1809
Cdd:pfam05483 648 ---AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIA------------------DEAVKLQKEIDKRCQHKIAEMV 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1810 AAQKSDNAR--QQLERQNKEL---KAKLQElEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1884
Cdd:pfam05483 707 ALMEKHKHQydKIIEERDSELglyKNKEQE-QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1660-1912 |
7.05e-10 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 64.27 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1660 LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIF--AQSKESEKKLKSLEAEILQLQEELASSErARRHA 1737
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDlsEEAKLLLQQLSELESQLAEARAELAEAE-ARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1738 EQERDELADEIANSASGKSALldekRRLEARIAQleeeleeeqsnmellndrfrkttlqvdtLNTELAAERSAAQKSDNA 1817
Cdd:COG3206 245 LRAQLGSGPDALPELLQSPVI----QQLRAQLAE----------------------------LEAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1818 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLvrrtEKKLKEIFMQVEDERRHAD 1897
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYE 368
|
250
....*....|....*
gi 1907083610 1898 QYKEQMEKANARMKQ 1912
Cdd:COG3206 369 SLLQRLEEARLAEAL 383
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1560-1771 |
7.13e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVRELEAELEDE 1639
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR-IRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1640 RKQRA--LAVASKKKMEIDLKDLEAQIEAANKARD-EVIKQL-RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKS 1715
Cdd:COG4942 103 KEELAelLRALYRLGRQPPLALLLSPEDFLDAVRRlQYLKYLaPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1716 LEAEILQLQEELASSERARRHAEQERDELADEIAnsasgksALLDEKRRLEARIAQ 1771
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELA-------ELQQEAEELEALIAR 231
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
877-1333 |
9.55e-10 |
|
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: 63.89 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEmerkHQQLLEEKNILAEQLQAE-TELFAEAEEMrarlaaKKQELEEIL 955
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSE----KQKELEQNNKKIKELEKQlNQLKSEISDL------NNQKEQDWN 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 956 HDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLM 1035
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1036 EDRIAECSSQLAEEEEKAKNlakirnkqevmisdLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ 1115
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQ--------------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1116 LTKKEeelqgalargddetlhknnalKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL---KTELEDTLDT 1192
Cdd:TIGR04523 456 IKNLD---------------------NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLneeKKELEEKVKD 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1193 TAAQQELRTKREQEVAELKKALEDETKNHEAQIQDM-----RQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKEL 1267
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDdfelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1268 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKK 1333
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1067-1243 |
1.08e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 60.71 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1067 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNAlKVARE 1146
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNV-RNNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1147 LQAqiaeLQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaqQELRTKREQEVAELKKALEDETKNHEAQIQ 1226
Cdd:COG1579 91 YEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAELE 159
|
170
....*....|....*..
gi 1907083610 1227 DMRQRHATALEELSEQL 1243
Cdd:COG1579 160 ELEAEREELAAKIPPEL 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1179-1650 |
1.11e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.63 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1179 LEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQ 1258
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE--------LEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1259 GLET--DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiK 1336
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ---D 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1337 FAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK-NLEKQVLALQSQLADTKKKVDDDL 1415
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlLIAAALLALLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1416 G----TIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEE 1491
Cdd:COG4717 277 GvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1492 KGISARYAEER---------DRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMS--SKDDVGKNVHE 1560
Cdd:COG4717 357 EELEEELQLEEleqeiaallAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1561 LEKSKRALEQQVEEMRTQLEELEDELQATEDaklrlEVNMQAMKAQFERDLQTRDEQNEE--KKRLLLKQVRELEAELED 1638
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEwaALKLALELLEEAREEYRE 511
|
490
....*....|..
gi 1907083610 1639 ERKQRALAVASK 1650
Cdd:COG4717 512 ERLPPVLERASE 523
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1098-1851 |
1.12e-09 |
|
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: 63.69 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1098 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD---ETLHKNNALKvaRELQAQIAELQEdfesekasrnkaekQKRD 1174
Cdd:pfam10174 1 LQAQLRDLQRENELLRRELDIKESKLGSSMNSIKTfwsPELKKERALR--KEEAARISVLKE--------------QYRV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1175 LSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDE------TKNHEAQIQDMRQRHATALEELSEQLEQakr 1248
Cdd:pfam10174 65 TQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKfstpelTEENFRRLQSEHERQAKELFLLRKTLEE--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1249 FKANLEKNKQGLETDNKELACEVKVLQ-----QVKAESEHKRKK----LDAQVQE----LHAKVSEGDRLRVELAEKaNK 1315
Cdd:pfam10174 142 MELRIETQKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRriaeAEMQLGHlevlLDQKEKENIHLREELHRR-NQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1316 LQNELDNVSTLLEEAEKKGIKFAKdaagLESQLQDTQELLQE-ETRQKLNLSSR---IRQLEEEKNSLQEQQEEEEEARK 1391
Cdd:pfam10174 221 LQPDPAKTKALQTVIEMKDTKISS----LERNIRDLEDEVQMlKTNGLLHTEDReeeIKQMEVYKSHSKFMKNKIDQLKQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1392 NLEK---QVLALQSQLADTKKKVDDDLGTIESLEE---AKKK----LLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELD 1461
Cdd:pfam10174 297 ELSKkesELLALQTKLETLTNQNSDCKQHIEVLKEsltAKEQraaiLQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1462 DLTVDLDHQRQIVSNLEKK----QKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLaraleealeakeeferqn 1537
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKinvlQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL------------------ 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1538 kqlrADMEDLMSSKDDVGKNV-HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQferdlQTRDE 1616
Cdd:pfam10174 439 ----TTLEEALSEKERIIERLkEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEH-----ASSLA 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1617 QNEEKKRLLLKQvreLEAELEDERKQRALAVASKKKMEidlkdleaQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR 1696
Cdd:pfam10174 510 SSGLKKDSKLKS---LEIAVEQKKEECSKLENQLKKAH--------NAEEAVRTNPEINDRIRLLEQEVARYKEESGKAQ 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1697 ASRDEIFAQSKESE-------KKLKSLEAEILQLQEELASSERARRHAEQERDEladeiansasgKSALLDEkrrlEARI 1769
Cdd:pfam10174 579 AEVERLLGILREVEnekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK-----------KGAQLLE----EARR 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1770 AQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSD----NARQQLERQNKE-LKAKLQELEGAVKSKfK 1844
Cdd:pfam10174 644 REDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDghltNLRAERRKQLEEiLEMKQEALLAAISEK-D 722
|
....*..
gi 1907083610 1845 ATISALE 1851
Cdd:pfam10174 723 ANIALLE 729
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1362-1958 |
1.14e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1362 KLNLSSRIRQLEEEKNSLQEQQEEEEeaRKNLEKQVLALQSQLADTKKKVDDdlGTIEslEEAKKKLLKDVEALSQRLEE 1441
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAK--EDNRADEATEEAFGKAEEAKKTET--GKAE--EARKAEEAKKKAEDARKAEE 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1442 KVLAYDKLEKTKNRLQQelDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEkgisARYAEERDRAEAEAREKETKALSLAR 1521
Cdd:PTZ00121 1133 ARKAEDARKAEEARKAE--DAKRVEIARKAEDARKAEEARKAEDAKKAEA----ARKAEEVRKAEELRKAEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1522 ALEEALEAKEEFERQNKQLRADMEDLMSSKDDVgknvhelEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEvnmQ 1601
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDA-------EEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE---E 1276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1602 AMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL----------AVASKKKMEIDLKDLEAQIEAANKAR 1671
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAkkkaeeakkkADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1672 DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEA-----EILQLQEELASSERARRHAEQERDelAD 1746
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkkadELKKAAAAKKKADEAKKKAEEKKK--AD 1434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1747 EIANSASGKSALLDEKRRLE-ARIAQLEEELEEEQSNMELLndrfRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQN 1825
Cdd:PTZ00121 1435 EAKKKAEEAKKADEAKKKAEeAKKAEEAKKKAEEAKKADEA----KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1826 KELKAKLQELEGAVKSKFKATISALEAKIGQLEEQleQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEK 1905
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1906 ANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNR 1958
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1559-1961 |
1.29e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1559 HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFE-RDLQTRDEQNEEKkrllLKQVRELEAELE 1637
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLEELEER----LEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1638 DERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1716
Cdd:COG4717 167 ELEAELAeLQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1717 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQ 1796
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1797 VDTLNTELAAE--RSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1873
Cdd:COG4717 327 ALGLPPDLSPEelLELLDRIEELQELLREAEElEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1874 LVRRTEKKLKEIFMQVEDErrhadqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE--GLSRE 1951
Cdd:COG4717 407 LEEQLEELLGELEELLEAL---------DEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQE 477
|
410
....*....|
gi 1907083610 1952 VSTLKNRLRR 1961
Cdd:COG4717 478 LEELKAELRE 487
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
897-1771 |
1.34e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 63.82 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 897 EKQTKVEGELEemerKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeILHDLESRVeeeeeRNQILQNEK 976
Cdd:COG3096 279 ERRELSERALE----LRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQ-AASDHLNLV-----QTALRQQEK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 977 -KKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV-----------LLLEDQNSKFIKEKKLMEdRIAECSS 1044
Cdd:COG3096 349 iERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladyqQALDVQQTRAIQYQQAVQ-ALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1045 QLAEEEEKAKN----LAKIRNKQEVMIS---DLEERLKKEEKTRQELEKAK---RKLDGETTdlqdqiaelQAQVDELKV 1114
Cdd:COG3096 428 LCGLPDLTPENaedyLAAFRAKEQQATEevlELEQKLSVADAARRQFEKAYelvCKIAGEVE---------RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1115 QLTKKEEELQGALARgddetlhknnalkvARELQAQIAELQEDFESEKASR------NKAEKQKRDLSEELEALKTELED 1188
Cdd:COG3096 499 ELLRRYRSQQALAQR--------------LQQLRAQLAELEQRLRQQQNAErlleefCQRIGQQLDAAEELEELLAELEA 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1189 TLDTTAAQQElrtkreqEVAELKKALEDETKNHEAQIQDMRQRH------ATALEELSEQLEQAkrfkanLEkNKQGLET 1262
Cdd:COG3096 565 QLEELEEQAA-------EAVEQRSELRQQLEQLRARIKELAARApawlaaQDALERLREQSGEA------LA-DSQEVTA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1263 DNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAN-KLQNEL-DNVStlLEeaekkgikfakD 1340
Cdd:COG3096 631 AMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGgVLLSEIyDDVT--LE-----------D 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1341 AAGLESqlqdtqelLQEETRQKL---NLSSRIRQLEEEKNSLQEqqeeeeearknlekqvLALQSQLADTkkkVDDDLGT 1417
Cdd:COG3096 698 APYFSA--------LYGPARHAIvvpDLSAVKEQLAGLEDCPED----------------LYLIEGDPDS---FDDSVFD 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1418 IESLEEAkkkllkDVEALSQRL-------EEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAE 1490
Cdd:COG3096 751 AEELEDA------VVVKLSDRQwrysrfpEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1491 EKGIsaryAEERDrAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRA-LE 1569
Cdd:COG3096 825 HLAV----AFAPD-PEAELAA-------LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADEtLA 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1570 QQVEEMRTQLEELED---ELQATEDAKLRLEVNMQAMK---AQFERdLQTRDEQNEEKKRLL------LKQVRELEAELE 1637
Cdd:COG3096 893 DRLEELREELDAAQEaqaFIQQHGKALAQLEPLVAVLQsdpEQFEQ-LQADYLQAKEQQRRLkqqifaLSEVVQRRPHFS 971
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1638 DERKQRALAVASkkkmeiDLKD-LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL 1716
Cdd:COG3096 972 YEDAVGLLGENS------DLNEkLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1717 EaeilqLQEELASSERARrhaeQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:COG3096 1046 G-----VQADAEAEERAR----IRRDELHEELSQNRSRRSQLEKQLTRCEAEMDS 1091
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1505-1733 |
1.97e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1505 AEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1584
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1585 ELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlkqvrELEAELEDERKQRALAVASKKKMEIDLK-DLEAQ 1663
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRaELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1664 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA 1733
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
881-1608 |
2.46e-09 |
|
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: 62.68 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 881 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEIlhdles 960
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI------ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 961 rveeeeernqILQNEKKKMQAHIQDLEEQLDEEEGARQKLQlekvTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIA 1040
Cdd:TIGR00618 287 ----------NRARKAAPLAAHIKAVTQIEQQAQRIHTELQ----SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1041 ECsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDeLKVQLTKKE 1120
Cdd:TIGR00618 353 QE-IHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1121 EELQGALARGDDETLHknnALKVARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELR 1200
Cdd:TIGR00618 431 KQQELQQRYAELCAAA---ITCTAQCEKLEKIHLQESAQSLKE-REQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPL 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1201 TKREQEV-AELKKALEDE-TKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELAcevKVLQQVK 1278
Cdd:TIGR00618 507 CGSCIHPnPARQDIDNPGpLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT---QCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1279 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEkkgikFAKDAAGLESQLQDTQ-ELLQE 1357
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQ-----CSQELALKLTALHALQlTLTQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1358 ETRQKlnlSSRIRQLEEEKnslqeqqeeeEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1437
Cdd:TIGR00618 659 RVREH---ALSIRVLPKEL----------LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIEN 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1438 RLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQRQIVSNLEKKQKKFDQLLAEEKgISARYAEERDRAEAEAREKETKAL 1517
Cdd:TIGR00618 726 ASSSLGSDLAAREDALNQSLKELMHQ-----ARTVLKARTEAHFNNNEEVTAALQ-TGAELSHLAAEIQFFNRLREEDTH 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1518 SLARALEealeakeeferQNKQLRADMEDLMSSKDdvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE 1597
Cdd:TIGR00618 800 LLKTLEA-----------EIGQEIPSDEDILNLQC------ETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730
....*....|.
gi 1907083610 1598 vnmQAMKAQFE 1608
Cdd:TIGR00618 863 ---QLTQEQAK 870
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
938-1517 |
2.55e-09 |
|
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: 62.53 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 938 EEMRARLAAKKQELEeilhdlesrveeeeERNQILQNEKKKMQAHIQDLEEQLDEEEGARQklqleKVTAEAKIKKMEee 1017
Cdd:pfam10174 140 EEMELRIETQKQTLG--------------ARDESIKKLLEMLQSKGLPKKSGEEDWERTRR-----IAEAEMQLGHLE-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1018 vLLLEDQNSKFIKEKKLMEDRiaecsSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEktrQELEKAKRKLDGETTD 1097
Cdd:pfam10174 199 -VLLDQKEKENIHLREELHRR-----NQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTED 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1098 LQDQIAELQA----------QVDELKVQLTKKEEELQGALARgdDETLHKNNA-----LKVARE-----------LQAQI 1151
Cdd:pfam10174 270 REEEIKQMEVykshskfmknKIDQLKQELSKKESELLALQTK--LETLTNQNSdckqhIEVLKEsltakeqraaiLQTEV 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1152 AELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAqqelrtkREQEVAELKKALE---DETKNHEAQIQDM 1228
Cdd:pfam10174 348 DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDV-------KERKINVLQKKIEnlqEQLRDKDKQLAGL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1229 RQRHA----------TALEELSEQLEQAKRFKANLEKNKqglETDNKELACEVKVLQQvkaesehKRKKLDAQVQELHAK 1298
Cdd:pfam10174 421 KERVKslqtdssntdTALTTLEEALSEKERIIERLKEQR---EREDRERLEELESLKK-------ENKDLKEKVSALQPE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1299 VSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQElLQEETRQKLNLSSRIRQLEEEkns 1378
Cdd:pfam10174 491 LTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-AEEAVRTNPEINDRIRLLEQE--- 566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1379 LQEQQEEEEEARKNLEKqVLALQSQLADTKKKVDDDLGTIESL------EEAKKKL-LKDVEALSQRLEEKVLA---YDK 1448
Cdd:pfam10174 567 VARYKEESGKAQAEVER-LLGILREVENEKNDKDKKIAELESLtlrqmkEQNKKVAnIKHGQQEMKKKGAQLLEearRRE 645
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1449 LEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKAL 1517
Cdd:pfam10174 646 DNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEAL 714
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
925-1293 |
2.77e-09 |
|
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: 62.45 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 925 EQLQAETELFAEAEEMRA-------RLAAKKQELEEILHDLESRVEEEEERNQILQNEK--KKMQAHIQDLEEQLDEEEG 995
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTmtpeytvRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 996 ARQKLQLEKVTAEAKIKKmeEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAE--EEEKAKNLAKIRNKQEVMIsdleER 1073
Cdd:pfam17380 314 RRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIRQEERKRELERirQEEIAMEISRMRELERLQM----ER 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1074 LKKEEKTRQELEKAkRKLDGETTDLQDQIAELQAQVDELK--------VQLTKKEEELQGALARGDDETLHKNNALKVAR 1145
Cdd:pfam17380 388 QQKNERVRQELEAA-RKVKILEEERQRKIQQQKVEMEQIRaeqeearqREVRRLEEERAREMERVRLEEQERQQQVERLR 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1146 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEElealktELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQI 1225
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEE 540
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1226 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQgletdnkelacEVKVLQQVKaESEHKRKKLDAQVQ 1293
Cdd:pfam17380 541 ERRKQQEMEERRRIQEQMRKATEERSRLEAMER-----------EREMMRQIV-ESEKARAEYEATTP 596
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
892-1485 |
3.45e-09 |
|
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: 61.96 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 892 LLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQI 971
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 972 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLE-----KVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQL 1046
Cdd:TIGR04523 286 LEKQLNQLKSEISDLNNQKEQDWNKELKSELKnqekkLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1047 AEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELqga 1126
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI--- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1127 largddetlhknnalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldttaaQQELRTKrEQE 1206
Cdd:TIGR04523 443 ------------------KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK------QKELKSK-EKE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1207 VAELKKaledETKNHEAQIQDMRQRHATALEELSEqleqakrfkanLEKNKQGLETDNKELACEVKvlqqvKAESEHKRK 1286
Cdd:TIGR04523 498 LKKLNE----EKKELEEKVKDLTKKISSLKEKIEK-----------LESEKKEKESKISDLEDELN-----KDDFELKKE 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1287 KLDAQVQELHAKVSE----GDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFakdaagleSQLQDTQELLQEETRQk 1362
Cdd:TIGR04523 558 NLEKEIDEKNKEIEElkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI--------SSLEKELEKAKKENEK- 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1363 lnLSSRIRQLEEEKNSLQEQQeeeeearKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1442
Cdd:TIGR04523 629 --LSSIIKNIKSKKNKLKQEV-------KQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR 699
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1907083610 1443 VLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFD 1485
Cdd:TIGR04523 700 MIRIKDLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKFD 742
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1714-1958 |
3.62e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1714 KSLEAEILQLQEELASSERARRHAEQERDELAdeiansasgksaLLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKT 1793
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIE------------LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1794 tlQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1873
Cdd:COG4913 289 --RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1874 LVRRTEkklkeifMQVEDErrhADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDateanegLSREVS 1953
Cdd:COG4913 367 LLAALG-------LPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-------LEAEIA 429
|
....*
gi 1907083610 1954 TLKNR 1958
Cdd:COG4913 430 SLERR 434
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1539-1871 |
4.00e-09 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 60.85 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1539 QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLevnmQAMKAQFERDLQTRDEQN 1618
Cdd:pfam19220 31 QLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEEL----VARLAKLEAALREAEAAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1619 EEKKRLL---LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEA 1695
Cdd:pfam19220 107 EELRIELrdkTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1696 RASRDEIFAQSKESEKKLKSLEAEILQLQ----EELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEgqlaAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1772 LEEELEEEQSNMELLNDRFRKTTLQVDT-------LNTELAAERSAAQKSDNARQQLERQ----NKELKAKLQELEGAVK 1840
Cdd:pfam19220 267 ARNQLRDRDEAIRAAERRLKEASIERDTlerrlagLEADLERRTQQFQEMQRARAELEERaemlTKALAAKDAALERAEE 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1907083610 1841 S-------------KFKATISALEAKIGQLEEQLEQEAKERAAA 1871
Cdd:pfam19220 347 RiaslsdriaeltkRFEVERAALEQANRRLKEELQRERAERALA 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
883-1301 |
4.23e-09 |
|
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: 61.57 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 883 EELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK-----NILAEQLQAETELFAEAEEMRARLAAKKQELEEILHD 957
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 958 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED 1037
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1038 RIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLT 1117
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1118 KKEEELQgALARGDDETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKA--EKQKRDLSEELEALKTELEDTLDTTA 1194
Cdd:TIGR04523 507 ELEEKVK-DLTKKISSLKEKIEKLESEKkEKESKISDLEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQKSLKKKQE 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1195 AQQELRTKREQEVAELKKALEDETKnheaqiqdmrqrhatALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVL 1274
Cdd:TIGR04523 586 EKQELIDQKEKEKKDLIKEIEEKEK---------------KISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
410 420
....*....|....*....|....*..
gi 1907083610 1275 QQVKAESEHKRKKLDAQVQELHAKVSE 1301
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1435-1884 |
4.44e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1435 LSQRLEEKVLAYDKLE-KTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEerDRAEAEAREKE 1513
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--LREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1514 TKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskddvgknvHELEKSKRALEQQVEEMRTQLEELEDELQATEDAK 1593
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEEL-----------RELEEELEELEAELAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1594 LRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL-----------AVASKKKMEIDLKDLEA 1662
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1663 QIEAA------------------NKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQ 1724
Cdd:COG4717 274 TIAGVlflvlgllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1725 EELASSERARR--HAEQERDELADEIA----NSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDrfrktTLQVD 1798
Cdd:COG4717 354 REAEELEEELQleELEQEIAALLAEAGvedeEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLE-----ALDEE 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1799 TLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGavkskfKATISALEAKIGQLEEQLEQEAKERAAAN---KLV 1875
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE------DGELAELLQELEELKAELRELAEEWAALKlalELL 502
|
....*....
gi 1907083610 1876 RRTEKKLKE 1884
Cdd:COG4717 503 EEAREEYRE 511
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1422-1960 |
5.34e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1422 EEAKKKLLKDVealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARyaEE 1501
Cdd:PRK03918 144 DESREKVVRQI----LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE--LP 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1502 RDRAEAEAREKETKalslaraleealeakeeferqnkqlraDMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEE 1581
Cdd:PRK03918 218 ELREELEKLEKEVK---------------------------ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1582 LEDELQATEDAKLRLEvNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELEAELED-ERKQRALAVASKKKME 1654
Cdd:PRK03918 271 LKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIekrlsrLEEEINGIEERIKElEEKEERLEELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1655 I--DLKDLEAQIEAANKARdEVIKQLRKLQAQMKDY-----QRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEEL 1727
Cdd:PRK03918 350 LekRLEELEERHELYEEAK-AKKEELERLKKRLTGLtpeklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1728 ASSERARRH--------AEQERDEL-----------ADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLN- 1787
Cdd:PRK03918 429 EELKKAKGKcpvcgrelTEEHRKELleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKEl 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1788 ----------------DRFRKTTLQVDTLNTE---LAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATIS 1848
Cdd:PRK03918 509 eeklkkynleelekkaEEYEKLKEKLIKLKGEiksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1849 ALEAKIGQLEEqLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEatRAN 1928
Cdd:PRK03918 589 ELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE--ELR 665
|
570 580 590
....*....|....*....|....*....|..
gi 1907083610 1929 ASRRKLQRELDDATEANEGLSREVSTLKNRLR 1960
Cdd:PRK03918 666 EEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1724-1962 |
5.57e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.55 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1724 QEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1803
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1804 LAAERSAAQKSDNARQQLERQNK-ELKAKLQELEGAVKSkfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1882
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPlALLLSPEDFLDAVRR-----LQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1883 KEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRRG 1962
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKG 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
839-1622 |
6.91e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 61.22 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 839 KKQQQLSALKVLQRNCAAYLKLRHWQWWRVFTKVKPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLE 918
Cdd:TIGR00606 285 NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIR 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 919 EKNILAEQLQAETEL-------FAEAE------EMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQD 985
Cdd:TIGR00606 365 ARDSLIQSLATRLELdgfergpFSERQiknfhtLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 986 LEEQLDEEEGARQ--KLQLEKVTAEAK-IKKMEEEV------LLLEDQNS----KFIKEKKLMEDRIAECSSQLAEEEEK 1052
Cdd:TIGR00606 445 KKEILEKKQEELKfvIKELQQLEGSSDrILELDQELrkaereLSKAEKNSltetLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1053 A-KNLAKIRNKQEVMISD--------------------------------LEERLKKEEKTRQELEKAKRKLDGETTDLQ 1099
Cdd:TIGR00606 525 EqLNHHTTTRTQMEMLTKdkmdkdeqirkiksrhsdeltsllgyfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASLE 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1100 DQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKN--NALKVARELQAQIA---ELQEDFESEKASRN-------- 1166
Cdd:TIGR00606 605 QNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERlkEEIEKSSKQRAMLAgatAVYSQFITQLTDENqsccpvcq 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1167 ---KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL 1243
Cdd:TIGR00606 685 rvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNK----LQKVNRDI 760
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1244 EqakRFKANLEKNKQGLETDN------KELACEVKVLQQVKAESEHKRKKLDAQVQELHAkvSEGDRLRVELAEKANKLQ 1317
Cdd:TIGR00606 761 Q---RLKNDIEEQETLLGTIMpeeesaKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQ 835
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1318 NELDNVSTLLEEAEKkgikfakdaaglesqlqdtqeLLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQV 1397
Cdd:TIGR00606 836 HELDTVVSKIELNRK---------------------LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1398 LALQSQLADTKKKVDDDLgtieSLEEAKKKLLKDVEAL-SQRLEEKVLAYDKLEKTKNRLQQELDDLTvDLDHQRQIVSN 1476
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDS----PLETFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHGYMK-DIENKIQDGKD 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1477 LEKKQKKfdqllAEEKGISARYAEERDRaeaeaREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGK 1556
Cdd:TIGR00606 970 DYLKQKE-----TELNTVNAQLEECEKH-----QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQ 1039
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1557 NVHELEkskralEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQ---FERDLQTRDEQNEEKK 1622
Cdd:TIGR00606 1040 HLKEMG------QMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQFRDAEEK 1102
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1213-1442 |
7.99e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 7.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1213 ALEDETKNHEAQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQV 1292
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1293 QELHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1372
Cdd:COG4942 93 AELRAEL---EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1373 EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEK 1442
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
891-1421 |
8.63e-09 |
|
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: 61.01 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 891 ELLKVKEKQTKVEGELEEMERKHQQLLEEKnilAEQLQAETELF----AEAEEMRARLAAKKQELEEILHDLESRVEEEE 966
Cdd:pfam12128 309 ELSAADAAVAKDRSELEALEDQHGAFLDAD---IETAAADQEQLpswqSELENLEERLKALTGKHQDVTAKYNRRRSKIK 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 967 ERNQILQNEKKKMQAHIqdleeqldeeegaRQKLQLEKVTAEAKIKKMEEEV-LLLEDQNSKFIKEKKLMEDRIAECSSQ 1045
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKI-------------REARDRQLAVAEDDLQALESELrEQLEAGKLEFNEEEYRLKSRLGELKLR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1046 LAEEEEKAKNLAKIRNKQEV---MISDLEERLKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKK 1119
Cdd:pfam12128 453 LNQATATPELLLQLENFDERierAREEQEAANAEVERLQSELRQARKRRDQASEALRQasrRLEERQSALDELELQLFPQ 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1120 ---------------EEELQGALARG---------------------------DDETLHKNNALKVARELQAQIAELQED 1157
Cdd:pfam12128 533 agtllhflrkeapdwEQSIGKVISPEllhrtdldpevwdgsvggelnlygvklDLKRIDVPEWAASEEELRERLDKAEEA 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1158 FESEKASRNKAEKQKRDLSEELEALKTELEDTLDT-----------TAAQQELRTKREQEVAELKKALEDETKNHEAQIQ 1226
Cdd:pfam12128 613 LQSAREKQAAAEEQLVQANGELEKASREETFARTAlknarldlrrlFDEKQSEKDKKNKALAERKDSANERLNSLEAQLK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1227 DMRQRHATALEELSEQLEQAKRFK------------ANLEKNKQGLETDNKELACEVKVLQQVKAESEHKR-------KK 1287
Cdd:pfam12128 693 QLDKKHQAWLEEQKEQKREARTEKqaywqvvegaldAQLALLKAAIAARRSGAKAELKALETWYKRDLASLgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1288 LDAQVQELHAKVSEGDRLRVELAE-----------KANKLQNELDNVSTLLEEAEKKGIKFAKDA----AGLESQL---Q 1349
Cdd:pfam12128 773 LKREIRTLERKIERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTklrrAKLEMERkasE 852
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1350 DTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKnLEKQVLALQSQLADTKKKVDDDLGTIESL 1421
Cdd:pfam12128 853 KQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADH 923
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
877-1408 |
9.52e-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: 60.51 E-value: 9.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELE 952
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 953 EILHDLESRVEEEEernQILQNEKKKMQAHIQDLEEQLDEEEGARQKL-QLEKVTAEAKIKKMEEEVLLLEDQnsKFIKE 1031
Cdd:pfam05483 349 FVVTEFEATTCSLE---ELLRTEQQRLEKNEDQLKIITMELQKKSSELeEMTKFKNNKEVELEELKKILAEDE--KLLDE 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1032 KKLMEdRIAEcssQLAEEEEKAKNLAKIRNKQevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1111
Cdd:pfam05483 424 KKQFE-KIAE---ELKGKEQELIFLLQAREKE---IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQedfESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEE 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1192 TTAAQQELRTKREQEVAELKKA---LEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELA 1268
Cdd:pfam05483 574 NARSIEYEVLKKEKQMKILENKcnnLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFE 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1269 CEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKAnklQNELDNVSTLLEEAEKKGIKFAKDAaglESQL 1348
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRC---QHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1349 QDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTK 1408
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1579-1961 |
1.15e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1579 LEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDERKQRALAVASKKKME--ID 1656
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEklLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1657 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDY---QRELEEARASRDEIFAQ--------SKESEKKLKSLEAEILQLQE 1725
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELrelEEELEELEAELAELQEEleelleqlSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1726 ELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1805
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1806 A--------ERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKL-VR 1876
Cdd:COG4717 287 AllflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1877 RTEKKLKEIFMQV----EDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATR--ANASRRKLQRELDDATEANEGLSR 1950
Cdd:COG4717 367 ELEQEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEllEALDEEELEEELEELEEELEELEE 446
|
410
....*....|.
gi 1907083610 1951 EVSTLKNRLRR 1961
Cdd:COG4717 447 ELEELREELAE 457
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1616-1820 |
1.60e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1616 EQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEE- 1694
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAq 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1695 --------------ARASRDEIFAQSKESEKKLKSLE----------AEILQLQEELASSERARRHAEQERDELADEIAN 1750
Cdd:COG4942 103 keelaellralyrlGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1751 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQ 1820
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1569-1781 |
2.38e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.30 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1569 EQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVA 1648
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1649 SKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELA 1728
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFS--DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1729 SSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQS 1781
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1140-1343 |
2.46e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1140 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETK 1219
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1220 NHEAQIQDMRQRHATA------------------------LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1275
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalllspedfldavrrLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1276 QVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAG 1343
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1395-1961 |
2.79e-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: 59.47 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1395 KQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEekvlayDKLEKTKNRLQQELDDLTVDLDHQRQIV 1474
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLD------DQWKEKRDELNGELSAADAAVAKDRSEL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1475 SNLEKKQKKFDQLLAEEKgisARYAEERD--RAEAEAREKETKALSlarALEEALEAKEEFERQNKQLRadmedlmsSKD 1552
Cdd:pfam12128 325 EALEDQHGAFLDADIETA---AADQEQLPswQSELENLEERLKALT---GKHQDVTAKYNRRRSKIKEQ--------NNR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1553 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRlevnmqamkaqferdlqtrdEQNEEKKRLllkqvrel 1632
Cdd:pfam12128 391 DIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL--------------------EFNEEEYRL-------- 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1633 EAELEDERKQRALAVASKKKMEidlkDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKK 1712
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLL----QLENFDERIERAREE----QEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1713 LKSLEAEILQLQEELASS-----ERARRHAEQERDELADEIA-------------NSASGKSAL------LDEKR----- 1763
Cdd:pfam12128 515 LEERQSALDELELQLFPQagtllHFLRKEAPDWEQSIGKVISpellhrtdldpevWDGSVGGELnlygvkLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1764 ------RLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1837
Cdd:pfam12128 595 waaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1838 AVKSKFKATISALEAKIGQLEEQLeQEAKERAAANKLVRRTEKklKEIFMQVEDERRhaDQYKEQMEKANARMKQLKRQL 1917
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKH-QAWLEEQKEQKREARTEK--QAYWQVVEGALD--AQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083610 1918 EEAEEEATRANASRrklqrelDDATEANEGLSREVSTLKNRLRR 1961
Cdd:pfam12128 750 KALETWYKRDLASL-------GVDPDVIAKLKREIRTLERKIER 786
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1227-1839 |
2.92e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.14 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1227 DMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLR 1306
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1307 VELAEKANKLQNELDNVstlleeaekkgikfakdaaglesqlqdtqellqeetrqklnlsSRIRQLEEEKNSLqeqQEEE 1386
Cdd:PRK01156 256 SEIKTAESDLSMELEKN-------------------------------------------NYYKELEERHMKI---INDP 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1387 EEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLlkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVD 1466
Cdd:PRK01156 290 VYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKL--------SVLQKDYNDYIKKKSRYDDLNNQILELEGY 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1467 LDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalslaraleealeakeeferqnkqLRADMED 1546
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDA----------------------------IKKELNE 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1547 LMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDE---------LQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ 1617
Cdd:PRK01156 414 INVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1618 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEI-DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQR-ELEEA 1695
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLeDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRtSWLNA 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1696 RASRD--EIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEiANSASGKSALLDEKRRLEARIAQLE 1773
Cdd:PRK01156 574 LAVISliDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE-ANNLNNKYNEIQENKILIEKLRGKI 652
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1774 EELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAV 1839
Cdd:PRK01156 653 DNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
936-1769 |
3.11e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 936 EAEEMRARLAAKKQELEEILHDLESRVeeeeernqilqnekKKMQAHIQDLEEQLDEEEGARQKLQL--EKVTAEAKIKK 1013
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMA--------------RELAELNEAESDLEQDYQAASDHLNLvqTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1014 MEEEVLLLEDQnskfiKEKKLMEdrIAECSSQLAEEEEKAKnlakiRNKQEV-----MISDLEERLKkEEKTR------- 1081
Cdd:PRK04863 353 YQADLEELEER-----LEEQNEV--VEEADEQQEENEARAE-----AAEEEVdelksQLADYQQALD-VQQTRaiqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1082 -QELEKAKRKL---DGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETlhknNALKVARELQAQIaELQED 1157
Cdd:PRK04863 420 vQALERAKQLCglpDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEV-SRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1158 FESEKASRNKAEKQkRDLSEELEALKTELEDtldttaAQQELRTKREQE--VAELKKALEdETKNHEAQIQDMRQRHATA 1235
Cdd:PRK04863 495 WDVARELLRRLREQ-RHLAEQLQQLRMRLSE------LEQRLRQQQRAErlLAEFCKRLG-KNLDDEDELEQLQEELEAR 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1236 LEELSEQLEQAkrfkanleknkqgletdnkelacevkvlQQVKAESEHKRKKLDAQVQELHAKVSEGdrlrVELAEKANK 1315
Cdd:PRK04863 567 LESLSESVSEA----------------------------RERRMALRQQLEQLQARIQRLAARAPAW----LAAQDALAR 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1316 LQneldnvstlleeaEKKGIKFAkDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEK 1395
Cdd:PRK04863 615 LR-------------EQSGEEFE-DSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1396 QVLA-LQSQLADtkkkvD---DDLGTIES-------------LEEAKKKLLKD---------VEALSQRLEEKVLAYDKL 1449
Cdd:PRK04863 681 RFGGvLLSEIYD-----DvslEDAPYFSAlygparhaivvpdLSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEEL 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1450 EKT--------------------------KNR---LQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAE 1500
Cdd:PRK04863 756 EKAvvvkiadrqwrysrfpevplfgraarEKRieqLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADP 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1501 ERDRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDvgknvhelekskRALEQQVEEMRTQL 1579
Cdd:PRK04863 836 EAELRQLNRRRVElERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD------------ETLADRVEEIREQL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1580 EELEDE---LQATEDAKLRLE---VNMQAMKAQFERdLQTRDEQNEEKKRLLLKQVRELeaeleDERKQRALAVASKKKM 1653
Cdd:PRK04863 904 DEAEEAkrfVQQHGNALAQLEpivSVLQSDPEQFEQ-LKQDYQQAQQTQRDAKQQAFAL-----TEVVQRRAHFSYEDAA 977
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1654 EIDLKD------LEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEaeiLQLQEEL 1727
Cdd:PRK04863 978 EMLAKNsdlnekLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG---VPADSGA 1054
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 1907083610 1728 AssERARRHaeqeRDELADEIANSASGKSALLDEKRRLEARI 1769
Cdd:PRK04863 1055 E--ERARAR----RDELHARLSANRSRRNQLEKQLTFCEAEM 1090
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1473-1943 |
3.59e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1473 IVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLmsskd 1552
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1553 DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE-VNMQAMKAQFERDLQTRDEQNEEKKRL--LLKQV 1629
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEeLEAELAELQEELEELLEQLSLATEEELqdLAEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1630 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKArdEVIKQLRKLQAQM-------------KDYQRELEEAR 1696
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAaallallglggslLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1697 ASRDEIFAQSKESEKKLKsleAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEEL 1776
Cdd:COG4717 280 FLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1777 EEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSdNARQQLERQNKELKAKLQELEGAVKSKFKA-TISALEAKIG 1855
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEAlDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1856 QLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQ 1935
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERLP 515
|
....*...
gi 1907083610 1936 RELDDATE 1943
Cdd:COG4717 516 PVLERASE 523
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1551-1771 |
4.49e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1551 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQAtedakLRLEVNMQAMKAQfERDLQTRDEQNEEKKRLLLKQVR 1630
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEE-AKLLLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1631 ELEAELEDERKQRALAVASKKKMEID--LKDLEAQIEAANKARDEVIK-------QLRKLQAQMKDYQREL-EEARASRD 1700
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLqQEAQRILA 316
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1701 EIFAQSKESEKKLKSLEAEILQLQEELAS-SERARRHAEQERD-ELADEIANSasgksaLLdeKRRLEARIAQ 1771
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAElPELEAELRRLEREvEVARELYES------LL--QRLEEARLAE 381
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
883-1873 |
5.31e-08 |
|
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: 58.52 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 883 EELQAK-DEELLKVKEKQTK-VEGELEEMERKHQQLLEekNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLES 960
Cdd:TIGR01612 699 DDLKSKiDKEYDKIQNMETAtVELHLSNIENKKNELLD--IIVEIKKHIHGEINKDLNKILEDFKNKEKELSNKINDYAK 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 961 RveeeeernqilQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIA 1040
Cdd:TIGR01612 777 E-----------KDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1041 ECSSQLAEEEEKAK--------NLAKIRNKQEVMISD----------------LEERLKKEEKTRQELEKAKrKLDG--- 1093
Cdd:TIGR01612 846 NKVDKFINFENNCKekidseheQFAELTNKIKAEISDdklndyekkfndskslINEINKSIEEEYQNINTLK-KVDEyik 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1094 --ETTdlQDQIAELQAQVDELKVQLTKKEEELQgalargDDETLHKNNALKVARELQAQIAELQEDFEseKASRNKAEKQ 1171
Cdd:TIGR01612 925 icENT--KESIEKFHNKQNILKEILNKNIDTIK------ESNLIEKSYKDKFDNTLIDKINELDKAFK--DASLNDYEAK 994
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1172 KRDLSEELEALKTELEDTLDTTAAQQelRTKREQEVAELKKALEDETKNheaqIQDMRQRHATALEELSEQLEqaKRFKA 1251
Cdd:TIGR01612 995 NNELIKYFNDLKANLGKNKENMLYHQ--FDEKEKATNDIEQKIEDANKN----IPNIEIAIHTSIYNIIDEIE--KEIGK 1066
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1252 NLEK-NKQGLETDNKELACEVKVLQQVK------------AESEHKRKKLDAQVQELHAKVsegDRLRVELAEKANKLQN 1318
Cdd:TIGR01612 1067 NIELlNKEILEEAEINITNFNEIKEKLKhynfddfgkeenIKYADEINKIKDDIKNLDQKI---DHHIKALEEIKKKSEN 1143
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1319 ELDNVSTLLEEAEKKGIK--FAKDAAGLESQLQ------DTQELLQEETRQKLNlssRIRQLEEEKNSLQEQQEEEEEAR 1390
Cdd:TIGR01612 1144 YIDEIKAQINDLEDVADKaiSNDDPEEIEKKIEnivtkiDKKKNIYDEIKKLLN---EIAEIEKDKTSLEEVKGINLSYG 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1391 KNLEKQVLalqSQLADTKKKVDDdlgTIESLEeAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDD----LTVD 1466
Cdd:TIGR01612 1221 KNLGKLFL---EKIDEEKKKSEH---MIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDdkdhHIIS 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1467 LDHQRQIvSNLEKKQKKFDQLLAEEKGIS------ARYAEERDRAEAEAREKETKALSLARALEEALEakeeferqnKQL 1540
Cdd:TIGR01612 1294 KKHDENI-SDIREKSLKIIEDFSEESDINdikkelQKNLLDAQKHNSDINLYLNEIANIYNILKLNKI---------KKI 1363
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1541 RADMEDLMSSKDDVGKNVH-ELEKSKRALEQQVEEmrTQLEELEDELQATEDAKLRLEV--NMQAMKAQF---ERDLQT- 1613
Cdd:TIGR01612 1364 IDEVKEYTKEIEENNKNIKdELDKSEKLIKKIKDD--INLEECKSKIESTLDDKDIDECikKIKELKNHIlseESNIDTy 1441
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1614 --RDEQNEEKKRLLLKQVreleaELEDERKQRALAVA---SKKKMEIDLKDLEAQIEAANKARDEV---IKQLRKLQAQM 1685
Cdd:TIGR01612 1442 fkNADENNENVLLLFKNI-----EMADNKSQHILKIKkdnATNDHDFNINELKEHIDKSKGCKDEAdknAKAIEKNKELF 1516
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1686 KDYQRE---------------------------LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE 1738
Cdd:TIGR01612 1517 EQYKKDvtellnkysalaiknkfaktkkdseiiIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAI 1596
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1739 QERDELAD------EIANSASGKSALLDEKRRLEARIaqleeeleeeqsnmellndrfrkTTLQVDTLNTELAAERSAAQ 1812
Cdd:TIGR01612 1597 DIQLSLENfenkflKISDIKKKINDCLKETESIEKKI-----------------------SSFSIDSQDTELKENGDNLN 1653
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1813 KSDNARQQLERQNKELKAKLQELEGaVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1873
Cdd:TIGR01612 1654 SLQEFLESLKDQKKNIEDKKKELDE-LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANK 1713
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
876-1248 |
5.31e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 876 LQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQEL---- 951
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLslat 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 952 EEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE 1031
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1032 KK---------------LMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETT 1096
Cdd:COG4717 271 LIltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1097 DLQDQIAELQAQVdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQkrdls 1176
Cdd:COG4717 351 ELLREAEELEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEA----- 424
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1177 EELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEaqIQDMRQRHATALEELSEQLEQAKR 1248
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAA 494
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1103-1403 |
5.50e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 58.38 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1103 AELQAQVDELKVQltKKEEELQGALARGDDETLhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEAL 1182
Cdd:PRK11281 39 ADVQAQLDALNKQ--KLLEAEDKLVQQDLEQTL----------ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1183 KTELEDTLDTTAAQQELR------TKREQEVAELKKALeDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKN 1256
Cdd:PRK11281 107 KDDNDEETRETLSTLSLRqlesrlAQTLDQLQNAQNDL-AEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1257 KQGLETDNK-ELACEvkvLQQVKAESEHKRKKLDA--QVQELhakvseGDRLRVELAEKANKLQNELdnvsTLLEEA--E 1331
Cdd:PRK11281 186 GKALRPSQRvLLQAE---QALLNAQNDLQRKSLEGntQLQDL------LQKQRDYLTARIQRLEHQL----QLLQEAinS 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1332 KKGIKFAKDAAGLESQlQDTQE-----LLQEETRQKLNLSSRIRQLEEEKNSLQeqqeeeeeaRKNLE-KQVL--ALQSQ 1403
Cdd:PRK11281 253 KRLTLSEKTVQEAQSQ-DEAARiqanpLVAQELEINLQLSQRLLKATEKLNTLT---------QQNLRvKNWLdrLTQSE 322
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1496-1868 |
5.59e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 57.60 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1496 ARYAEERDRaEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEM 1575
Cdd:pfam07888 49 AQEAANRQR-EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1576 RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLllkQVRELEAELEDERKQRALAVASKKkmei 1655
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQL---QAKLQQTEEELRSLSKEFQELRNS---- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1656 dlkdLEAQIEAANKARDEVIKQLRKL-QAQMKDYQRE--LEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSER 1732
Cdd:pfam07888 201 ----LAQRDTQVLQLQDTITTLTQKLtTAHRKEAENEalLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1733 ARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERsaaq 1812
Cdd:pfam07888 277 ARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREK---- 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1813 ksDNARQQL---ERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKER 1868
Cdd:pfam07888 353 --DCNRVQLsesRRELQELKASLRVAQKE-KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
901-1364 |
6.46e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 901 KVEGELEEMERKHQQLLEeknILAEQLQAETELFAEAEEMRARLAAKKQELEEilhdLESRVEEEEERNQILQNEKKKMQ 980
Cdd:COG4717 50 RLEKEADELFKPQGRKPE---LNLKELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 981 AHIqdleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQnskfIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR 1060
Cdd:COG4717 123 KLL------------QLLPLYQELEALEAELAELPERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1061 NKQEvmisdlEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE------------------ 1122
Cdd:COG4717 187 SLAT------EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaalla 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1123 LQGALARGDDETLHKNNAL---------------KVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE 1187
Cdd:COG4717 261 LLGLGGSLLSLILTIAGVLflvlgllallflllaREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1188 DTLDTTAAQQELRTKREQEVAELKKAledetKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQ-----GLET 1262
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQLE-----ELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEEleeqlEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1263 DNKELACEVKVLQQVKAESEHKRKKLDA---QVQELHAKVSEgDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAK 1339
Cdd:COG4717 416 GELEELLEALDEEELEEELEELEEELEEleeELEELREELAE-LEAELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|....*
gi 1907083610 1340 DAAGLESqLQDTQELLQEETRQKLN 1364
Cdd:COG4717 495 LKLALEL-LEEAREEYREERLPPVL 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1652 |
7.18e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1389 ARKNLEKQVLALQSQLADTKKKvdddlgtIESLEEAKKKLLKDVEALSQRLEEkvlaydkLEKTKNRLQQELDDLTvdld 1468
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAA-------LARRIRALEQELAALE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1469 hqrqivSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLM 1548
Cdd:COG4942 83 ------AELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1549 SSKDdvgknvhELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRlLLKQ 1628
Cdd:COG4942 157 ADLA-------ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-LEAL 228
|
250 260
....*....|....*....|....
gi 1907083610 1629 VRELEAELEDERKQRALAVASKKK 1652
Cdd:COG4942 229 IARLEAEAAAAAERTPAAGFAALK 252
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1287-1841 |
8.06e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.60 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1287 KLDAQVQELHAKVSEGDRLRVELAEKanklQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQ---DTQELLQEETRQKL 1363
Cdd:PRK01156 170 KLKDVIDMLRAEISNIDYLEEKLKSS----NLELENIKKQIADDEKSHSITLKEIERLSIEYNnamDDYNNLKSALNELS 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1364 NLSSRIRQLEEE---KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLE 1440
Cdd:PRK01156 246 SLEDMKNRYESEiktAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1441 E--KVLA--------YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAR 1510
Cdd:PRK01156 326 AiiKKLSvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPD 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1511 EketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHEL---------------EKSKRALEQQVEE- 1574
Cdd:PRK01156 406 A-------IKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsvcpvcgttlgeEKSNHIINHYNEKk 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1575 --MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKkRLLLKQVRELEAELEDERKQRALAVASKKK 1652
Cdd:PRK01156 479 srLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA-RADLEDIKIKINELKDKHDKYEEIKNRYKS 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1653 MeiDLKDLEAQ---------------IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFaqsKESEKKLKSLE 1717
Cdd:PRK01156 558 L--KLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSI---REIENEANNLN 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1718 AEILQLQEELASSERARRHAEQERDELAdeiansasGKSALLDEKRRLEARIAQleeeleeeqsnmelLNDRFRKTTLQV 1797
Cdd:PRK01156 633 NKYNEIQENKILIEKLRGKIDNYKKQIA--------EIDSIIPDLKEITSRIND--------------IEDNLKKSRKAL 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083610 1798 DTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKS 1841
Cdd:PRK01156 691 DDAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKA 734
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
905-1129 |
8.71e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 56.70 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 905 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIq 984
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 985 dleeqldeeegARQKLQLEKVTAEA-KIKKMEEEVLLLEDQN-SKFIKEKKLME-------DRIAECSSQLAEEEEKAKN 1055
Cdd:COG4942 100 -----------EAQKEELAELLRALyRLGRQPPLALLLSPEDfLDAVRRLQYLKylaparrEQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1056 LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1129
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1308-1939 |
1.53e-07 |
|
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: 56.65 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1308 ELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEE--TRQKLNLSSRIRQLEEEKNSLQEQQEE 1385
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENnaTRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1386 EEEA-----RKNLEKQVLALQSQLADTKK-------KVDDDLGTIESLEEAKKKLLKDVEAlsqrlEEKVLAYDKLEKtk 1453
Cdd:pfam05483 180 ETRQvymdlNNNIEKMILAFEELRVQAENarlemhfKLKEDHEKIQHLEEEYKKEINDKEK-----QVSLLLIQITEK-- 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1454 nrlQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKgisaryaeerDRAEAEAREKETKALSLARALEEALEAKEEF 1533
Cdd:pfam05483 253 ---ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELI----------EKKDHLTKELEDIKMSLQRSMSTQKALEEDL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1534 ERQNKQL-------RADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ--ATEDAKLRLEVN-MQAM 1603
Cdd:pfam05483 320 QIATKTIcqlteekEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiiTMELQKKSSELEeMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1604 KAQFERDLQTRDEQNEEKKRLLL--KQVRELEAELEDERKQRALAVASKKKmeiDLKDLEAQIEAANKARDEVIKQLRKL 1681
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKGKEQELIFLLQAREK---EIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1682 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERarrhaeqERDELADEIANSASGKSALLDE 1761
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK-------QEERMLKQIENLEEKEMNLRDE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1762 krrLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELaaeRSAAQKSDNARQQLERQNKELKaKLQELEGAVKS 1841
Cdd:pfam05483 550 ---LESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM---KILENKCNNLKKQIENKNKNIE-ELHQENKALKK 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1842 KFKA---TISALEAKIGQLEEQLEqeakerAAANKLVRRTEKKLKEIfmqvEDERRHADQYKEQMEKANARMKQLKrqle 1918
Cdd:pfam05483 623 KGSAenkQLNAYEIKVNKLELELA------SAKQKFEEIIDNYQKEI----EDKKISEEKLLEEVEKAKAIADEAV---- 688
|
650 660
....*....|....*....|.
gi 1907083610 1919 eaeeeatranasrrKLQRELD 1939
Cdd:pfam05483 689 --------------KLQKEID 695
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1308-1955 |
1.55e-07 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 56.77 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1308 ELAEKANKLQNELDNVSTLleEAEKKGIKFA-KDAAGLESQLQDTQELLQEETRQKLnlSSRIRQLEEEKNSLQEQQEEE 1386
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESA--ELRLSHLHFGyKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAA 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1387 EEARKNLEKQVLALQSQLadtKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQElddltVD 1466
Cdd:pfam12128 314 DAAVAKDRSELEALEDQH---GAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSK-----IK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1467 LDHQRQIVSNLEKKQKKFD----QLLAEEKGISARYAEERDRAEA---EAREKETKALSLARALEEALEAKEEFERQNKQ 1539
Cdd:pfam12128 386 EQNNRDIAGIKDKLAKIREardrQLAVAEDDLQALESELREQLEAgklEFNEEEYRLKSRLGELKLRLNQATATPELLLQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1540 LRADMEDLMSSKDDVGKNVHELEKSKRAL-----------------EQQVEEMRTQLEELEDELQA----------TEDA 1592
Cdd:pfam12128 466 LENFDERIERAREEQEAANAEVERLQSELrqarkrrdqasealrqaSRRLEERQSALDELELQLFPqagtllhflrKEAP 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1593 KLRLEVNMQAMKAQFER--------DLQTRDEQNEEKKRLLLKQVRELE-AELEDERKQRAlavaskKKMEIDLKDLEAQ 1663
Cdd:pfam12128 546 DWEQSIGKVISPELLHRtdldpevwDGSVGGELNLYGVKLDLKRIDVPEwAASEEELRERL------DKAEEALQSAREK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1664 IEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQsKESEKklksleaeiLQLQEELassERARRHAEQERDE 1743
Cdd:pfam12128 620 QAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDE-KQSEK---------DKKNKAL---AERKDSANERLNS 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1744 LADEIANSASGKSALLDEKRR--LEARIAQLeeeleeeQSNMELLNDRfrktTLQVDTLNTELAAERSAAqksDNARQQL 1821
Cdd:pfam12128 687 LEAQLKQLDKKHQAWLEEQKEqkREARTEKQ-------AYWQVVEGAL----DAQLALLKAAIAARRSGA---KAELKAL 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1822 ERQNK-ELKAKLQELEgavkskfkaTISALEAKIGQLEEQLEQEAKERAAanklVRRTEKKLKEIFMQvederrHADQYK 1900
Cdd:pfam12128 753 ETWYKrDLASLGVDPD---------VIAKLKREIRTLERKIERIAVRRQE----VLRYFDWYQETWLQ------RRPRLA 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1901 EQMEKANARMK----QLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTL 1955
Cdd:pfam12128 814 TQLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKL 872
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1429-1961 |
1.58e-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: 56.98 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1429 LKDVEALSQRLEE------KVLAYDKLEKTKNRLQQELDDLTVDLDHQRQivsNLEKKQKKFDQLLAEE------KGISA 1496
Cdd:TIGR00606 165 LSEGKALKQKFDEifsatrYIKALETLRQVRQTQGQKVQEHQMELKYLKQ---YKEKACEIRDQITSKEaqlessREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1497 RYAEERDRAEAEAREKE---TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSK-RALEQQV 1572
Cdd:TIGR00606 242 SYENELDPLKNRLKEIEhnlSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTvREKEREL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1573 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFER-------------DLQTRDEQNEEKKRLLLKQVRELEAELEDE 1639
Cdd:TIGR00606 322 VDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRhqehirardsliqSLATRLELDGFERGPFSERQIKNFHTLVIE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1640 RKQRALAVASKKKMEIDLKDLEAQiEAANKARDEVI----------KQLRKLQAQMKDYQRELEEARASRDEIFAQSKES 1709
Cdd:TIGR00606 402 RQEDEAKTAAQLCADLQSKERLKQ-EQADEIRDEKKglgrtielkkEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1710 EKKLKSL------------EAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEK-RRLEARIAQ 1771
Cdd:TIGR00606 481 RKAERELskaeknsltetlKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTrtqmeMLTKDKMDKDEQiRKIKSRHSD 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1772 LEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVkskFKATIS-AL 1850
Cdd:TIGR00606 561 ELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL---FDVCGSqDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1851 EAKIGQLEEQLEQEAKERA---AANKL---------------------VRRTEKKLKEIFMQVEDERRHADQYKEQMEKA 1906
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQRAmlaGATAVysqfitqltdenqsccpvcqrVFQTEAELQEFISDLQSKLRLAPDKLKSTESE 717
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1907 NARMKqlKRQLEEAEEEATRANASRRKlQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:TIGR00606 718 LKKKE--KRRDEMLGLAPGRQSIIDLK-EKEIPELRNKLQKVNRDIQRLKNDIEE 769
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1160-1399 |
1.75e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1160 SEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALedetKNHEAQIQDMRQRHATALEEL 1239
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI----RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1240 SEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNE 1319
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1320 LDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLA 1399
Cdd:COG4942 173 RAELEALLAELEEE-------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1559-1955 |
2.02e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.50 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1559 HELEKSKRAL---EQQVEEMRTQLEE-------LEDELQATEDaklRLEVNMQAMKAQfERDLQTRDEQNEEKKRLllkq 1628
Cdd:COG3096 292 RELFGARRQLaeeQYRLVEMARELEElsaresdLEQDYQAASD---HLNLVQTALRQQ-EKIERYQEDLEELTERL---- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1629 vRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEviKQLRKLQAQMKdyQRELEEARA-------SRDE 1701
Cdd:COG3096 364 -EEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV--QQTRAIQYQQA--VQALEKARAlcglpdlTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1702 IFAQSKESEKKLKSLEAEILQLQEELASSERARR---HAEQERDELADEIANSASGKSA--LLDEKRRLEARIAQleeel 1776
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfeKAYELVCKIAGEVERSQAWQTAreLLRRYRSQQALAQR----- 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1777 eeeqsnmellndrfrkttlqVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQ 1856
Cdd:COG3096 514 --------------------LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE------------ELEELLAE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1857 LEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHA--------------DQYKEQMEKANARMKQLKRQLEEAee 1922
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqdalerlrEQSGEALADSQEVTAAMQQLLERE-- 639
|
410 420 430
....*....|....*....|....*....|...
gi 1907083610 1923 eatranasrRKLQRELDDATEANEGLSREVSTL 1955
Cdd:COG3096 640 ---------REATVERDELAARKQALESQIERL 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1352-1595 |
2.58e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1352 QELLQEETRQKLN-LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLK 1430
Cdd:COG4942 18 QADAAAEAEAELEqLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1431 DVEALSQRLEEKVLAYDKLEKTKNRL----QQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1506
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1507 AEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlmsskddvgknvhELEKSKRALEQQVEEMRTQLEELEDEL 1586
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELA--------------ELQQEAEELEALIARLEAEAAAAAERT 243
|
....*....
gi 1907083610 1587 QATEDAKLR 1595
Cdd:COG4942 244 PAAGFAALK 252
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1754 |
3.13e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1538 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDaklRLEVNMQAMKAQFeRDLQTRDEQ 1617
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERA-RALYRSGGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1618 NEEKKRLL--------LKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ 1689
Cdd:COG3883 102 VSYLDVLLgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1690 RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASG 1754
Cdd:COG3883 182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1071-1342 |
5.38e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 5.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1071 EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQ 1150
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---------------------KLQAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1151 IAELQEDFESEKA---SRNKAEKQKRDLSEELEALK--TELEDTLDTTAAqqelrtkreqevaelkkaledetknheaqI 1225
Cdd:COG3883 74 IAEAEAEIEERREelgERARALYRSGGSVSYLDVLLgsESFSDFLDRLSA-----------------------------L 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1226 QDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRL 1305
Cdd:COG3883 125 SKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907083610 1306 RVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAA 1342
Cdd:COG3883 205 LAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1323-1896 |
5.81e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 5.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1323 VSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNslqeqqEEEEEARKNLEKQVLALQS 1402
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREA------EAEEALREQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1403 QLADTKKKVDDDLgTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQK 1482
Cdd:pfam05557 85 LEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1483 kfdqllaeekgisaryaeerDRAEAEAREKETKalslARALEEALEAKEEFERQNKQLR-ADMEDLMSSKDDVGKNVHEL 1561
Cdd:pfam05557 164 --------------------SLAEAEQRIKELE----FEIQSQEQDSEIVKNSKSELARiPELEKELERLREHNKHLNEN 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1562 EKSKRALEQQVEEMRTQLEELE---DELQATEDAKLRLEVNMQAMKAQFE---------RDLQTRDEQNEEKKRLLLKQV 1629
Cdd:pfam05557 220 IENKLLLKEEVEDLKRKLEREEkyrEEAATLELEKEKLEQELQSWVKLAQdtglnlrspEDLSRRIEQLQQREIVLKEEN 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1630 RELEAELEDERKQRalavaskKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARA---SRDEIFAQS 1706
Cdd:pfam05557 300 SSLTSSARQLEKAR-------RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAileSYDKELTMS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1707 KESEKKLKSLE--AEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNME 1784
Cdd:pfam05557 373 NYSPQLLERIEeaEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1785 LL--NDRFR--KTTLQVDTLNTELAAERSAA-----QKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIG 1855
Cdd:pfam05557 453 LEleRQRLReqKNELEMELERRCLQGDYDPKktkvlHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLR 532
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083610 1856 QLEEQLEQEAKERAAANKLVRRTEKK---LKEIFMQVEDERRHA 1896
Cdd:pfam05557 533 LPETTSTMNFKEVLDLRKELESAELKnqrLKEVFQAKIQEFRDV 576
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
881-1104 |
6.24e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 881 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAET----ELFAEAEEMRARLAAKKQELEEILH 956
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 957 DLESRVEEEEERNQILQnekKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEevllLEDQNSKFIKEKKLME 1036
Cdd:COG4942 98 ELEAQKEELAELLRALY---RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1037 DRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAE 1104
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1081-1944 |
7.19e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1081 RQELEKAKRKLDGEttdlQDQIAELQAQVDELKVQLTKKEEELQGALARgddetLHK-NNAL----KVAR------ELQA 1149
Cdd:PRK04863 292 RRELYTSRRQLAAE----QYRLVEMARELAELNEAESDLEQDYQAASDH-----LNLvQTALrqqeKIERyqadleELEE 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1150 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALE---------DETKN 1220
Cdd:PRK04863 363 RLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQlcglpdltaDNAED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1221 HEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEH-KRKKLDAQVQELHAKV 1299
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLrEQRHLAEQLQQLRMRL 522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1300 SEGDRlRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1379
Cdd:PRK04863 523 SELEQ-RLRQQQRAERLLAEFCKRLGKNLDDED-------ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQAR 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1380 qeqqeeeeeaRKNLEKQV---LALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQrleekvlAYDKLEKTKNRL 1456
Cdd:PRK04863 595 ----------IQRLAARApawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTV-------ERDELAARKQAL 657
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1457 QQELDDL----TVDLDHQRQI--------VSNLekkqkkFDQLLAEEKG-ISARYAEER------DraeaeareketkaL 1517
Cdd:PRK04863 658 DEEIERLsqpgGSEDPRLNALaerfggvlLSEI------YDDVSLEDAPyFSALYGPARhaivvpD-------------L 718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1518 SLARaleealeakeefeRQNKQLRADMEDLM------SSKDDVGKNVHELEKS----------------------KRALE 1569
Cdd:PRK04863 719 SDAA-------------EQLAGLEDCPEDLYliegdpDSFDDSVFSVEELEKAvvvkiadrqwrysrfpevplfgRAARE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1570 QQVEEMRTQLEELEDELqatedAKLRLEVN-MQAMKAQFERDLQTR-----DEQNEEKKRLLLKQVRELEAELED----E 1639
Cdd:PRK04863 786 KRIEQLRAEREELAERY-----ATLSFDVQkLQRLHQAFSRFIGSHlavafEADPEAELRQLNRRRVELERALADhesqE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1640 RKQRALAVASKKKMEiDLKDLEAQIEAAnkARDEVIKQLRKLQAQMKdyqrELEEARASRDE---IFAQSKESEKKLKSL 1716
Cdd:PRK04863 861 QQQRSQLEQAKEGLS-ALNRLLPRLNLL--ADETLADRVEEIREQLD----EAEEAKRFVQQhgnALAQLEPIVSVLQSD 933
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1717 EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSAllDEKRRLEAriaqleeeleeEQSNMELLNDRFRKTTLQ 1796
Cdd:PRK04863 934 PEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYE--DAAEMLAK-----------NSDLNEKLRQRLEQAEQE 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1797 VDTLNTELaaeRSAAQKSDNARQQLERQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKlvr 1876
Cdd:PRK04863 1001 RTRAREQL---RQAQAQLAQYNQVLASLKSSYDAKRQMLQ------------ELKQELQDLGVPADSGAEERARARR--- 1062
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1877 rtekklKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLeeaeeeatranasrRKLQRELDDATEA 1944
Cdd:PRK04863 1063 ------DELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKL--------------RKLERDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1063-1520 |
9.45e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1063 QEVMISDLEERLKKEektRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQlTKKEEELQGALARGDDETLHKNNALK 1142
Cdd:COG4717 40 LAFIRAMLLERLEKE---ADELFKPQGRKP---ELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1143 VARELQAQIAELQEDFESEKAsRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1222
Cdd:COG4717 113 ELREELEKLEKLLQLLPLYQE-LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1223 AQIQDMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1302
Cdd:COG4717 192 EELQDLAEE----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1303 DRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLS-----SRIRQLEEEKN 1377
Cdd:COG4717 268 LLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPpdlspEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1378 SLQEQQEEEEEARKNLEKQVL--ALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEK--TK 1453
Cdd:COG4717 348 ELQELLREAEELEEELQLEELeqEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDE 427
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1454 NRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLL--AEEKGISARYAEERDRAEAEAREKETKALSLA 1520
Cdd:COG4717 428 EELEEELEELEEELEELEEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
882-1294 |
1.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 882 EEELQAKDEELLKVKEKQTKVEGELEEMER--KHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE 959
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 960 SrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDR- 1038
Cdd:COG4717 174 E---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARl 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1039 -------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQElEKAKRKLDGETTDLQDQiaELQAQVDE 1111
Cdd:COG4717 251 llliaaaLLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK-EAEELQALPALEELEEE--ELEELLAA 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKVQLTKKEEELQGALARGDDetlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLD 1191
Cdd:COG4717 328 LGLPPDLSPEELLELLDRIEE-----------LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1192 TTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKelacev 1271
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE------ 470
|
410 420
....*....|....*....|...
gi 1907083610 1272 kvLQQVKAESEHKRKKLDAQVQE 1294
Cdd:COG4717 471 --LAELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1091-1333 |
1.47e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1091 LDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALArgddetlhKNNALKVARELQ---AQIAELQEDFESEKASRNK 1167
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQ--------KNGLVDLSEEAKlllQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1168 AEKQKRDLSEELEALKTELEDTLDTTAAQQeLRTKREQEVAELKKALEDETKNHEaQIQDMRQRhataLEELSEQLEQ-A 1246
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQSPVIQQ-LRAQLAELEAELAELSARYTPNHP-DVIALRAQ----IAALRAQLQQeA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1247 KRFKANLEKNKQGLETdnkelacevkvlqqvkaesehKRKKLDAQVQELHAKVSEGDRLRVELAEkankLQNELDNVSTL 1326
Cdd:COG3206 312 QRILASLEAELEALQA---------------------REASLQAQLAQLEARLAELPELEAELRR----LEREVEVAREL 366
|
....*..
gi 1907083610 1327 LEEAEKK 1333
Cdd:COG3206 367 YESLLQR 373
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1078-1355 |
1.63e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.23 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1078 EKTRQeLEKAKRKLDGETTDLQDQ---------------IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALK 1142
Cdd:pfam00038 18 DKVRF-LEQQNKLLETKISELRQKkgaepsrlyslyekeIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1143 VARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTEledtldttaaqqelrtkREQEVAELKKALEDETKNHE 1222
Cdd:pfam00038 97 LRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN-----------------HEEEVRELQAQVSDTQVNVE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1223 ---AQIQDMrqrhATALEELSEQLE-QAKRFKANLEKN-KQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1297
Cdd:pfam00038 160 mdaARKLDL----TSALAEIRAQYEeIAAKNREEAEEWyQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1298 KVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgiKFAKDAAGLESQLQDTQELL 1355
Cdd:pfam00038 236 LKKQKASLERQLAETEERYELQLADYQELISELEA---ELQETRQEMARQLREYQELL 290
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1560-1838 |
1.84e-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: 53.20 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEM--RTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRdeQNEEKKRLL-----------L 1626
Cdd:pfam17380 297 EQERLRQEKEEKAREVerRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERI--RQEERKRELerirqeeiameI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1627 KQVRELE--------------AELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1692
Cdd:pfam17380 375 SRMRELErlqmerqqknervrQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1693 EEARASRDEIFAQsKESEKKLKSLEAEILQLQEELASSERaRRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1772
Cdd:pfam17380 455 EQERQQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQR-RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE 532
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1773 EEELEEEQSNMELLNDRFRKTTLQVDTLNTElaaERSAAQKSDNARQQLeRQNKELKAKLQELEGA 1838
Cdd:pfam17380 533 ERRREAEEERRKQQEMEERRRIQEQMRKATE---ERSRLEAMEREREMM-RQIVESEKARAEYEAT 594
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1631-1877 |
1.92e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 53.38 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1631 ELEAELeDERKQRALAVASKKKMEIDLK---DLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1707
Cdd:PRK11281 40 DVQAQL-DALNKQKLLEAEDKLVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1708 ES------EKKLKSLEAEILQLQEELAS-----------SERARR---HAEQERDELADEIANSASGKSALLDEKR-RLE 1766
Cdd:PRK11281 119 STlslrqlESRLAQTLDQLQNAQNDLAEynsqlvslqtqPERAQAalyANSQRLQQIRNLLKGGKVGGKALRPSQRvLLQ 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1767 ARIAQleeeleeeqsnMELLNDrFRKTTLQVDTLNTELAAER----SAAQksdnarQQLERQnkelkakLQELEGAVKSK 1842
Cdd:PRK11281 199 AEQAL-----------LNAQND-LQRKSLEGNTQLQDLLQKQrdylTARI------QRLEHQ-------LQLLQEAINSK 253
|
250 260 270
....*....|....*....|....*....|....*
gi 1907083610 1843 fkatisALEAKIGQLEEQLEQEAKERAAANKLVRR 1877
Cdd:PRK11281 254 ------RLTLSEKTVQEAQSQDEAARIQANPLVAQ 282
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1550-1947 |
2.48e-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: 52.92 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1550 SKDDVGKNVHElekskRALEQQVEEMRTQLEELEDELQATEDAKLRL---EVNMQAMKAQFERDLQTRDEQNEEKK---R 1623
Cdd:pfam12128 219 NRQQVEHWIRD-----IQAIAGIMKIRPEFTKLQQEFNTLESAELRLshlHFGYKSDETLIASRQEERQETSAELNqllR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1624 LLLKQVRELEAELEDERKQRALAVAsKKKMEIDLkdLEAQIEAANKARDEVIK----QLRKLQAQMKDYQRELEEARASR 1699
Cdd:pfam12128 294 TLDDQWKEKRDELNGELSAADAAVA-KDRSELEA--LEDQHGAFLDADIETAAadqeQLPSWQSELENLEERLKALTGKH 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1700 DEIFAQSKESEKKLKS-LEAEILQLQEELASS--ERARRHAEQE----------RDELADEIANSASG----KSALLDEK 1762
Cdd:pfam12128 371 QDVTAKYNRRRSKIKEqNNRDIAGIKDKLAKIreARDRQLAVAEddlqaleselREQLEAGKLEFNEEeyrlKSRLGELK 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1763 RRLEARIAQLEEELEEEQSNMEL--LNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEgavk 1840
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDERIerAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELE---- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1841 skfkatiSALEAKIGQLEEQLEQEAKE------RAAANKLVRRTEK--------------------KLKEI----FMQVE 1890
Cdd:pfam12128 527 -------LQLFPQAGTLLHFLRKEAPDweqsigKVISPELLHRTDLdpevwdgsvggelnlygvklDLKRIdvpeWAASE 599
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1891 DE-RRHADQYKEQMEKANARMKQLKRQLEEaeeeatrANASRRKLQRELDDATEANEG 1947
Cdd:pfam12128 600 EElRERLDKAEEALQSAREKQAAAEEQLVQ-------ANGELEKASREETFARTALKN 650
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1704-1943 |
3.10e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1704 AQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDeladeIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNM 1783
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1784 ELLNDRFRKTTLQVDTLNtelaaersaaqkSDNARQQLERQNKELKAKLQELEgavkSKFKA---TISALEAKIGQLEEQ 1860
Cdd:COG3206 243 AALRAQLGSGPDALPELL------------QSPVIQQLRAQLAELEAELAELS----ARYTPnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1861 LEQEAKERAAanklvrrtekklkEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEaeeeatranasRRKLQRELDD 1940
Cdd:COG3206 307 LQQEAQRILA-------------SLEAELEALQAREASLQAQLAQLEARLAELPELEAE-----------LRRLEREVEV 362
|
...
gi 1907083610 1941 ATE 1943
Cdd:COG3206 363 ARE 365
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
882-1468 |
3.28e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.21 E-value: 3.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 882 EEELQAKDEELLKVKE-------KQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 954
Cdd:PRK01156 189 EEKLKSSNLELENIKKqiaddekSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 955 LHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQ---LEKVTAEAKIKKMEEevllLEDQNSKFIKE 1031
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSnidAEINKYHAIIKKLSV----LQKDYNDYIKK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1032 KKLMEDRIAECS----------SQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:PRK01156 345 KSRYDDLNNQILelegyemdynSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSK 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVQLTKKEEELQGALAR----------GDDETLH--------KNNALKVARELQAQIAELQEDFESEKA 1163
Cdd:PRK01156 425 VSSLNQRIRALRENLDELSRNMEMLNGQsvcpvcgttlGEEKSNHiinhynekKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1164 SRNKAEKQKRDLSE----ELEALKTELEDTLDTTAAQQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATALEE 1238
Cdd:PRK01156 505 RKEYLESEEINKSIneynKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLkLEDLDSKRTSWLNALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1239 LSEQLEQAKRFKANLEKNKQGLETDnkelacevkvLQQVKAESEHKRKKLDAQVQELHAKVsegdrlrvelaekanklqN 1318
Cdd:PRK01156 585 NRSRSNEIKKQLNDLESRLQEIEIG----------FPDDKSYIDKSIREIENEANNLNNKY------------------N 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1319 ELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEllqeetrqklnLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVL 1398
Cdd:PRK01156 637 EIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-----------ITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1399 ALQSQLADTKKKVDDDLGTIESLEEAKKKL--LKDV-EALSQ-------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLD 1468
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKKIKKAIgdLKRLrEAFDKsgvpamiRKSASQAMTSLTRKYLFEFNLDFDDIDVDQD 785
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1620-1915 |
3.29e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1620 EKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR 1699
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1700 DEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKsALLDEKRRLEARIAQLEEELEEE 1779
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK-ELVEKIKELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1780 QSNMELLNdRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELegavkskfKATISALEAKIGQLEE 1859
Cdd:COG1340 160 EKLKELRA-ELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADEL--------HKEIVEAQEKADELHE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1860 QLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRHADQyKEQMEKANARMKQLKR 1915
Cdd:COG1340 231 EIIELQKE-------LRELRKELKKLRKKQRALKREKEK-EELEEKAEEIFEKLKK 278
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
940-1401 |
3.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 940 MRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVL 1019
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1020 LLED--QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNkqevmisDLEERLKKEEKTRQELEKAKRKLDGET-- 1095
Cdd:COG4717 120 KLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEE-------ELEELEAELAELQEELEELLEQLSLATee 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1096 --TDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDD-----ETLHKNNALKVARELQAQIAELQEdFESEKASRNKA 1168
Cdd:COG4717 193 elQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlenelEAAALEERLKEARLLLLIAAALLA-LLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1169 EKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKR 1248
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1249 FKANLEKNKQGLETDNKELACEvKVLQQVKAESEHKRKKLDAQVQELHAkvsegdrLRVELAEKANKLQNELDNVSTLLE 1328
Cdd:COG4717 352 LLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQE-------LKEELEELEEQLEELLGELEELLE 423
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1329 EAEKKGIKfaKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKN--SLQEQQEEEEEARKNLEKQVLALQ 1401
Cdd:COG4717 424 ALDEEELE--EELEELEEELEELEEELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALK 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1605-1943 |
3.78e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1605 AQFERDLQ-TRDEQNEEKKRLL-----LKQVRELEAELEDE---------RKQRALAVASK-KKMEIDLKDLEAQIEAAN 1668
Cdd:COG3096 288 LELRRELFgARRQLAEEQYRLVemareLEELSARESDLEQDyqaasdhlnLVQTALRQQEKiERYQEDLEELTERLEEQE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1669 KARDEVIKQLRKLQAQmkdyqreLEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR-------HAEQER 1741
Cdd:COG3096 368 EVVEEAAEQLAEAEAR-------LEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEKARAlcglpdlTPENAE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1742 DELADEIANSASGKSALLDEKRRLeariaqleeeleeeqSNMELLNDRFRKTtLQvdtLNTELAAERSAAQKSDNARQQL 1821
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKL---------------SVADAARRQFEKA-YE---LVCKIAGEVERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1822 eRQNKELKAKLQELEgavkskfkatisALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKeifmqvederrHADQYKE 1901
Cdd:COG3096 502 -RRYRSQQALAQRLQ------------QLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLD-----------AAEELEE 557
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907083610 1902 QMEKANARMKQLKRQLEeaeeeatRANASRRKLQRELDDATE 1943
Cdd:COG3096 558 LLAELEAQLEELEEQAA-------EAVEQRSELRQQLEQLRA 592
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
833-1330 |
4.37e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 833 ARKAFAKKQQQLSALKVLQRNCAAYLKLR-----------HWQWWRVFTKVKpLLQ--VTRQEEELQAKDEELLKVKEKQ 899
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARerlaeleylraALRLWFAQRRLE-LLEaeLEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 900 TKV-----------------------------EGELEEMERKHQQLLEekniLAEQLQAETELFAEA-EEMRARLAAKKQ 949
Cdd:COG4913 319 DALreeldeleaqirgnggdrleqlereierlERELEERERRRARLEA----LLAALGLPLPASAEEfAALRAEAAALLE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 950 ELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLeeqldeeegARQKLQLEKvtAEAKIKKMEEEVLLLEDQNSKFI 1029
Cdd:COG4913 395 ALEEELEALEEALAEAEAALRDLRRELRELEAEIASL---------ERRKSNIPA--RLLALRDALAEALGLDEAELPFV 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1030 KEkkLMEDRIAECSSQLAEE-------------EEKAKNLAKI--RNKQEVMISDLEERLKKEEKTRQELEKAK--RKLD 1092
Cdd:COG4913 464 GE--LIEVRPEEERWRGAIErvlggfaltllvpPEHYAAALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSlaGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1093 GETTDLQDQI-AELQAQVDELKVQltkKEEELQ---------------GALARGDDETLHK-------NNALKVAReLQA 1149
Cdd:COG4913 542 FKPHPFRAWLeAELGRRFDYVCVD---SPEELRrhpraitragqvkgnGTRHEKDDRRRIRsryvlgfDNRAKLAA-LEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1150 QIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELE---DTLDTTAAQQELRTKrEQEVAELKKAlEDETKNHEAQIQ 1226
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswDEIDVASAEREIAEL-EAELERLDAS-SDDLAALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1227 DMRQRhataLEELSEQLEQAKRFKANLEKNKQGLETDNKELacEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEgDRLR 1306
Cdd:COG4913 696 ELEAE----LEELEEELDELKGEIGRLEKELEQAEEELDEL--QDRLEAAEDLARLELRALLEERFAAALGDAVE-RELR 768
|
570 580
....*....|....*....|....
gi 1907083610 1307 VELAEKANKLQNELDNVSTLLEEA 1330
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERA 792
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1102-1358 |
4.37e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 52.14 E-value: 4.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVQLTKKEEElQGALArgdDETLHKNNALKVARELQAQIAEL---QEDFES--EKASRNKAEKQKRDLS 1176
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAA-QNALA---DKERAEADRQRLEQEKQQQLAAIsgsQSQLEStdQNALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1177 EELEALKTELE------DTLDTTAAQQELRTK--REQEVAELKKALE---DETKNH-EAQIQDMRQRHATALEELSEQLE 1244
Cdd:NF012221 1613 EESRAVTKELTtlaqglDALDSQATYAGESGDqwRNPFAGGLLDRVQeqlDDAKKIsGKQLADAKQRHVDNQQKVKDAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1245 QAKRFKANLEKNKQGLETDNKelacevkvlqqvKAESEHKRKKLDAQVQELHAKVSEGDrlrvelaekanklqneldnVS 1324
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDID------------DAKADAEKRKDDALAKQNEAQQAESD-------------------AN 1741
|
250 260 270
....*....|....*....|....*....|....*
gi 1907083610 1325 TLLEEAEKKGIKFAKDAAGLESQLQ-DTQELLQEE 1358
Cdd:NF012221 1742 AAANDAQSRGEQDASAAENKANQAQaDAKGAKQDE 1776
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1423-1673 |
6.81e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1423 EAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKkfdqllaeekgisaryAEER 1502
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----------------ALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1503 DRAEAEAREKETKAlSLARALEEALEAKEEFERQNKQLRADMedLMSSKD--DVGKNVHELEKSKRALEQQVEEMRTQLE 1580
Cdd:COG4942 84 ELAELEKEIAELRA-ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDflDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1581 ELE---DELQATEDAKLRLevnmqamkaqferdlqtRDEQNEEKKRL--LLKQVRELEAELEDERKQRALAVASKKKMEI 1655
Cdd:COG4942 161 ELAalrAELEAERAELEAL-----------------LAELEEERAALeaLKAERQKLLARLEKELAELAAELAELQQEAE 223
|
250
....*....|....*...
gi 1907083610 1656 DLKDLEAQIEAANKARDE 1673
Cdd:COG4942 224 ELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1646-1813 |
6.94e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1646 AVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQE 1725
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1726 ELASSERARrhaeqERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELA 1805
Cdd:COG1579 81 QLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
....*...
gi 1907083610 1806 AERSAAQK 1813
Cdd:COG1579 156 AELEELEA 163
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1148-1367 |
7.28e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1148 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQD 1227
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1228 MRQ--RHATALEEL--SEQLEQakrFKANLEKNKQGLETDNKELacevKVLQQVKAESEHKRKKLDAQVQELHAKVSEGD 1303
Cdd:COG3883 95 LYRsgGSVSYLDVLlgSESFSD---FLDRLSALSKIADADADLL----EELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1304 RLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSS 1367
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1431-1687 |
8.46e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1431 DVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLD--HQRQIVS--NLEKKQKKFDQllAEEKGISARYAEERDRAE 1506
Cdd:pfam05667 227 NSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTeaTSGASRSaqDLAELLSSFSG--SSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1507 AEAREKETKALSLARALEEALEAKEEFERQNK--QLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELED 1584
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVETEEELQQQREEEleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEK 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1585 ELQATEDAKLRL---EVNMQAMKAQFE---RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQralavASKKKMEI-DL 1657
Cdd:pfam05667 385 QYKVKKKTLDLLpdaEENIAKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE-----SQRKLEEIkEL 459
|
250 260 270
....*....|....*....|....*....|
gi 1907083610 1658 KDLEAQIEAANKARDEVIKQlrkLQAQMKD 1687
Cdd:pfam05667 460 REKIKEVAEEAKQKEELYKQ---LVAEYER 486
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1538-1757 |
8.51e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1538 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDEL-------QATEDAKLRLEV------------ 1598
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgeraralYRSGGSVSYLDVllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1599 NMQAMKAQFERDLQTRDEQNEEKKRLllkqvRELEAELEDERKQralAVASKKKMEIDLKDLEAQIEAANKARDEVIKQL 1678
Cdd:COG3883 120 RLSALSKIADADADLLEELKADKAEL-----EAKKAELEAKLAE---LEALKAELEAAKAELEAQQAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1679 RKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSA 1757
Cdd:COG3883 192 AAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1036-1209 |
9.92e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.79 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1036 EDRIAECSSQLAEEEEKAKNLakirnKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQ------- 1108
Cdd:COG3206 181 EEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQlgsgpda 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1109 ---------VDELKVQLTKKEEELQGALARGDDEtlHknnalKVARELQAQIAELQEDFESE--------KASRNKAEKQ 1171
Cdd:COG3206 256 lpellqspvIQQLRAQLAELEAELAELSARYTPN--H-----PDVIALRAQIAALRAQLQQEaqrilaslEAELEALQAR 328
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907083610 1172 KRDLSEELEALKTELEDTLDTTAAQQELrtKREQEVAE 1209
Cdd:COG3206 329 EASLQAQLAQLEARLAELPELEAELRRL--EREVEVAR 364
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1424-1690 |
1.01e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1424 AKKKLLKDVealsqrLEEKVLA-YDKLEKTKNR-LQQELDDLTVDLDH-QRQIVS--------------NLEKKQKKFDQ 1486
Cdd:PHA02562 151 ARRKLVEDL------LDISVLSeMDKLNKDKIReLNQQIQTLDMKIDHiQQQIKTynknieeqrkkngeNIARKQNKYDE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1487 LLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRadmedlMSSKDDV----GKNVHELE 1562
Cdd:PHA02562 225 LVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK------MYEKGGVcptcTQQISEGP 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1563 KSKRALEQQVEEMRTQLEELEDELQatEDAKLRLEVNMQAMKAqfeRDLQTRDEQNEEKKRLLLKQVRELEAELEderkq 1642
Cdd:PHA02562 299 DRITKIKDKLKELQHSLEKLDTAID--ELEEIMDEFNEQSKKL---LELKNKISTNKQSLITLVDKAKKVKAAIE----- 368
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1907083610 1643 ralavaskkKMEIDLKDLEAQIEAANKARDEVIKQLRKLqaQMKDYQR 1690
Cdd:PHA02562 369 ---------ELQAEFVDNAEELAKLQDELDKIVKTKSEL--VKEKYHR 405
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1050-1459 |
1.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1050 EEKAKNLAKIRNKQEVM----ISDLEERLKKEEKTRQELEKAKRKLDgettDLQDQIAELQAQVDELKVQLTKKEEELQG 1125
Cdd:COG4717 52 EKEADELFKPQGRKPELnlkeLKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1126 AlargddetlhknNALKVARELQAQIAELQEDFESEKAsrnkAEKQKRDLSEELEALKTELEdtldttaaqqELRTKREQ 1205
Cdd:COG4717 128 L------------PLYQELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELA----------ELQEELEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1206 EVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKE------------------- 1266
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearlllliaaallal 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1267 --------------------------------------LACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVE 1308
Cdd:COG4717 262 lglggsllsliltiagvlflvlgllallflllarekasLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1309 LAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQ--EETRQKLNLSSRIRQLEEE----------- 1375
Cdd:COG4717 342 LLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQleellgeleel 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1376 -----KNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDD--DLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDK 1448
Cdd:COG4717 422 lealdEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAALKLALEL 501
|
490
....*....|.
gi 1907083610 1449 LEKTKNRLQQE 1459
Cdd:COG4717 502 LEEAREEYREE 512
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1237-1886 |
1.09e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1237 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSegdRLRVELAEKA--- 1313
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS---AQRVELAERQlqe 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1314 NKLQN-ELDNVSTLLEEAEKKGIKFAKDaaglesqlqdTQELLQEETRQKLNLSSRirqLEEEKNSLQEQQEEEEEARKN 1392
Cdd:COG5022 887 LKIDVkSISSLKLVNLELESEIIELKKS----------LSSDLIENLEFKTELIAR---LKKLLNNIDLEEGPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1393 LEKQVLALQ-SQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQR 1471
Cdd:COG5022 954 PELNKLHEVeSKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASK 1033
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1472 QIVSNLEKKQKKfdQLLAEEKGISAryaeerdrAEAEAREKETKALSLARALEEALEAKEEFER--QNKQLRADMEDLMS 1549
Cdd:COG5022 1034 IISSESTELSIL--KPLQKLKGLLL--------LENNQLQARYKALKLRRENSLLDDKQLYQLEstENLLKTINVKDLEV 1103
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1550 SKDDVGKNVHELEK-----SKRALEQQVEEMRTQLeeledeLQATEDAKLRLEVNMQAMKAQFerDLQTRDEQNEEKKRL 1624
Cdd:COG5022 1104 TNRNLVKPANVLQFivaqmIKLNLLQEISKFLSQL------VNTLEPVFQKLSVLQLELDGLF--WEANLEALPSPPPFA 1175
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1625 LLKQVRELEAELEDERKQRALAVASKKKMEIDLkdlEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFA 1704
Cdd:COG5022 1176 ALSEKRLYQSALYDEKSKLSSSEVNDLKNELIA---LFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDT 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1705 QSKESEKKLKSLEAEI---LQLQEELASSERARRHAEQER--DELADEIANSAS-GKSALLDEKRRLEARIAQLEEELEE 1778
Cdd:COG5022 1253 PASMSNEKLLSLLNSIdnlLSSYKLEEEVLPATINSLLQYinVGLFNALRTKASsLRWKSATEVNYNSEELDDWCREFEI 1332
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1779 EQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNarqQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLE 1858
Cdd:COG5022 1333 SDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLN---PAEIQNLKSRYDPADKENNLPKEILKKIEALLIK---QE 1406
|
650 660
....*....|....*....|....*...
gi 1907083610 1859 EQLEQEAKeraaanklvRRTEKKLKEIF 1886
Cdd:COG5022 1407 LQLSLEGK---------DETEVHLSEIF 1425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
918-1167 |
1.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 918 EEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIqdleeqldeeegar 997
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 998 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQevmISDLEERLKKE 1077
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ---AEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1078 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQED 1157
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
250
....*....|
gi 1907083610 1158 FESEKASRNK 1167
Cdd:COG4942 243 TPAAGFAALK 252
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
688-712 |
1.31e-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: 1.31e-05
10 20
....*....|....*....|....*
gi 1907083610 688 YKESLTKLMATLRNTNPNFVRCIIP 712
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
873-1373 |
1.32e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 873 KPLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKhqqlLEEKNILAEQLQA-----ETELFAEAEEMRARLAAK 947
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE----LDDRNMEVQRLEAllkamKSECQGQMERQMAAIQGK 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 948 KQELEEI---LHDLESrvEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEakIKKMEEEVLLLEDQ 1024
Cdd:pfam15921 457 NESLEKVsslTAQLES--TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE--ITKLRSRVDLKLQE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1025 NSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGEttdLQDQIAE 1104
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKE---INDRRLE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1105 LQaqvdELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKt 1184
Cdd:pfam15921 606 LQ----EFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK- 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1185 eledtldttaaqQELRTKREqevaelkkalEDETKNHEAQIQdmrqrhataLEELSEQLEQAKrfkaNLEKNKQGleTDN 1264
Cdd:pfam15921 681 ------------RNFRNKSE----------EMETTTNKLKMQ---------LKSAQSELEQTR----NTLKSMEG--SDG 723
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1265 KELACEVKVLQQVKAesehKRKKLDA---QVQELHAKVSEGDRLRVELAEKANKLQNELDNVST----------LLEEAE 1331
Cdd:pfam15921 724 HAMKVAMGMQKQITA----KRGQIDAlqsKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATeknkmageleVLRSQE 799
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1332 KK------GIKFAKDAAGLE-SQLQD-TQELLQEETRQKLNLSSRIRQLE 1373
Cdd:pfam15921 800 RRlkekvaNMEVALDKASLQfAECQDiIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1343-1828 |
1.42e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1343 GLESQLQDTQELLQEE--TRQKLNLSSRIRQL-----EEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKK---KVD 1412
Cdd:PRK04863 227 GVRKAFQDMEAALRENrmTLEAIRVTQSDRDLfkhliTESTNYVAADYMRHANERRVHLEEALELRRELYTSRRqlaAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1413 DDLGTI----ESLEEAKKKLLKDVEALSQRL---EEKVLAYDKLEktknRLQQELDDLTVDLDHQRQIVSNLekkqkkfd 1485
Cdd:PRK04863 307 YRLVEMarelAELNEAESDLEQDYQAASDHLnlvQTALRQQEKIE----RYQADLEELEERLEEQNEVVEEA-------- 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1486 qllaeekgisaryAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKsk 1565
Cdd:PRK04863 375 -------------DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADN-- 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1566 raLEQQVEEMRTQLEELEDELQATEDaKLRLEvnmQAMKAQFERDLQTRDEQNEEKKRLLLKQV-RELeaeLEDERKQRA 1644
Cdd:PRK04863 440 --AEDWLEEFQAKEQEATEELLSLEQ-KLSVA---QAAHSQFEQAYQLVRKIAGEVSRSEAWDVaREL---LRRLREQRH 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1645 LAvASKKKMEIDLKDLE---AQIEAANKARDEVIKQLRKLQAQMKDYQRELEEarasrdeifaqskesekklksLEAEIL 1721
Cdd:PRK04863 511 LA-EQLQQLRMRLSELEqrlRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEE---------------------LEARLE 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1722 QLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLND---RFRKTTLQVD 1798
Cdd:PRK04863 569 SLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQlleRERELTVERD 648
|
490 500 510
....*....|....*....|....*....|
gi 1907083610 1799 tlntelaaeRSAAQKsdnarQQLERQNKEL 1828
Cdd:PRK04863 649 ---------ELAARK-----QALDEEIERL 664
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1656-1950 |
1.49e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1656 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARR 1735
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1736 HAEQERDELADEIANsasgKSALLdekRRLEARIAQLEEELEeeqsNMELLNDRFRKTTLQVDTLNTELAAER-SAAQKS 1814
Cdd:pfam19220 101 EAEAAKEELRIELRD----KTAQA---EALERQLAAETEQNR----ALEEENKALREEAQAAEKALQRAEGELaTARERL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1815 DNARQQLERQNK----------ELKAKLQELEG----------AVKSKFKATISALEAKIGQLEEQLEQEAKERA----- 1869
Cdd:pfam19220 170 ALLEQENRRLQAlseeqaaelaELTRRLAELETqldatrarlrALEGQLAAEQAERERAEAQLEEAVEAHRAERAslrmk 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1870 --AANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEG 1947
Cdd:pfam19220 250 leALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEM 329
|
...
gi 1907083610 1948 LSR 1950
Cdd:pfam19220 330 LTK 332
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1022-1264 |
1.55e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 49.93 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1022 EDQNSKFIKEKKLMEdRIAECSSQLAEEEEKAKNLAKIRNKQEVmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:PRK05771 39 ELSNERLRKLRSLLT-KLSEALDKLRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKIEKEIKELEEEISELENE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVqLTKKEEELQgaLARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNK-------AEKQKRD 1174
Cdd:PRK05771 116 IKELEQEIERLEP-WGNFDLDLS--LLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYvyvvvvvLKELSDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1175 LSEELEALKTELEDTLDTTAAQQELRTKrEQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSEQLEQAkRFKANLE 1254
Cdd:PRK05771 193 VEEELKKLGFERLELEEEGTPSELIREI-KEELEEIEKERESL----LEELKELAKKYLEELLALYEYLEIE-LERAEAL 266
|
250
....*....|
gi 1907083610 1255 KNkqGLETDN 1264
Cdd:PRK05771 267 SK--FLKTDK 274
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1077-1371 |
1.77e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.05 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1077 EEKTRQELEKAKrklDGETTDLQDQIAELQAQVDELkvqltkkeEELQGALARGDDETLHKNNALKVARELQAQIAElqe 1156
Cdd:PRK10929 25 EKQITQELEQAK---AAKTPAQAEIVEALQSALNWL--------EERKGSLERAKQYQQVIDNFPKLSAELRQQLNN--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1157 dfESEKASRNKAEKQKRDLSEELEALKTELEDtlDTTAAQQElrtkreqevaelkkaledetknheaqiQDMRQRHATAL 1236
Cdd:PRK10929 91 --ERDEPRSVPPNMSTDALEQEILQVSSQLLE--KSRQAQQE---------------------------QDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1237 EELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQvkAESEHKRkkldAQVQELH-AKVS-----EGDRLRVELA 1310
Cdd:PRK10929 140 SQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTALQ--AESAALK----ALVDELElAQLSannrqELARLRSELA 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1311 EK-ANKLQNELDNVSTLL--------EEAEKKGIKFAKDAAGLE----SQLQDTQELLQE--ETRQKLNL-SSRIRQ 1371
Cdd:PRK10929 214 KKrSQQLDAYLQALRNQLnsqrqreaERALESTELLAEQSGDLPksivAQFKINRELSQAlnQQAQRMDLiASQQRQ 290
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1215-1437 |
2.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1215 EDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELacevkvlqqvkaesehkrKKLDAQVQE 1294
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI------------------DKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1295 LHAKVsegDRLRVELAEKANKLQNELDNVSTLLEEAEKKGI-KFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLE 1373
Cdd:COG3883 77 AEAEI---EERREELGERARALYRSGGSVSYLDVLLGSESFsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1374 EEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQ 1437
Cdd:COG3883 154 AKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1571-1916 |
2.11e-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: 49.97 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1571 QVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRAL--AVA 1648
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1649 SKKKMEIDLKDLEAQIEAANKARD-----EVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQL 1723
Cdd:TIGR00618 268 RIEELRAQEAVLEETQERINRARKaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1724 QEELASSERARRHAEQErdeladeiansaSGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE 1803
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVA------------TSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1804 LAAERSAAQKSDNARQQLERQNKELKaklqelegavkskfkatisaleakigQLEEQLEQEAKERAAANKLVRRTEKKLK 1883
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAE--------------------------LCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
330 340 350
....*....|....*....|....*....|...
gi 1907083610 1884 EIFMQVEDERRHADQYKEQMEKANARMKQLKRQ 1916
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEE 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1401-1619 |
3.33e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1401 QSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKK 1480
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1481 QKK-------FDQLLAeekgiSARYAEERDRAEAeareketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDD 1553
Cdd:COG3883 95 LYRsggsvsyLDVLLG-----SESFSDFLDRLSA-----------LSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1554 VGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNE 1619
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1078-1248 |
4.07e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1078 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQ--LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1155
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1156 EDFES--EKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1233
Cdd:COG3206 247 AQLGSgpDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170
....*....|....*
gi 1907083610 1234 TALEELSEQLEQAKR 1248
Cdd:COG3206 327 AREASLQAQLAQLEA 341
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1630-1744 |
4.51e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1630 RELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEifaqSKES 1709
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR----EIRK 463
|
90 100 110
....*....|....*....|....*....|....*
gi 1907083610 1710 EKKLKSLEAEILQLQEELASSERARRHAEQERDEL 1744
Cdd:COG2433 464 DREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1145-1294 |
4.56e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1145 RELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTldtTAAQQELRTKREQEvaelkkALEDETKNHEAQ 1224
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY---EEQLGNVRNNKEYE------ALQKEIESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1225 IQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQE 1294
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1344-1713 |
4.78e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.35 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1344 LESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEE 1423
Cdd:pfam07888 36 LEECLQERAELLQAQEAAN-------RQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1424 AKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL-----------EKKQKKFDQLLAEEK 1492
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAgaqrkeeeaerKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1493 GISARYAEERDRAEaearEKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQV 1572
Cdd:pfam07888 189 SLSKEFQELRNSLA----QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1573 EEM-RTQLEELEDELQATE------DAKLRLEVNmQAMKAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRal 1645
Cdd:pfam07888 265 AQRdRTQAELHQARLQAAQltlqlaDASLALREG-RARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMER-- 341
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1646 avaskKKMEIDLkdleAQIEAANKA-RDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1713
Cdd:pfam07888 342 -----EKLEVEL----GREKDCNRVqLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
996-1211 |
5.16e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 996 ARQKLQlekvTAEAKIKKMEEE--VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEEr 1073
Cdd:COG3206 187 LRKELE----EAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1074 LKKEEKTRQELEKAKRKLDGETTDLQD---QIAELQAQVDELKVQLTKKEEELQGALargddetlhkNNALKVARELQAQ 1150
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAALRAQLQQEAQRILASL----------EAELEALQAREAS 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1151 IAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLdttAAQQELRTKREQEVAELK 1211
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLL---QRLEEARLAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1340-1520 |
5.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1340 DAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVD------- 1412
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1413 ----------------------DDLGTIESLEEAKKKLLKDVEALSQRLEEKvlaydklektKNRLQQELDDLTVDLDHQ 1470
Cdd:COG3883 97 rsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAK----------KAELEAKLAELEALKAEL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1471 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLA 1520
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1048-1319 |
5.32e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 48.41 E-value: 5.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1048 EEEEKAKNLAKIRNKQEvmisdlEERLKKEEKTRQEleKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1127
Cdd:PRK05035 442 EQEKKKAEEAKARFEAR------QARLEREKAAREA--RHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGAR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1128 ARGDDETLHKNNALKVARELQAQIAELQEDfESEKAS------RNKAEKQkrdlseELEALKTELEDTLDTTAAQQELRT 1201
Cdd:PRK05035 514 PDNSAVIAAREARKAQARARQAEKQAAAAA-DPKKAAvaaaiaRAKAKKA------AQQAANAEAEEEVDPKKAAVAAAI 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1202 KREQEVAELKKALEDETKNHEAQIQDMRQRHATAleelseqLEQAKRFKANLE-KNKQGLETDNKELAcevkvlqqVKAE 1280
Cdd:PRK05035 587 ARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAA-------IARAKAKKAEQQaNAEPEEPVDPRKAA--------VAAA 651
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083610 1281 SEHKRKKLDAQVQELHAKVSEGDRLRVELAE-----KANKLQNE 1319
Cdd:PRK05035 652 IARAKARKAAQQQANAEPEEAEDPKKAAVAAaiaraKAKKAAQQ 695
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1304-1509 |
5.86e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1304 RLRVELAEKANK-LQNELDNVSTLLEEAEKKGIKFAKdaaglESQLQDTQELLQEETRQKLNLSSRIRQLEEEknslqeq 1382
Cdd:COG3206 167 ELRREEARKALEfLEEQLPELRKELEEAEAALEEFRQ-----KNGLVDLSEEAKLLLQQLSELESQLAEARAE------- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1383 qeeeeeaRKNLEKQVLALQSQLADTKKKVDDDLG--TIESLEEAKKKLLKDVEALSQRLEEK----VLAYDKLEKTKNRL 1456
Cdd:COG3206 235 -------LAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIAALRAQL 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1457 QQELDDLTVDLDHQRQI----VSNLEKKQKKFDQLLAEEKGISARYAE-ERDRAEAEA 1509
Cdd:COG3206 308 QQEAQRILASLEAELEAlqarEASLQAQLAQLEARLAELPELEAELRRlEREVEVARE 365
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1159-1374 |
6.01e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 6.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1159 ESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAElkkALEDETKNHEAQIQDMRQRhataLEE 1238
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELE------EAEAALEEFRQKNGLV---DLSEEAKLLLQQLSELESQ----LAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1239 LSEQLEQAKRFKANLEKNKQGLETDNKELAcEVKVLQQVKAEsehkRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQN 1318
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELL-QSPVIQQLRAQ----LAELEAELAELSARYTPNHPDVIALRAQIAALRA 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1319 ELDnvstllEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEE 1374
Cdd:COG3206 306 QLQ------QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1032-1372 |
6.06e-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. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1032 KKLMEDRIAECSSQLAEEEE--------KAKN--------LAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1095
Cdd:pfam06160 55 DDIVTKSLPDIEELLFEAEElndkyrfkKAKKaldeieelLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1096 TDLQDQ-------IAELQAQVDELKVQLTKKEEELQGalarGDDETlhknnALKVARELQAQIAELQEDFESEKASRNKA 1168
Cdd:pfam06160 135 KTLLANrfsygpaIDELEKQLAEIEEEFSQFEELTES----GDYLE-----AREVLEKLEEETDALEELMEDIPPLYEEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1169 EKQKRDLSEELEALKTELED---TLDTTAAQQELRTKREQeVAELKKALED-ETKNHEAQIQDMRQRhataLEELSEQLE 1244
Cdd:pfam06160 206 KTELPDQLEELKEGYREMEEegyALEHLNVDKEIQQLEEQ-LEENLALLENlELDEAEEALEEIEER----IDQLYDLLE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1245 QAKRFKANLEKNKQGLETD-------NKELACEVKVLQQ---VKAESEHKRKKLDAQVQELHAKVsegDRLRVELAEKA- 1313
Cdd:pfam06160 281 KEVDAKKYVEKNLPEIEDYlehaeeqNKELKEELERVQQsytLNENELERVRGLEKQLEELEKRY---DEIVERLEEKEv 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1314 --NKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQL 1372
Cdd:pfam06160 358 aySELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1279-1456 |
7.19e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1279 AESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEE 1358
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLGNVRNNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1359 TRQKLnlssRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDlgtIESLEEAKKKLLKDVEALSQR 1438
Cdd:COG1579 99 ESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAK 171
|
170
....*....|....*....
gi 1907083610 1439 LEEKVLA-YDKLEKTKNRL 1456
Cdd:COG1579 172 IPPELLAlYERIRKRKNGL 190
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1081-1245 |
7.44e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1081 RQEL---EKAKRKLDGETTDLQDQIA-------ELQAQVDELKVQLTKKEEE---LQGALARGDDEtlhknnalkvAREL 1147
Cdd:PRK09039 45 SREIsgkDSALDRLNSQIAELADLLSlerqgnqDLQDSVANLRASLSAAEAErsrLQALLAELAGA----------GAAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1148 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELedtldttaaqqelrtkreQEVAELKKALEDETKNHEAQIQD 1227
Cdd:PRK09039 115 EGRAGELAQELDSEKQVSARALAQVELLNQQIAALRRQL------------------AALEAALDASEKRDRESQAKIAD 176
|
170
....*....|....*...
gi 1907083610 1228 MRQRHATALEELSEQLEQ 1245
Cdd:PRK09039 177 LGRRLNVALAQRVQELNR 194
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1656-1887 |
7.95e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 47.76 E-value: 7.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1656 DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskeSEKKLKSLE-AEILQLQEELASSERAR 1734
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEEL------EAAALQPGEeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1735 RHAEQERDELADEIANSASgksaLLDE-KRRLEaRIAQleeeleeEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQk 1813
Cdd:COG0497 226 EALQEALEALSGGEGGALD----LLGQaLRALE-RLAE-------YDPSLAELAERLESALIELEEAASELRRYLDSLE- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1814 SDNAR-QQLE-RQN--------------------KELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKE---- 1867
Cdd:COG0497 293 FDPERlEEVEeRLAllrrlarkygvtveellayaEELRAELAELENS-----DERLEELEAELAEAEAELLEAAEKlsaa 367
|
250 260
....*....|....*....|.
gi 1907083610 1868 -RAAANKLVRRTEKKLKEIFM 1887
Cdd:COG0497 368 rKKAAKKLEKAVTAELADLGM 388
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1560-1961 |
8.23e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAklrlevnmQAMKAQFERDLQTRDEQNEEKKRLLlKQVRELEAELEDE 1639
Cdd:TIGR00618 202 RSQLLTLCTPCMPDTYHERKQVLEKELKHLREA--------LQQTQQSHAYLTQKREAQEEQLKKQ-QLLKQLRARIEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1640 RKQraLAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSL--- 1716
Cdd:TIGR00618 273 RAQ--EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLqtl 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1717 ------------EAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE-----------KRRLEARIAQLE 1773
Cdd:TIGR00618 351 hsqeihirdaheVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQReqatidtrtsaFRDLQGQLAHAK 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1774 EELEEEQSNMELLnDRFRKTTLQVDTLntELAAERSAAQKSDNARQQLerQNKELKAKLQELEGAVKSKFKATISALEAK 1853
Cdd:TIGR00618 431 KQQELQQRYAELC-AAAITCTAQCEKL--EKIHLQESAQSLKEREQQL--QTKEQIHLQETRKKAVVLARLLELQEEPCP 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1854 IGQLEEQLEQEAKERAAANKLVRRT----------EKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQleeaeee 1923
Cdd:TIGR00618 506 LCGSCIHPNPARQDIDNPGPLTRRMqrgeqtyaqlETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC------- 578
|
410 420 430
....*....|....*....|....*....|....*...
gi 1907083610 1924 ATRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:TIGR00618 579 DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHA 616
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
873-1276 |
9.10e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 873 KPLLQVTRQEEELQAKD--EELLKVKEKQTKVEGELEEMERKhqqlleekniLAEQLQAETELFAEAEEMRARLAAKKQE 950
Cdd:pfam07888 1 KPLDELVTLEEESHGEEggTDMLLVVPRAELLQNRLEECLQE----------RAELLQAQEAANRQREKEKERYKRDREQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 951 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 1030
Cdd:pfam07888 71 WERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERET 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1031 EKKLMEDRIAECSSQLAEEEEKAKNLakirnkqEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVD 1110
Cdd:pfam07888 151 ELERMKERAKKAGAQRKEEEAERKQL-------QAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1111 ELKvqltKKEEELQGALA--RGDDETLH--KNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALK--- 1183
Cdd:pfam07888 224 TAH----RKEAENEALLEelRSLQERLNasERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALRegr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1184 ----TELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL---EKN 1256
Cdd:pfam07888 300 arwaQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLrvaQKE 379
|
410 420
....*....|....*....|
gi 1907083610 1257 KQGLETDNKELACEVKVLQQ 1276
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQLEQ 399
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
880-1228 |
9.17e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 9.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 880 RQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleEKNILAEQlqaetelfaeaeemRARLAAKkQELEEILHDLE 959
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNA--EKNILLLN--------------QARLQAL-EDLEKILTEKE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 960 SrveeeeernqiLQNEKKKMQAHIQDLEEQLdeeegarqklqleKVTAEAKIKkmeeeVLLLEDQNSKFIKEKKLMEDRI 1039
Cdd:PLN02939 167 A-----------LQGKINILEMRLSETDARI-------------KLAAQEKIH-----VEILEEQLEKLRNELLIRGATE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1040 AECSSQLAEEEE--KAKNLAkIRNKQEVM------ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIaelqAQVDE 1111
Cdd:PLN02939 218 GLCVHSLSKELDvlKEENML-LKDDIQFLkaelieVAETEERVFKLEKERSLLDASLRELESKFIVAQEDV----SKLSP 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKVQ-LTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTELEDTL 1190
Cdd:PLN02939 293 LQYDcWWEKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASD 371
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1907083610 1191 DTTAAQQELRTKREQEVAELKKALEDETKNH--EAQIQDM 1228
Cdd:PLN02939 372 HEIHSYIQLYQESIKEFQDTLSKLKEESKKRslEHPADDM 411
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1112-1317 |
1.04e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL---EALKTELED 1188
Cdd:PRK09039 44 LSREISGKDSALD---------------------RLNSQIAELADLLSLERQGNQDLQDSVANLRASLsaaEAERSRLQA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1189 TLDTTAAQqelRTKREQEVAELKKALEDEtknheaqiQDMRQRHATALEELSEQLEQAKRfkanleknkqgletdnkELA 1268
Cdd:PRK09039 103 LLAELAGA---GAAAEGRAGELAQELDSE--------KQVSARALAQVELLNQQIAALRR-----------------QLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1907083610 1269 cevkVLQQVKAESEHKRKKLDAQVQELhakvseGDRLRVELAEKANKLQ 1317
Cdd:PRK09039 155 ----ALEAALDASEKRDRESQAKIADL------GRRLNVALAQRVQELN 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1274-1401 |
1.06e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1274 LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAglESQLQDTQE 1353
Cdd:PRK00409 518 LNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA--DEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1907083610 1354 LLQEETRqklnlSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQ 1401
Cdd:PRK00409 596 LQKGGYA-----SVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1090-1516 |
1.31e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1090 KLDGETTDLQDQIAELQAQVDelkvqlTKKEEELQGALARGDDETLHKNNALKVarelqaqiaelQEDFESEKASRNKAE 1169
Cdd:NF012221 1355 EIDEVGSDLGDSLTGSVTQVE------TPDLNAMQNALNIDESVLSTQAPNLIV-----------NGDFEQGAEGWNSTY 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1170 KQKRDLS--------EELEALKTELeDTLDTTAAQQELRTKREQEVAELK----KALEDETKNHEAQIQDMRQRHATALE 1237
Cdd:NF012221 1418 GVEASHSasvyglraEGHGARVSEL-DTYTNTSLYQDLSNLTAGEVIALSfdfaRRAGLSTNNGIEVLWNGEVVFASSGD 1496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1238 ELSEQLEQAK----------RFKANLEKNKQGLETDNKELACEVKvlQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRV 1307
Cdd:NF012221 1497 ASAWQQKTLKltakagsnrlEFKGTGHNDGLGYILDNVVATSESS--QQADAVSKHAKQDDAAQNALADKERAEADRQRL 1574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1308 ElAEKanklQNELDNVSTLLEEAEkkgikfAKDAAGLESQLQDTQELLQEETRQ-KLNLSSRIRQLEEEKNSLQEQQEEE 1386
Cdd:NF012221 1575 E-QEK----QQQLAAISGSQSQLE------STDQNALETNGQAQRDAILEESRAvTKELTTLAQGLDALDSQATYAGESG 1643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1387 EEARKNLEKQVLA-LQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTV 1465
Cdd:NF012221 1644 DQWRNPFAGGLLDrVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG------EQNQANAEQDIDDAKA 1717
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1907083610 1466 DLDHQRQivsnlEKKQKKFDQLLAEEKGiSARYAEERDRAEAEAREKETKA 1516
Cdd:NF012221 1718 DAEKRKD-----DALAKQNEAQQAESDA-NAAANDAQSRGEQDASAAENKA 1762
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
876-1090 |
1.34e-04 |
|
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: 47.04 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 876 LQVTRQEEelqaKDEELLKVKEKQTKVEGE-LEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEI 954
Cdd:pfam17380 350 LERIRQEE----RKRELERIRQEEIAMEISrMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 955 LHDLESrveEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIkEKKL 1034
Cdd:pfam17380 426 RAEQEE---ARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKEL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1035 MEDRIAecssqLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRK 1090
Cdd:pfam17380 502 EERKQA-----MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1538-1873 |
1.36e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1538 KQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMR---TQLEELEDELQATEDAKLRLEVNMQAMKAQ------FE 1608
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSitlKEIERLSIEYNNAMDDYNNLKSALNELSSLedmknrYE 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1609 RDLQTRDE--QNEEKKRLLLKQVRELEAELEDE----RKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQ 1682
Cdd:PRK01156 256 SEIKTAESdlSMELEKNNYYKELEERHMKIINDpvykNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1683 AQMKDY---QRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALL 1759
Cdd:PRK01156 336 KDYNDYikkKSRYDDLNNQILEL----EGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1760 DEKRR-----------LEARIAQLEEELEEEQSNMELLNDRFR-----------KTTLQVDTLNTELAAERSAAQKSDNA 1817
Cdd:PRK01156 412 NEINVklqdisskvssLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEEKIREIEIE 491
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1818 RQQLERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANK 1873
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1617-1937 |
1.40e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1617 QNEEKKRLLLKQVRELEAELEDERKQRALA----VASKKKMEI---DLKDLEAQIEAA----NKARDEVI--KQLRKLQA 1683
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEqyrlVEMARELAElneAESDLEQDYQAAsdhlNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1684 QMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERA----------RRHAEQERDE---LADEIAN 1750
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERakqLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1751 SASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRkttlQVDTLNTELAAERSAAQKSDNARQqLERQNKELKA 1830
Cdd:PRK04863 436 TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSRSEAWDVARE-LLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1831 KLQELEgavkskfkatisALEAKIGQLEEQLEQEAkeraAANKLVRRTEKKLKeifMQVEDErrhaDQYKEQMEKANARM 1910
Cdd:PRK04863 511 LAEQLQ------------QLRMRLSELEQRLRQQQ----RAERLLAEFCKRLG---KNLDDE----DELEQLQEELEARL 567
|
330 340
....*....|....*....|....*..
gi 1907083610 1911 KQLKRQLEEAEEEATRANASRRKLQRE 1937
Cdd:PRK04863 568 ESLSESVSEARERRMALRQQLEQLQAR 594
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1288-1646 |
1.41e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.60 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1288 LDAQVQEL---HAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKkgikfakDAAGLESQLQDTQELLQEETRQKLN 1364
Cdd:pfam19220 36 IEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEG-------ELEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1365 LSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVL 1444
Cdd:pfam19220 109 LRIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1445 AYDKLEKTKNRLQQELDDltvdldhQRQIVSNLEKKqkkfdqlLAEEKgisaryaEERDRAEAEAREK----ETKALSLA 1520
Cdd:pfam19220 189 ELAELTRRLAELETQLDA-------TRARLRALEGQ-------LAAEQ-------AERERAEAQLEEAveahRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1521 RALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLE--V 1598
Cdd:pfam19220 248 MKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEerA 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1599 NM-----QAMKAQFER------DLQTRDEQNE---EKKRLLLKQ-VRELEAELEDERKQRALA 1646
Cdd:pfam19220 328 EMltkalAAKDAALERaeeriaSLSDRIAELTkrfEVERAALEQaNRRLKEELQRERAERALA 390
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1564-1719 |
1.56e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1564 SKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRLLLKQV---RELEAEL---- 1636
Cdd:pfam09787 41 SSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERsarREAEAELerlq 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1637 -------EDERKQRALAVASKKKMEIDLKDLEAQIEA---ANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQS 1706
Cdd:pfam09787 121 eelryleEELRRSKATLQSRIKDREAEIEKLRNQLTSksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQL 200
|
170
....*....|...
gi 1907083610 1707 KESEKKLKSLEAE 1719
Cdd:pfam09787 201 ERMEQQIKELQGE 213
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1600-1994 |
1.70e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1600 MQAMKAQFERDLQTRDEQ----NEEKKRLLLKQVRELEAELEDERKQralaVASKKKMEIDLKDLEAQIEAANKARDEVI 1675
Cdd:COG4717 40 LAFIRAMLLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1676 KQLRKLQaQMKDYQRELEEARASRDEIfaqsKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGK 1755
Cdd:COG4717 116 EELEKLE-KLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1756 SA----LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTE-----------LAAERSAAQKSDNARQQ 1820
Cdd:COG4717 191 EEelqdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlkearllllIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1821 LERQNKELKAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYK 1900
Cdd:COG4717 271 LILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1901 EQMEKANARMKQLKRQLEEAEEEA--TRANASRRKLQRELDDATEANEGLSREVSTLKNRLRR-GGPISFSSSRSGRRQL 1977
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAAllAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEElLGELEELLEALDEEEL 430
|
410
....*....|....*..
gi 1907083610 1978 HIEGASLELSDDDTESK 1994
Cdd:COG4717 431 EEELEELEEELEELEEE 447
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
923-1243 |
1.76e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 923 LAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLE-------SRVEEEEERNQILQNEKKKMQAhiqdleeqlDEEEG 995
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQrlaeyswDEIDVASAEREIAELEAELERL---------DASSD 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 996 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkQEVMISDLEERLK 1075
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA---------RLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1076 KEEKTRQELEKAKRkldgettdLQDQIAELQAQVDELKVQLTKKeeeLQGALARGDDETLHKNNALKVARELQAQIAELQ 1155
Cdd:COG4913 757 AALGDAVERELREN--------LEERIDALRARLNRAEEELERA---MRAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1156 ED----FESE-KASRNKAEKQKR-DLSEELEALKTELEDTLDT-------------TAAQQELRTKREQEVAELKKALED 1216
Cdd:COG4913 826 EDglpeYEERfKELLNENSIEFVaDLLSKLRRAIREIKERIDPlndslkripfgpgRYLRLEARPRPDPEVREFRQELRA 905
|
330 340
....*....|....*....|....*..
gi 1907083610 1217 ETKNHEAQIQDMRQRHATALEELSEQL 1243
Cdd:COG4913 906 VTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
932-1506 |
1.84e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 932 ELFAEAEEMRaRLAAKKQELEEILHDLESRVEEEEErnqiLQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKI 1011
Cdd:PRK01156 153 KILDEILEIN-SLERNYDKLKDVIDMLRAEISNIDY----LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1012 KKMEEEVLLLED---QNSKFIKEKKLMEDRIAECSSQLAEEEEKAknlakirnkqeVMISDLEERLKKEEKTRQeleKAK 1088
Cdd:PRK01156 228 NNAMDDYNNLKSalnELSSLEDMKNRYESEIKTAESDLSMELEKN-----------NYYKELEERHMKIINDPV---YKN 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1089 RKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGA--LARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1166
Cdd:PRK01156 294 RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLsvLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1167 KAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRhataLEELSEQL--- 1243
Cdd:PRK01156 374 SLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALREN----LDELSRNMeml 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1244 ---------------EQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDA-QVQELHAKVSEGDRLRV 1307
Cdd:PRK01156 450 ngqsvcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESeEINKSINEYNKIESARA 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1308 ELAEKANKLqNELDNVSTLLEEA--EKKGIKFakdaaglesqlqdtqELLQEETRQKLNLSSRIRQLEEEknSLQEQQEE 1385
Cdd:PRK01156 530 DLEDIKIKI-NELKDKHDKYEEIknRYKSLKL---------------EDLDSKRTSWLNALAVISLIDIE--TNRSRSNE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1386 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIE---SLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDD 1462
Cdd:PRK01156 592 IKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEneaNNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE 671
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1907083610 1463 LTVDLDhqrQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAE 1506
Cdd:PRK01156 672 ITSRIN---DIEDNLKKSRKALDDAKANRARLESTIEILRTRIN 712
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1049-1518 |
1.85e-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: 46.67 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1049 EEEKAKNLAKIRNKQEVMISDL----EERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQ 1124
Cdd:pfam07111 135 EEGSQRELEEIQRLHQEQLSSLtqahEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELE 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1125 GALARgdDETLHKNNALKVARELQAQIAE------------LQEDFESEKAS------RNKAEKQKRDLSEELEALKTEL 1186
Cdd:pfam07111 215 AQVTL--VESLRKYVGEQVPPEVHSQTWElerqelldtmqhLQEDRADLQATvellqvRVQSLTHMLALQEEELTRKIQP 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1187 EDTLD---TTAAQQELRTKREQeVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETD 1263
Cdd:pfam07111 293 SDSLEpefPKKCRSLLNRWREK-VFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1264 N---KELACEVKVLQQVKAESEHKRKKLDAQVQ-----------ELHAKVSEGDRLRVELAEKANKLQNELDNVSTL--- 1326
Cdd:pfam07111 372 RmsaKGLQMELSRAQEARRRQQQQTASAEEQLKfvvnamsstqiWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIkgl 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1327 ------LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQ---KLNLSSRIRQLE--EEKNSLQEQQEEEEEARKNLEK 1395
Cdd:pfam07111 452 markvaLAQLRQESCPPPPPAPPVDADLSLELEQLREERNRldaELQLSAHLIQQEvgRAREQGEAERQQLSEVAQQLEQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1396 QVLALQSQLADTKKKVDDDL-GTIESLEEA---KKKLLKDVEALSQRLEEKVlaydklEKTKNRLQQELDDLTVDLDHQR 1471
Cdd:pfam07111 532 ELQRAQESLASVGQQLEVARqGQQESTEEAaslRQELTQQQEIYGQALQEKV------AEVETRLREQLSDTKRRLNEAR 605
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907083610 1472 QIVSNLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKALS 1518
Cdd:pfam07111 606 REQAKAVVSLRQIQHRATQEK----ERNQELRRLQDEARKEEGQRLA 648
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1663-1943 |
1.86e-04 |
|
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: 46.66 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1663 QIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASR----DEIFAQSKESEKKLKSLEAEILQLQEElassERARRHAE 1738
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1739 QERDELADEIANSASGKSALLDEKRRLEaRIAQLEEELEEEQSNMEllnDRFRKTTLQVDTLNtELAAERSAAQKSDNAR 1818
Cdd:pfam17380 365 IRQEEIAMEISRMRELERLQMERQQKNE-RVRQELEAARKVKILEE---ERQRKIQQQKVEME-QIRAEQEEARQREVRR 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1819 QQLERQNKELKAKLQELEgavKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRT-EKKLKEIFMQ-VEDERRHA 1896
Cdd:pfam17380 440 LEEERAREMERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAmIEEERKRK 516
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907083610 1897 DQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATE 1943
Cdd:pfam17380 517 LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE 563
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1051-1186 |
1.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.74 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1051 EKAK-NLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLtkkEEELQGALar 1129
Cdd:PRK00409 505 EEAKkLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAI-- 579
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1130 gddetlhkNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRdLSEELEALKTEL 1186
Cdd:PRK00409 580 --------KEAKKEADEIIKELRQLQKGGYASVKAHELIEARKR-LNKANEKKEKKK 627
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1676-1961 |
2.05e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1676 KQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAE---QERDELADEIANSA 1752
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEkevKELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1753 SGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRfrkttlqvdtlntelAAERSAAQKSDNARQQLERQNKELKAKL 1832
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK---------------VKELKELKEKAEEYIKLSEFYEEYLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1833 QELEgavkskfkATISALEAKIGQLEEQLeqeaKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANaRMKQ 1912
Cdd:PRK03918 310 REIE--------KRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELER 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907083610 1913 LKRQLeeaeeeatrANASRRKLQRELDDATEANEGLSREVSTLKNRLRR 1961
Cdd:PRK03918 377 LKKRL---------TGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1537-1669 |
2.15e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 46.59 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1537 NKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDE 1616
Cdd:pfam05911 683 NKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYE-DLETRLT 761
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1617 QNEEKKRLLLKQVRELEAELEDERKqralavaSKKKMEIDLKDLEAQIEAANK 1669
Cdd:pfam05911 762 ELEAELNELRQKFEALEVELEEEKN-------CHEELEAKCLELQEQLERNEK 807
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1391-1915 |
2.20e-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: 46.28 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1391 KNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLtvdldHQ 1470
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRL-----HQ 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1471 RQIVSNLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREketkalsLARALEEALEAKEEFERQNKQLRADMEDLMSS 1550
Cdd:pfam07111 151 EQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQ-------LAEAQKEAELLRKQLSKTQEELEAQVTLVESL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1551 KDDVGKNV--------------------HELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD 1610
Cdd:pfam07111 224 RKYVGEQVppevhsqtwelerqelldtmQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1611 LQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVAS--------------------KKKMEIDL-----KDLEAQIE 1665
Cdd:pfam07111 304 CRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAElqeqvtsqsqeqailqralqDKAAEVEVermsaKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1666 AANKAR-------DEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL----------KSLEAEILQLQEELA 1728
Cdd:pfam07111 384 RAQEARrrqqqqtASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQ 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1729 SSERARRHAEQERDELADEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNME---------LLNDRFRKTTLQVDT 1799
Cdd:pfam07111 464 ESCPPPPPAPPVDADLSLELEQLREERNRL-DAELQLSAHLIQQEVGRAREQGEAErqqlsevaqQLEQELQRAQESLAS 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1800 LNTELAAERSAAQKSD----NARQQLERQNKELKAKLQELEGAVKSKFKATISALEAKigqLEEQLEQEAKERAAANKLV 1875
Cdd:pfam07111 543 VGQQLEVARQGQQESTeeaaSLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRR---LNEARREQAKAVVSLRQIQ 619
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1907083610 1876 RRT--EKKLKEIFMQVEDERRhadqyKEQMEKANARMKQLKR 1915
Cdd:pfam07111 620 HRAtqEKERNQELRRLQDEAR-----KEEGQRLARRVQELER 656
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1803-1915 |
2.29e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1803 ELAAERSAAQKSDNARQ--QLERQNKELKAKLQELEGAVKSKfKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEK 1880
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLEEQVERLEAEVEELEAELEEK-DERIERLERELSEARSEERREIRKDREISRLDREIER 476
|
90 100 110
....*....|....*....|....*....|....*
gi 1907083610 1881 KLKEIfmqvEDERRHADQYKEQMEkanaRMKQLKR 1915
Cdd:COG2433 477 LEREL----EEERERIEELKRKLE----RLKELWK 503
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
875-1297 |
2.34e-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: 46.58 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 875 LLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEME---RKHQQLLEEKNI---LAEQLQAET----ELFAEAEEMRARL 944
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKndiEEQETLLGTIMPeeeSAKVCLTDVtimeRFQMELKDVERKI 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 945 AAKKQELEEIlhDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQL---EKVTAEAKIKKMEEEVLLL 1021
Cdd:TIGR00606 809 AQQAAKLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnELKSEKLQIGTNLQRRQQF 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1022 EDQNSKFIKEkklMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:TIGR00606 887 EEQLVELSTE---VQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK 963
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQvdelkvQLTKKEEELQGALARGDDETLHKNnalkvarelqaqiaELQEDFESEKASRNKAEKQKRDLSEELEA 1181
Cdd:TIGR00606 964 IQDGKDD------YLKQKETELNTVNAQLEECEKHQE--------------KINEDMRLMRQDIDTQKIQERWLQDNLTL 1023
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1182 LKTELEDTLDTTAAQQELRTKREQEVAELKKaledETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL-EKNKQGL 1260
Cdd:TIGR00606 1024 RKRENELKEVEEELKQHLKEMGQMQVLQMKQ----EHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELrEPQFRDA 1099
|
410 420 430
....*....|....*....|....*....|....*..
gi 1907083610 1261 ETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHA 1297
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFHS 1136
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
905-1503 |
2.54e-04 |
|
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: 46.58 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 905 ELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEeilhdLESRVEEEEERNQILQNEKKKmqahiq 984
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALA-----IKNKFAKTKKDSEIIIKEIKD------ 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 985 dleeqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMED--------------------RIAECss 1044
Cdd:TIGR01612 1556 -----------AHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDiqlslenfenkflkisdikkKINDC-- 1622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1045 qLAEEEEKAKNLAKIR-NKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQdqiaELQAQVDELKVQLTKKEEEL 1123
Cdd:TIGR01612 1623 -LKETESIEKKISSFSiDSQDTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELD----ELDSEIEKIEIDVDQHKKNY 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1124 QGALARGDDETLHKNNalkvaRELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKR 1203
Cdd:TIGR01612 1698 EIGIIEKIKEIAIANK-----EEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEFIELYNIIAGC 1772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1204 EQEVAElkkalEDETKNheaQIQDMRqrhATALEELSEQLEQAKRFKANLeknkqgletDNKELACEVKVLQQVKAESEH 1283
Cdd:TIGR01612 1773 LETVSK-----EPITYD---EIKNTR---INAQNEFLKIIEIEKKSKSYL---------DDIEAKEFDRIINHFKKKLDH 1832
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1284 KRKKLDAQvqelHAKVSEG-DRL-----RVELAEKANKLQNELDNVSTLL------------EEAEKKGIKFAKDAAGLE 1345
Cdd:TIGR01612 1833 VNDKFTKE----YSKINEGfDDIsksieNVKNSTDENLLFDILNKTKDAYagiigkkyysykDEAEKIFINISKLANSIN 1908
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1346 SQLQDTQEL-------------LQEETRQKL-------NLSSRIRQLEEEKNSLQEQQEEEEEARKNlEKQVLAL---QS 1402
Cdd:TIGR01612 1909 IQIQNNSGIdlfdniniailssLDSEKEDTLkfipspeKEPEIYTKIRDSYDTLLDIFKKSQDLHKK-EQDTLNIifeNQ 1987
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1403 QLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEE---------------KVLAYDKLEKTKNRLQQELDDLTVDL 1467
Cdd:TIGR01612 1988 QLYEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDElnklscdsqnydtilELSKQDKIKEKIDNYEKEKEKFGIDF 2067
|
650 660 670
....*....|....*....|....*....|....*...
gi 1907083610 1468 DHQ--RQIVSNLEKKQKKFDQLLAEEKGISARYAEERD 1503
Cdd:TIGR01612 2068 DVKamEEKFDNDIKDIEKFENNYKHSEKDNHDFSEEKD 2105
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
882-1166 |
2.60e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 882 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETElfaEAEEMRARLAAKKQELEEilhdlesr 961
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA---EIDKLQAEIAEAEAEIEE-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 962 veeeeeRNQILQNEKKKMQahiqdleeqldeeegaRQKLQLEKVtaeakikkmeeEVLLLEDQNSKFIKEKKLMeDRIAE 1041
Cdd:COG3883 84 ------RREELGERARALY----------------RSGGSVSYL-----------DVLLGSESFSDFLDRLSAL-SKIAD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1042 CSSQLAEEEEKAKnlAKIRNKQevmiSDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEE 1121
Cdd:COG3883 130 ADADLLEELKADK--AELEAKK----AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907083610 1122 ELQGALARGDDETLHKNNALKVARELQAQIAELQEDFESEKASRN 1166
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAG 248
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1560-1705 |
2.76e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERD---------------LQTRDEQNEEKKRL 1624
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrnnkeyeaLQKEIESLKRRISD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1625 LLKQVRELEAELEDERKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKlqaqmkdyqrELEEARASRDEIFA 1704
Cdd:COG1579 108 LEDEILELMERIEELEEE-------LAELEAELAELEAELEEKKAELDEELAELEA----------ELEELEAEREELAA 170
|
.
gi 1907083610 1705 Q 1705
Cdd:COG1579 171 K 171
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1657-1915 |
2.93e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.45 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1657 LKDLEAQIEAANKARDEVIKQLRKLQAQMKdyQRELEEARASRdeifaQSKESEKKLKSLEAEILQLQEELASSERarRH 1736
Cdd:PRK11637 49 LKSIQQDIAAKEKSVRQQQQQRASLLAQLK--KQEEAISQASR-----KLRETQNTLNQLNKQIDELNASIAKLEQ--QQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1737 AEQERDeLADEIANS-----ASGKSALL--DEKRRLEaRIaqleeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERS 1809
Cdd:PRK11637 120 AAQERL-LAAQLDAAfrqgeHTGLQLILsgEESQRGE-RI----------LAYFGYLNQARQETIAELKQTREELAAQKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1810 AAQKSDNARQQLERQNKELKAKLQELEGAVKSkfkaTISALEAKIGQLEEQLEQeakeraaanklVRRTEKKLKEIFMQV 1889
Cdd:PRK11637 188 ELEEKQSQQKTLLYEQQAQQQKLEQARNERKK----TLTGLESSLQKDQQQLSE-----------LRANESRLRDSIARA 252
|
250 260
....*....|....*....|....*..
gi 1907083610 1890 EDE-RRHADQYKEQMEKANARMKQLKR 1915
Cdd:PRK11637 253 EREaKARAEREAREAARVRDKQKQAKR 279
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1102-1379 |
3.29e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 45.62 E-value: 3.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVQLTKKEEELQGALARGDDETLHKnnalkVARELQAQIAE------LQEDFESEKASRNKAEKQK--- 1172
Cdd:PLN03229 431 VRELEGEVEKLKEQILKAKESSSKPSELALNEMIEK-----LKKEIDLEYTEaviamgLQERLENLREEFSKANSQDqlm 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1173 -RDLSEELEALKTELEDTLDTTAAQQELRTKRE--QEVAELKKALEDETKNHEAQiQDMRQRHATALE--ELSEQLEQAK 1247
Cdd:PLN03229 506 hPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlNEFSRAKALSEKKSKAEKLK-AEINKKFKEVMDrpEIKEKMEALK 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1248 RFKANLEKNKQG-LETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELD----- 1321
Cdd:PLN03229 585 AEVASSGASSGDeLDDDLKEKVEKMKKEIELELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINkkier 664
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1322 --NVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSL 1379
Cdd:PLN03229 665 viRSSDLKSKIELLKLEVAKASKTPDVTEKEKIEALEQQIKQKIAEALNSSELKEKFEEL 724
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1671-1836 |
3.37e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 3.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1671 RDEVIKQLRKLQAQMKDyQRELEEARASrdeifaqskesekklkSLEAEILQLQEELASSERARRHAEQERDELADEiAN 1750
Cdd:PRK09039 51 KDSALDRLNSQIAELAD-LLSLERQGNQ----------------DLQDSVANLRASLSAAEAERSRLQALLAELAGA-GA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1751 SASGKSALLDEKRRLEARIAQLEeeleeeQSNMELLNDrfrkttlQVDTLNTELAAERSAAQKSDNARQQLERQ------ 1824
Cdd:PRK09039 113 AAEGRAGELAQELDSEKQVSARA------LAQVELLNQ-------QIAALRRQLAALEAALDASEKRDRESQAKiadlgr 179
|
170
....*....|....
gi 1907083610 1825 --NKELKAKLQELE 1836
Cdd:PRK09039 180 rlNVALAQRVQELN 193
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1446-1888 |
3.48e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 45.67 E-value: 3.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1446 YDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaeEKGISARYAEERDRAEAEAREKETKALsLARALEE 1525
Cdd:COG5278 81 YEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAEL--EQVIALRRAGGLEAALALVRSGEGKAL-MDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1526 ALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1605
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1606 QFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQM 1685
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1686 KDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1765
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1766 EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKA 1845
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1907083610 1846 TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQ 1888
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAA 520
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1560-1728 |
3.59e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.05 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFErDLQTRDEQ-----NEEKKRLLLKQVRELEA 1634
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAE-KWEEKARLalekgREDLAREALERKAELEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1635 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQ---------------------MKDYQRELE 1693
Cdd:COG1842 99 QAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQekvnealsgidsddatsalerMEEKIEEME 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1907083610 1694 EARASRDEIfAQSKESEKKLKSLEAEIlQLQEELA 1728
Cdd:COG1842 179 ARAEAAAEL-AAGDSLDDELAELEADS-EVEDELA 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1568-1959 |
3.84e-04 |
|
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: 45.40 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1568 LEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQF------ERDLQTRDEQNEEKKRLLLKQVRELEAELEDERK 1641
Cdd:TIGR04523 38 LEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIkileqqIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1642 QralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAqmkdyqrELEEARASRDEIFAQSKESEKKLKSLEAEIL 1721
Cdd:TIGR04523 118 Q-------KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-------ELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1722 QLQEELASSERARRHAEQerdeladeianSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLN 1801
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLEL-----------LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1802 TELaaersaaqksDNARQQLERQNKELKAKLQELEGAvkskfKATISALEAKIGQLEEQLEQEAKERAAAnklvrrTEKK 1881
Cdd:TIGR04523 253 TQL----------NQLKDEQNKIKKQLSEKQKELEQN-----NKKIKELEKQLNQLKSEISDLNNQKEQD------WNKE 311
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1882 LKEIFMQVEDERRhadQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:TIGR04523 312 LKSELKNQEKKLE---EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1288-1956 |
4.20e-04 |
|
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: 45.58 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1288 LDAQVQELHakvSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQklnLSS 1367
Cdd:pfam10174 1 LQAQLRDLQ---RENELLRRELDIKESKLGSSMNSIKTFWSPELKKERALRKEEAARISVLKEQYRVTQEENQH---LQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1368 RIRQLEEEKnslqeqqeeeeEARKNLEKqvlALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDvealsqrleekvlaYD 1447
Cdd:pfam10174 75 TIQALQDEL-----------RAQRDLNQ---LLQQDFTTSPVDGEDKFSTPELTEENFRRLQSE--------------HE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1448 KLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLaEEKGISARYAEERDR-----AEAEAREKETKALSLARA 1522
Cdd:pfam10174 127 RQAKELFLLRKTLEEMELRIETQKQTLGARDESIKKLLEML-QSKGLPKKSGEEDWErtrriAEAEMQLGHLEVLLDQKE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1523 LEEALEAKEEFER-QNKQLRADMEDLMSSKDDVGKNVHELEKSKRALEQQVEE--------------------------- 1574
Cdd:pfam10174 206 KENIHLREELHRRnQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMlktngllhtedreeeikqmevykshsk 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1575 -MRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRD------EQNEEKKRLLLKQVRELEAELEdeRKQRALAV 1647
Cdd:pfam10174 286 fMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEvlkeslTAKEQRAAILQTEVDALRLRLE--EKESFLNK 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1648 ASKKKMEI---------DLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEa 1718
Cdd:pfam10174 364 KTKQLQDLteekstlagEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1719 EILQLQEELAssERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVD 1798
Cdd:pfam10174 443 EALSEKERII--ERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1799 TLNTELAAERSAAQKsdnarqqLERQNKelkaKLQELEGAVKSKfkatiSALEAKIGQLEEQLEQEAKERAAANKLVRRt 1878
Cdd:pfam10174 521 SLEIAVEQKKEECSK-------LENQLK----KAHNAEEAVRTN-----PEINDRIRLLEQEVARYKEESGKAQAEVER- 583
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1879 ekkLKEIFMQVEDERRHADQYKEQMEKANARmkQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLK 1956
Cdd:pfam10174 584 ---LLGILREVENEKNDKDKKIAELESLTLR--QMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQ 656
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
874-1247 |
4.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 4.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 874 PLLQVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNI-LAEQLQAETElfaeaEEMRArLAAKKQELE 952
Cdd:PRK04863 777 PLFGRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGShLAVAFEADPE-----AELRQ-LNRRRVELE 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 953 EILHDLESrvEEEEERNQILQnekkkmqahiqdleeqldeeegARQKLQLekvtaeakIKKMEEEVLLLEDQNskfikek 1032
Cdd:PRK04863 851 RALADHES--QEQQQRSQLEQ----------------------AKEGLSA--------LNRLLPRLNLLADET------- 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1033 klMEDRIAECSSQLAEEEEKA-------KNLAKIRNKQEVMISDLE--ERLKKE-EKTRQELEKAKRKLDGETTDLQ--- 1099
Cdd:PRK04863 892 --LADRVEEIREQLDEAEEAKrfvqqhgNALAQLEPIVSVLQSDPEqfEQLKQDyQQAQQTQRDAKQQAFALTEVVQrra 969
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1100 ----DQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhknnalkvARELQAQIAELQEDFESEKASRNKAEKQKRDL 1175
Cdd:PRK04863 970 hfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ----------LRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1176 SEELEALKTELEDTLDTTAA------QQELRTKREQEvAELKKALEDETKNHEAQiqdmrQRHATALEE----LSEQLEQ 1245
Cdd:PRK04863 1040 KQELQDLGVPADSGAEERARarrdelHARLSANRSRR-NQLEKQLTFCEAEMDNL-----TKKLRKLERdyheMREQVVN 1113
|
..
gi 1907083610 1246 AK 1247
Cdd:PRK04863 1114 AK 1115
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1565-1719 |
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 1907083610 1565 KRALEQQVEEMRTQ----LEELEDELQATEDAKLrLEVNMQAM--KAQFERDLQTRDEQNEEKKRLLLKQVRELEAELED 1638
Cdd:PRK12704 26 KKIAEAKIKEAEEEakriLEEAKKEAEAIKKEAL-LEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1639 ERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRE--LEEARA-SRDEIFAQSKESEKKLKs 1715
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKEilLEKVEEeARHEAAVLIKEIEEEAK- 183
|
....
gi 1907083610 1716 LEAE 1719
Cdd:PRK12704 184 EEAD 187
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1558-1959 |
5.03e-04 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 45.02 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1558 VHELEKSKrALEQQVEEMRTQLEELEDELQATEDAKLR----LEVN---MQAMKAQFERdLQTRDEQNEEKKRLLLKQVR 1630
Cdd:pfam05701 31 IQTVERRK-LVELELEKVQEEIPEYKKQSEAAEAAKAQvleeLESTkrlIEELKLNLER-AQTEEAQAKQDSELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1631 ELEAELEDErkqraLAVASKKKMEIDLKDLEAQIEAANKARDEvikqLRKLQAQMKDYQRELEEARASRDEIFAQSKESE 1710
Cdd:pfam05701 109 EMEQGIADE-----ASVAAKAQLEVAKARHAAAVAELKSVKEE----LESLRKEYASLVSERDIAIKRAEEAVSASKEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1711 KKLKSLEAEILQLQEELASSERARRHAEQERDELA-----DEIANSASGKSALlDEKRRLEARIAQLEEELEEEQSNMEL 1785
Cdd:pfam05701 180 KTVEELTIELIATKESLESAHAAHLEAEEHRIGAAlareqDKLNWEKELKQAE-EELQRLNQQLLSAKDLKSKLETASAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1786 LNDrfrkttlqvdtLNTELAAERSAAQKSDNARQQLERQ-NKELKAKL----QELEGAVKSKFKAT--ISALEAKIGQLE 1858
Cdd:pfam05701 259 LLD-----------LKAELAAYMESKLKEEADGEGNEKKtSTSIQAALasakKELEEVKANIEKAKdeVNCLRVAAASLR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1859 EQLEQEAKERAAanklVRRTEKKLKEIFMQVEDERRHADQ----YKEQMEKANARMKQLKRQLEEAEEEATRANASRRKL 1934
Cdd:pfam05701 328 SELEKEKAELAS----LRQREGMASIAVSSLEAELNRTKSeialVQAKEKEAREKMVELPKQLQQAAQEAEEAKSLAQAA 403
|
410 420
....*....|....*....|....*
gi 1907083610 1935 QRELDDATEANEGLSREVSTLKNRL 1959
Cdd:pfam05701 404 REELRKAKEEAEQAKAAASTVESRL 428
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1614-1884 |
5.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1614 RDEQNEEKKRLLLKQVRELEAELEDERKQRA-LAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL 1692
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLrKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1693 EEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQL 1772
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1773 EEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATISALEA 1852
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270
....*....|....*....|....*....|..
gi 1907083610 1853 KIGQLEEQLEQEAKERAAANKLVRRTEKKLKE 1884
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1006-1333 |
5.13e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 5.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1006 TAEAKIKKMEEEVLLL---EDQNSKFIKE---------KKLMEDR------IAECSSQLAEEEE---KAKNLAKIRNKQE 1064
Cdd:PRK04778 116 LIEEDIEQILEELQELlesEEKNREEVEQlkdlyrelrKSLLANRfsfgpaLDELEKQLENLEEefsQFVELTESGDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1065 --VMISDLEERLKKEEKTRQELEKAKRKLDgetTDLQDQIAELQAQVDELKVQ------------LTKKEEELQGALArg 1130
Cdd:PRK04778 196 arEILDQLEEELAALEQIMEEIPELLKELQ---TELPDQLQELKAGYRELVEEgyhldhldiekeIQDLKEQIDENLA-- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1131 DDETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQE---LRTKREQEV 1207
Cdd:PRK04778 271 LLEELDLDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQsytLNESELESV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1208 AELKKALEDETKNHEAQIQDMRQRHATA------LEELSEQLEQAKRFKANLEKNKQGLETDnkELACEVKVLQQVKAES 1281
Cdd:PRK04778 351 RQLEKQLESLEKQYDEITERIAEQEIAYselqeeLEEILKQLEEIEKEQEKLSEMLQGLRKD--ELEAREKLERYRNKLH 428
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1282 EHKRK------------------KLDAQVQELHAKVSEGdRLRVElaekanKLQNELDNVSTLLEEAEKK 1333
Cdd:PRK04778 429 EIKRYleksnlpglpedylemffEVSDEIEALAEELEEK-PINME------AVNRLLEEATEDVETLEEE 491
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1560-1698 |
5.75e-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: 44.28 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQTRDEQ-NEEKKRLLLKQVRELEAELED 1638
Cdd:cd22656 111 ELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLlTDEGGAIARKEIKDLQKELEK 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1639 ERKqrALAVASKKKMEiDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAS 1698
Cdd:cd22656 191 LNE--EYAAKLKAKID-ELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIGPAIPA 247
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1341-1942 |
6.18e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1341 AAGLESQLQDTQELLQEETRQKLNLSsriRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQladtkKKVD---DDLGT 1417
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMA---RELEELSARESDLEQDYQAASDHLNLVQTALRQQ-----EKIEryqEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1418 IES-LEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRL---QQELDDLTVDLDHQRQIVSNLEKKQKkfdqlLAEEKG 1493
Cdd:COG3096 359 LTErLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLadyQQALDVQQTRAIQYQQAVQALEKARA-----LCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1494 ISARYAEERdRAEAEAREKE-TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD--DVGKNVHELEKSKRALEQ 1570
Cdd:COG3096 434 LTPENAEDY-LAAFRAKEQQaTEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQawQTARELLRRYRSQQALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1571 QVEEMRTQLEELEDELQATEDAKLRLEvnmqAMKAQFERDLQTRDEQNEEKKrlllkqvrELEAELEDERKQRALAVASK 1650
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLLE----EFCQRIGQQLDAAEELEELLA--------ELEAQLEELEEQAAEAVEQR 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1651 KKMEIDLKDLEAQI--------------EAANKARDEVIKQLRKLQAQMKDYQRELE---EARASRDEIFAQSKESEKKL 1713
Cdd:COG3096 581 SELRQQLEQLRARIkelaarapawlaaqDALERLREQSGEALADSQEVTAAMQQLLErerEATVERDELAARKQALESQI 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1714 KSL-------EAEILQLQEELA---------------------------------------------------------- 1728
Cdd:COG3096 661 ERLsqpggaeDPRLLALAERLGgvllseiyddvtledapyfsalygparhaivvpdlsavkeqlagledcpedlyliegd 740
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1729 ---------------------SSERARR-----------------HAEQ---ERDELADEIANSASGKSALLDEKRRLEA 1767
Cdd:COG3096 741 pdsfddsvfdaeeledavvvkLSDRQWRysrfpevplfgraarekRLEElraERDELAEQYAKASFDVQKLQRLHQAFSQ 820
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1768 RIAQLEEELEEEQSNMELLNDRFRKTTLQvDTLNTELAAERSAAQKSDNARQQLERQNK------------------ELK 1829
Cdd:COG3096 821 FVGGHLAVAFAPDPEAELAALRQRRSELE-RELAQHRAQEQQLRQQLDQLKEQLQLLNKllpqanlladetladrleELR 899
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1830 AKLQELEGAVKS--KFKATISALEAKIGQL------EEQLEQEAKERAAANKLVRRTEKKLKEIFmqvedERRHADQYKE 1901
Cdd:COG3096 900 EELDAAQEAQAFiqQHGKALAQLEPLVAVLqsdpeqFEQLQADYLQAKEQQRRLKQQIFALSEVV-----QRRPHFSYED 974
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1907083610 1902 --QMEKANARM-KQLKRQLEEAEEEATRANASRRKLQRELDDAT 1942
Cdd:COG3096 975 avGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYN 1018
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1055-1287 |
6.40e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1055 NLAKIR-NKQEVMISDLEERLKKEE-KTRQELEKAKRKLDGE-TTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1131
Cdd:PHA02562 172 NKDKIReLNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1132 DETlhknNALKVARELQAQIAelqedfeSEKASRNKAEKQ----------KRDLSEElEALKTELEDTLDTTAAQQELRT 1201
Cdd:PHA02562 252 DPS----AALNKLNTAAAKIK-------SKIEQFQKVIKMyekggvcptcTQQISEG-PDRITKIKDKLKELQHSLEKLD 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1202 KREQEVAELKKALEDETKNheaqIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAE- 1280
Cdd:PHA02562 320 TAIDELEEIMDEFNEQSKK----LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTk 395
|
....*..
gi 1907083610 1281 SEHKRKK 1287
Cdd:PHA02562 396 SELVKEK 402
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1026-1184 |
6.69e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.85 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1026 SKFIK-EKKLMEDR---------IAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGET 1095
Cdd:COG2433 350 NKFERvEKKVPPDVdrdevkarvIRGLSIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEV 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1096 TDLQDQIAELQAQVDELKVQLTK-KEEELQGALARgddetlhknnalkvaRElqaqIAELQEDFESEKASRNKAEKQKRD 1174
Cdd:COG2433 430 EELEAELEEKDERIERLERELSEaRSEERREIRKD---------------RE----ISRLDREIERLERELEEERERIEE 490
|
170
....*....|
gi 1907083610 1175 LSEELEALKT 1184
Cdd:COG2433 491 LKRKLERLKE 500
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
882-1244 |
6.92e-04 |
|
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: 44.75 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 882 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELEEILHDLESR 961
Cdd:pfam09731 84 EEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHT 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 962 VEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAE 1041
Cdd:pfam09731 164 DSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1042 CSSQLAEEEEKAKN-----LAKIRNKQEVMISDLEERLKKEEKTRqeLEKAKRKLDgettDLQDQIAELQAQVDE-LKVQ 1115
Cdd:pfam09731 244 LVDQYKELVASERIvfqqeLVSIFPDIIPVLKEDNLLSNDDLNSL--IAHAHREID----QLSKKLAELKKREEKhIERA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1116 LTKKEEELqgalargddETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQKrdLSEELEALKTELEDTLDTTAA 1195
Cdd:pfam09731 318 LEKQKEEL---------DKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEK--LRTELERQAEAHEEHLKDVLV 386
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1907083610 1196 QQELRTKREQEvAELKKALEDETKNHEAQIQDMrqrhATALEELSEQLE 1244
Cdd:pfam09731 387 EQEIELQREFL-QDIKEKVEEERAGRLLKLNEL----LANLKGLEKATS 430
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1644-1860 |
7.15e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.66 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1644 ALAVASKKKMEIDLKDLEAqieAANKARDEVIKQL---------RKLQAQ-MKDYQRELEE----ARASRDEIFAQSKE- 1708
Cdd:PRK10929 19 AATAPDEKQITQELEQAKA---AKTPAQAEIVEALqsalnwleeRKGSLErAKQYQQVIDNfpklSAELRQQLNNERDEp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1709 ----SEKKLKSLEAEILQLQEELAssERARRhAEQERDElADEIANSASGKSALLDEKRRL----EARI-AQLEEELEEE 1779
Cdd:PRK10929 96 rsvpPNMSTDALEQEILQVSSQLL--EKSRQ-AQQEQDR-AREISDSLSQLPQQQTEARRQlneiERRLqTLGTPNTPLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1780 QSNMELLNDRFRKTTLQVDTLntELAaersaaQKSDNARQQLER--------QNKELKAKLQELEGAVKS-KFKATISAL 1850
Cdd:PRK10929 172 QAQLTALQAESAALKALVDEL--ELA------QLSANNRQELARlrselakkRSQQLDAYLQALRNQLNSqRQREAERAL 243
|
250
....*....|
gi 1907083610 1851 EaKIGQLEEQ 1860
Cdd:PRK10929 244 E-STELLAEQ 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
996-1135 |
8.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 996 ARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIR---------NKQEVM 1066
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealqkeiESLKRR 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1067 ISDLEERLK----KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETL 1135
Cdd:COG1579 105 ISDLEDEILelmeRIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELL 177
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1145-1333 |
9.39e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1145 RELQAQIAELQEdFESEKAsrnKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQevaelKKALEDETKNHEAQ 1224
Cdd:COG1579 3 PEDLRALLDLQE-LDSELD---RLEHRLKELPAELAELEDELA------ALEARLEAAKTE-----LEDLEKEIKRLELE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1225 IQDMRQRhataLEELSEQLEQAKRFK--ANLEKNKQGLETDNKELAcevKVLQQVKAESEHKRKKLDAQVQELHAKVSEG 1302
Cdd:COG1579 68 IEEVEAR----IKKYEEQLGNVRNNKeyEALQKEIESLKRRISDLE---DEILELMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1907083610 1303 DRLRVELAEKANKLQNELDNVSTLLEEAEKK 1333
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1067-1224 |
1.10e-03 |
|
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: 42.67 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1067 ISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARE 1146
Cdd:pfam12795 80 LEELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQAELA 159
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1147 -LQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEdtldttAAQQELRTKREQEVAELKKALEDETKNHEAQ 1224
Cdd:pfam12795 160 aLKAQIDMLEQELLSNNNRQDLLKARRDLLTLRIQRLEQQLQ------ALQELLNEKRLQEAEQAVAQTEQLAEEAAGD 232
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1560-1771 |
1.13e-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: 43.30 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEDELQATEDAKlrlevnmqamkaqferdlqtRDEQNEEKKRLLLKQVRELEAELEDE 1639
Cdd:TIGR02794 72 KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK--------------------QAEQAAKQAEEKQKQAEEAKAKQAAE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1640 RKQRALAVASKKKMEidlkdleaqiEAANKARDEVIKqlrKLQAQMKdyqRELEEARASRDEIFAQSKESEKKLKSLEAE 1719
Cdd:TIGR02794 132 AKAKAEAEAERKAKE----------EAAKQAEEEAKA---KAAAEAK---KKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1720 ILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQ 1771
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAE 247
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1609-1915 |
1.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1609 RDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDLK-------DLEAQIEAANKARDEVIKQLRKL 1681
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQaaqaelaQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1682 QAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELASSERARRHAEQERDELA----DEIANSASGKSA 1757
Cdd:COG4372 121 QKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldelLKEANRNAEKEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1758 LLDEKRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEG 1837
Cdd:COG4372 201 ELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1838 AVKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKR 1915
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLEL 358
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
877-1231 |
1.21e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.96 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKqtkvegeLEEMERKHQQLleekNILAEQLQAETELFAEAEEMRARLAAKKQELE---E 953
Cdd:pfam05557 119 QIQRAELELQSTNSELEELQER-------LDLLKAKASEA----EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEqdsE 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 954 ILHDLESRVeeeeERNQILQNEKKKMQAHIQDLEEQLdeeegaRQKLQLEKVTAEAKIK-----KMEEEVLLLEDQNSKF 1028
Cdd:pfam05557 188 IVKNSKSEL----ARIPELEKELERLREHNKHLNENI------ENKLLLKEEVEDLKRKlereeKYREEAATLELEKEKL 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1029 IKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMI---SDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1105
Cdd:pfam05557 258 EQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKeenSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRH 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1106 QAQVDEL--KVQLTKKEEELQGALARGDDETLHKNNA----LKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEEL 1179
Cdd:pfam05557 338 KALVRRLqrRVLLLTKERDGYRAILESYDKELTMSNYspqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1180 EALKTELeDTLDTTAAQQELRTKREqEVAELKKALEDetknHEAQIQDMRQR 1231
Cdd:pfam05557 418 QTLEREL-QALRQQESLADPSYSKE-EVDSLRRKLET----LELERQRLREQ 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1628-1818 |
1.26e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1628 QVRELEAELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSK 1707
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1708 ESEKKLKSLEA--------------------------EILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDE 1761
Cdd:COG3883 97 RSGGSVSYLDVllgsesfsdfldrlsalskiadadadLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1762 KRRLEARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAAERSAAQKSDNAR 1818
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
924-1517 |
1.38e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 924 AEQLQAETELfaeaEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQAHIQdleeqldeeegarqKLQLE 1003
Cdd:pfam05557 2 AELIESKARL----SQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIR--------------LLEKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1004 KVTAEAKIKKMEEEVLLL---EDQNSKFIKEKKLMEDRIAECSSQLAEEeekaknLAKIRNKQEVMISDLEERLKKEEKT 1080
Cdd:pfam05557 64 EAEAEEALREQAELNRLKkkyLEALNKKLNEKESQLADAREVISCLKNE------LSELRRQIQRAELELQSTNSELEEL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1081 RQELEKAKRKLdgetTDLQDQIAELQAQVDELKVQLTK-KEEELQGALARGDDETlhknnaLKVARELQAQIAELQEDFE 1159
Cdd:pfam05557 138 QERLDLLKAKA----SEAEQLRQNLEKQQSSLAEAEQRiKELEFEIQSQEQDSEI------VKNSKSELARIPELEKELE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1160 SEKASRNKAEKQKRD---LSEELEALKTELEdtldttaaqQELRTKREQEVAELKKA-LEDETKNHEAQIQDMRQRHATA 1235
Cdd:pfam05557 208 RLREHNKHLNENIENkllLKEEVEDLKRKLE---------REEKYREEAATLELEKEkLEQELQSWVKLAQDTGLNLRSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1236 lEELSEQLEQAKRFKANLEKNKQGLETDnkelaceVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1315
Cdd:pfam05557 279 -EDLSRRIEQLQQREIVLKEENSSLTSS-------ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1316 LQNELDNVSTLLEEAEKKgIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEearknLEK 1395
Cdd:pfam05557 351 LTKERDGYRAILESYDKE-LTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLE-----REL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1396 QVLALQSQLAD---TKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYD--------------KLEKTKNRLQQ 1458
Cdd:pfam05557 425 QALRQQESLADpsySKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDydpkktkvlhlsmnPAAEAYQQRKN 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1459 ELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERdRAEAEAREKETKAL 1517
Cdd:pfam05557 505 QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDL-RKELESAELKNQRL 562
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1645-1899 |
1.44e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1645 LAVASKKKMEIDLKDLE--AQIEAANKARDEVIKQ--------LRKLQAQMKDYQRELEEARASRDEIFA--QSK--ESE 1710
Cdd:PHA02562 147 LSAPARRKLVEDLLDISvlSEMDKLNKDKIRELNQqiqtldmkIDHIQQQIKTYNKNIEEQRKKNGENIArkQNKydELV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1711 KKLKSLEAEILQLQEELAsserarrhaeqerdELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSN-------- 1782
Cdd:PHA02562 227 EEAKTIKAEIEELTDELL--------------NLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEKGgvcptctq 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1783 -MELLNDRFRKTTLQVDTLNTELaaersaaQKSDNARQQLERQNKELKA---KLQELEGAVkSKFKATISALEAKIGQLE 1858
Cdd:PHA02562 293 qISEGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMDEFNEqskKLLELKNKI-STNKQSLITLVDKAKKVK 364
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907083610 1859 EQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQY 1899
Cdd:PHA02562 365 AAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEKYHR 405
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1008-2000 |
1.51e-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: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1008 EAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQlAEEEEKAKNLAKIRNKQEVMISDLE--------ERLKKEEK 1079
Cdd:TIGR01612 578 EKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDK-NEYIKKAIDLKKIIENNNAYIDELAkispyqvpEHLKNKDK 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1080 TRQELEKAKRKL-DGETTDLQDQIA-----------ELQAQVDELKVQLTKKEEELQGAlargDDET--LHKNNALKVAR 1145
Cdd:TIGR01612 657 IYSTIKSELSKIyEDDIDALYNELSsivkenaidntEDKAKLDDLKSKIDKEYDKIQNM----ETATveLHLSNIENKKN 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1146 ELQAQIAELQEDFESEKAsrnkaekqkRDLSEELEALKT---ELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHE 1222
Cdd:TIGR01612 733 ELLDIIVEIKKHIHGEIN---------KDLNKILEDFKNkekELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDN 803
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1223 AQIQDMRQRHATALE----------ELSEQLEQAKRFK----------ANLEKN-KQGLETDNKELAcevKVLQQVKAES 1281
Cdd:TIGR01612 804 IKDEDAKQNYDKSKEyiktisikedEIFKIINEMKFMKddflnkvdkfINFENNcKEKIDSEHEQFA---ELTNKIKAEI 880
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1282 EhkrkklDAQVQELHAKVSEGDRLrveLAEKANKLQNELDNVSTLLEEAEKkgIKFAKDAAGLESQLQDTQELLQEETRQ 1361
Cdd:TIGR01612 881 S------DDKLNDYEKKFNDSKSL---INEINKSIEEEYQNINTLKKVDEY--IKICENTKESIEKFHNKQNILKEILNK 949
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1362 KLNLSsrirqleEEKNSLQeqqeeeeearKNLEKQvlaLQSQLADTKKKVDDDL--GTIESLEEAKKKLLKDVEALSQRL 1439
Cdd:TIGR01612 950 NIDTI-------KESNLIE----------KSYKDK---FDNTLIDKINELDKAFkdASLNDYEAKNNELIKYFNDLKANL 1009
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1440 ---EEKVL--AYDKLEKTKNRLQQELDDLTVDLDH-QRQIVSNLEKKQKKFDQLLAeeKGISARYAEERDRAEA------ 1507
Cdd:TIGR01612 1010 gknKENMLyhQFDEKEKATNDIEQKIEDANKNIPNiEIAIHTSIYNIIDEIEKEIG--KNIELLNKEILEEAEInitnfn 1087
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1508 EAREKetkaLSLARALEEALEAKEEFERQNKQLRADMEDLmssKDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQ 1587
Cdd:TIGR01612 1088 EIKEK----LKHYNFDDFGKEENIKYADEINKIKDDIKNL---DQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVAD 1160
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1588 AT---EDAKlRLEVNMQAMKAQFERDLQTRDEQNEekkrlLLKQVRELEAELEDERKQRALAVA---------------S 1649
Cdd:TIGR01612 1161 KAisnDDPE-EIEKKIENIVTKIDKKKNIYDEIKK-----LLNEIAEIEKDKTSLEEVKGINLSygknlgklflekideE 1234
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1650 KKKMEIDLKDLEAQIEAAnkarDEVIKQLRKLQAQM---KDYQRELEEARASRDE-----IFAQSKES------EKKLK- 1714
Cdd:TIGR01612 1235 KKKSEHMIKAMEAYIEDL----DEIKEKSPEIENEMgieMDIKAEMETFNISHDDdkdhhIISKKHDEnisdirEKSLKi 1310
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1715 ----SLEAEILQLQEELASSERARRHAEQERDELADEIAN-----SASGKSALLDEKRRLEARIAQLEEELEEEQSNMEL 1785
Cdd:TIGR01612 1311 iedfSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEK 1390
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1786 LNDRFR------------KTTL----------QVDTLNTELAAERSaaqKSDNARQQLERQNKELKAKLQELEGA----- 1838
Cdd:TIGR01612 1391 LIKKIKddinleeckskiESTLddkdidecikKIKELKNHILSEES---NIDTYFKNADENNENVLLLFKNIEMAdnksq 1467
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1839 --VKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKlKEIFMQVEDE-------------RRHADQYKEQM 1903
Cdd:TIGR01612 1468 hiLKIKKDNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKN-KELFEQYKKDvtellnkysalaiKNKFAKTKKDS 1546
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1904 EKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANE-------GLSREVSTLKNRLRRGGPISFSSSRSGRRQ 1976
Cdd:TIGR01612 1547 EIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDksnkaaiDIQLSLENFENKFLKISDIKKKINDCLKET 1626
|
1130 1140
....*....|....*....|....
gi 1907083610 1977 LHIEGASLELSDDDTESKTSDVND 2000
Cdd:TIGR01612 1627 ESIEKKISSFSIDSQDTELKENGD 1650
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1268-1516 |
1.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1268 ACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQ 1347
Cdd:COG3883 1 ALALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1348 LQDTQELLQEETRQKLNLSSRIRQLEEEKNSlqeqqeeeeearKNLE---KQVLALQSQLADTKKKVDDDLGTIESLEEA 1424
Cdd:COG3883 81 IEERREELGERARALYRSGGSVSYLDVLLGS------------ESFSdflDRLSALSKIADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1425 KKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQLLAEEKGISARYAEERDR 1504
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|..
gi 1907083610 1505 AEAEAREKETKA 1516
Cdd:COG3883 229 AAAAAAAAAAAA 240
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1618-1954 |
1.61e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1618 NEEKKRLLLKQVRELEAELEDERKQRALAVASKKKMEIDL-------KDLEAQIEAANKARDEVIKQLRkLQAQMKDYQR 1690
Cdd:COG3096 276 HANERRELSERALELRRELFGARRQLAEEQYRLVEMARELeelsareSDLEQDYQAASDHLNLVQTALR-QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1691 ELEEArasrdeifaqskesEKKLKSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAria 1770
Cdd:COG3096 355 DLEEL--------------TERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSL----------KSQLADYQQALDV--- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1771 QLEEELEEEQSNMELLNDRfrkTTLQVDTLNTELAAERSAAQKSDnaRQQLERQNKELKAKLQeLEGAVKSKFKATISAL 1850
Cdd:COG3096 408 QQTRAIQYQQAVQALEKAR---ALCGLPDLTPENAEDYLAAFRAK--EQQATEEVLELEQKLS-VADAARRQFEKAYELV 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1851 EAKIGQLE-EQLEQEAKEraaanklVRRTEKKLKEIFMQVEDERRhadQYKEqMEKANARMKQLKRQLEEAEEEATRANA 1929
Cdd:COG3096 482 CKIAGEVErSQAWQTARE-------LLRRYRSQQALAQRLQQLRA---QLAE-LEQRLRQQQNAERLLEEFCQRIGQQLD 550
|
330 340
....*....|....*....|....*
gi 1907083610 1930 SRRKLQRELDDATEANEGLSREVST 1954
Cdd:COG3096 551 AAEELEELLAELEAQLEELEEQAAE 575
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
998-1171 |
1.66e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 998 QKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLE------ 1071
Cdd:COG3883 33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgse 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1072 --------------------ERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGD 1131
Cdd:COG3883 113 sfsdfldrlsalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907083610 1132 DETLHKNNALKVARELQAQIAELQEDFESEKASRNKAEKQ 1171
Cdd:COG3883 193 AAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
877-1108 |
1.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQaetELFAEAEEMRARLAAKKQELEEILH 956
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID---KLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 957 D--------------LESR-----VEEEEERNQILQNEKKKMQAHIQdleeqldeeegARQKLQLEKVTAEAKIKKMEEE 1017
Cdd:COG3883 94 AlyrsggsvsyldvlLGSEsfsdfLDRLSALSKIADADADLLEELKA-----------DKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1018 VLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTD 1097
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250
....*....|.
gi 1907083610 1098 LQDQIAELQAQ 1108
Cdd:COG3883 243 AASAAGAGAAG 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1686-1884 |
1.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1686 KDYQRELEEARASRDEIFAQSK---ESEKKLKSLEAeilqlQEELassERARRHAEQERDELADEIAnsasgksalldek 1762
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKkeaEAIKKEALLEA-----KEEI---HKLRNEFEKELRERRNELQ------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1763 rRLEARIAQLEeeleeeqsnmELLNDRFRkttlQVDTLNTELaaersaaqksDNARQQLERQNKELKAKLQELEGAVKSK 1842
Cdd:PRK12704 86 -KLEKRLLQKE----------ENLDRKLE----LLEKREEEL----------EKKEKELEQKQQELEKKEEELEELIEEQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907083610 1843 FKA--TISAL---EAKiGQLEEQLEQEAKERAAanKLVRRTEKKLKE 1884
Cdd:PRK12704 141 LQEleRISGLtaeEAK-EILLEKVEEEARHEAA--VLIKEIEEEAKE 184
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1148-1513 |
1.91e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1148 QAQIAELQEDFESEKASRNKAEKQKRDLSEELEalkteledtldttaaqqelrtkREQEVAELKKALEDETkNHEAQIQD 1227
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----------------------RRRKLEEAEKARQAEM-DRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1228 MRQRHATALEELSEQLEQAKRfKANLEKNKQgletdnKELACEVKVLQQVKAESEHKRKKLDAQVQELHA----KVSEGD 1303
Cdd:pfam17380 338 EQERMAMERERELERIRQEER-KRELERIRQ------EEIAMEISRMRELERLQMERQQKNERVRQELEAarkvKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1304 RLRvelaeKANKLQNELDNVSTLLEEAEKKGIKFakdaagLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNslqeqq 1383
Cdd:pfam17380 411 RQR-----KIQQQKVEMEQIRAEQEEARQREVRR------LEEERAREMERVRLEEQERQQQVERLRQQEEERK------ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1384 eeeeeaRKNLEKQVLALQSQLADtkkkvdddlgtieslEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKNRLQQELDDl 1463
Cdd:pfam17380 474 ------RKKLELEKEKRDRKRAE---------------EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE- 531
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1464 tvdlDHQRQIVSNLEKKQKKFDQLLAEEKGISaRYAEERDRAEAEAREKE 1513
Cdd:pfam17380 532 ----EERRREAEEERRKQQEMEERRRIQEQMR-KATEERSRLEAMERERE 576
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1628-1765 |
2.00e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1628 QVRELEAELEDERKQRALAVASKKKMEIdlkdLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEAR---------AS 1698
Cdd:pfam00529 59 ALDSAEAQLAKAQAQVARLQAELDRLQA----LESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQidlarrrvlAP 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1699 RDEIFAQSKESEKKL-KSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRL 1765
Cdd:pfam00529 135 IGGISRESLVTAGALvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1674-1917 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1674 VIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEE----LASSERARRHAE---QERDELAD 1746
Cdd:pfam06008 10 ALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKatqtLAKAQQVNAESErtlGHAKELAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1747 EIANSASGKSALLDEKRRL-----EARIAQLEEELEEEQSNMELLNDRFRKTTLQVDTlntelaAERSAAQKSDNarqQL 1821
Cdd:pfam06008 90 AIKNLIDNIKEINEKVATLgendfALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAE------AELKAAQDLLS---RI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1822 ERQNKELKAKLQELEGAVKSKfkatISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKE 1901
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDS----LAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEE 236
|
250
....*....|....*.
gi 1907083610 1902 QMEKANARMKQLKRQL 1917
Cdd:pfam06008 237 TLKTARDSLDAANLLL 252
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
997-1241 |
2.20e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 42.86 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 997 RQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKE--KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERL 1074
Cdd:COG5391 306 FEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVfaKRLEQNQNSILNEGVVQAETLRSSLKELLTQLQDEIKSRESLI 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1075 KkeekTRQELEKAKrkldgettdlqdqiAELQAQVDELKVQLTKKEEElqgalargDDETLHKNNALKVARELQAQIAE- 1153
Cdd:COG5391 386 L----TDSNLEKLT--------------DQNLEDVEELSRSLRKNSSQ--------RAVVSQQPEGLTSFSKLSYKLRDf 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1154 LQEDFESEKasRNKAEKQKRDLSEELEALKTELEDTldTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHA 1233
Cdd:COG5391 440 VQEKSRSKS--IESLQQDKEKLEEQLAIAEKDAQEI--NEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWK 515
|
....*...
gi 1907083610 1234 TALEELSE 1241
Cdd:COG5391 516 SVKEQLDR 523
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1075-1454 |
2.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1075 KKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkvarELQAQIAEL 1154
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELE---------------------QAREELEQL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1155 QEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKK---ALEDETKNHEAQIQDMRQR 1231
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKerqDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1232 HATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAE 1311
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1312 KANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARK 1391
Cdd:COG4372 225 DSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1392 NLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKLLKDVEALSQRLEEKVLAYDKLEKTKN 1454
Cdd:COG4372 305 AALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1098-1362 |
2.28e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1098 LQDQIAELQAQVDELKVQLTKKEEELQgalargddetLHKNNaLKVARELQAQ-IAELQEDFESEKASRNKAEKQKRDLS 1176
Cdd:PHA02562 172 NKDKIRELNQQIQTLDMKIDHIQQQIK----------TYNKN-IEEQRKKNGEnIARKQNKYDELVEEAKTIKAEIEELT 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1177 EELEALKTELEdtlDTTAAQQELRTKReqevAELKKALEDETKNHEaqiqdMRQRHA---TALEELSEQLEQakrfkanL 1253
Cdd:PHA02562 241 DELLNLVMDIE---DPSAALNKLNTAA----AKIKSKIEQFQKVIK-----MYEKGGvcpTCTQQISEGPDR-------I 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1254 EKNKQGLetdnkelacevkvlqqvkAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTL------- 1326
Cdd:PHA02562 302 TKIKDKL------------------KELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLvdkakkv 363
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907083610 1327 ---LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQK 1362
Cdd:PHA02562 364 kaaIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1061-1336 |
2.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1061 NKQEVMISDLEERLKKEEKTRQELEKAKRKLDG---ETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHK 1137
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDElneELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1138 NNALKVARELQAQIAELQEdfesEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTK---REQEVAELKKAL 1214
Cdd:COG1340 81 DELNEKLNELREELDELRK----ELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKikeLEKELEKAKKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1215 EDETKNHE--AQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKElacevkvlqqvkaesehkRKKLDAQV 1292
Cdd:COG1340 157 EKNEKLKElrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKE------------------ADELHKEI 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083610 1293 QELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIK 1336
Cdd:COG1340 219 VEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1653-1815 |
2.38e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.41 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1653 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQ---RELEEARASRDEIFAQSKESEKKLKSLEAEILQLQEELAs 1729
Cdd:pfam00529 49 FQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQaleSELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1730 seRARRHAEQE---RDELADEIANSASGKSALLDEKRRLEariAQLEEELEEEQSNMELLNDRFRKTTLQVDTLNTELAA 1806
Cdd:pfam00529 128 --RRRVLAPIGgisRESLVTAGALVAQAQANLLATVAQLD---QIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
....*....
gi 1907083610 1807 ERSAAQKSD 1815
Cdd:pfam00529 203 AKLDLERTE 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1573-1959 |
2.40e-03 |
|
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: 43.09 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1573 EEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFerdlqTRDEQNEEKKRLLLKQVRELEAELEDERKQRALAVASKKK 1652
Cdd:TIGR04523 162 NDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKL-----LKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEK 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1653 MEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARAsrdeifaQSKESEKKLKSLEAEILQLQEElasser 1732
Cdd:TIGR04523 237 KQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK-------KIKELEKQLNQLKSEISDLNNQ------ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1733 arrhAEQERD-ELADEIANSAsgksallDEKRRLEARIAQLeeeleeeQSNMELLNDRFRKTTLQVDTLNTELAAERSAA 1811
Cdd:TIGR04523 304 ----KEQDWNkELKSELKNQE-------KKLEEIQNQISQN-------NKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1812 QKSDNARQQLERQNKELKAKLQELEGAvKSKFKATISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKLKEIFMQVED 1891
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQ-INDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907083610 1892 ERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSREVSTLKNRL 1959
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1346-1605 |
2.97e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1346 SQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAK 1425
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1426 KKLLKDVEALSQRLEEKVLAYDKLEKTK---NRLQQELDDL-------TVDLDHQRQIVSNLEKKQKKFDQLLAEEKG-- 1493
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLewrqqteVLSPEEEKELVEKIKELEKELEKAKKALEKne 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1494 ----ISARYAEERDRAEAEAREKETkalsLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKRALE 1569
Cdd:COG1340 161 klkeLRAELKELRKEAEEIHKKIKE----LAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 1907083610 1570 QQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKA 1605
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1812-1960 |
3.01e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1812 QKSDNARQQLERQNKELKAKLQELEGAVkSKFKA---------TISALEAKIGQLEEQLEQEAKERAAANKLVRRTEKKL 1882
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAAL-EEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1883 KEIFMQVEDERRHAdqykeQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEA-NEGLSREVSTLKNRLR 1960
Cdd:COG3206 250 GSGPDALPELLQSP-----VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQlQQEAQRILASLEAELE 323
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1545-1695 |
3.20e-03 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 42.44 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1545 EDLMSSKD-DVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLRLEVNMQAMKAQFERDLQT---------- 1613
Cdd:COG1193 506 RELLGEESiDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEKEEILEKAREEAEEilrearkeae 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1614 ------RDEQNEEKK-RLLLKQVRELEAELEDERKQRA-----------------------------LAVASKK------ 1651
Cdd:COG1193 586 elirelREAQAEEEElKEARKKLEELKQELEEKLEKPKkkakpakppeelkvgdrvrvlslgqkgevLEIPKGGeaevqv 665
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1652 ---KMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQREL-------EEA 1695
Cdd:COG1193 666 gilKMTVKLSDLEKVEKKKPKKPKKRPAGVSVSVSKASTVSPELdlrgmrvEEA 719
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1002-1129 |
3.21e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1002 LEKVTAEAKIKKMEEEVllledqnSKFIKE-KKLMEDRIAECSSQLAEEEEKAKNLA----KIRNKQevmISDLEERLK- 1075
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEA-------KRILEEaKKEAEAIKKEALLEAKEEIHKLRNEFekelRERRNE---LQKLEKRLLq 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1076 KEEKTRQELEKAKRKlDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALAR 1129
Cdd:PRK12704 94 KEENLDRKLELLEKR-EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
867-975 |
3.22e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 867 RVFTKVKPLLQVTRQEEELQAKDEELlkVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAA 946
Cdd:COG0542 405 EIDSKPEELDELERRLEQLEIEKEAL--KKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQ 482
|
90 100
....*....|....*....|....*....
gi 1907083610 947 KKQELEEILHDLESRVEEEEERNQILQNE 975
Cdd:COG0542 483 RYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
877-1029 |
3.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEellkVKEKQTKVEGELEEMERKHQQ----LLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELE 952
Cdd:PRK12704 52 EAIKKEALLEAKEE----IHKLRNEFEKELRERRNELQKlekrLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 953 EILHDLEsrveeeeernQILQNEKKKMQaHIQDLEEQLdeeegARQKLqLEKVTAEAK------IKKMEEEVLLLEDQNS 1026
Cdd:PRK12704 128 KKEEELE----------ELIEEQLQELE-RISGLTAEE-----AKEIL-LEKVEEEARheaavlIKEIEEEAKEEADKKA 190
|
...
gi 1907083610 1027 KFI 1029
Cdd:PRK12704 191 KEI 193
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1551-1726 |
3.34e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1551 KDDVGKNVHELEKSKRALEQQVEEMRTQLEELEDELQATEdaklrlevnmqamkaQFERDLQTRDEQNEEKKrlllkqvR 1630
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAE---------------KLKEELEEKKEKLQEEE-------D 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1631 ELEAELEDERKQRalavaskkkmeidlkdleaqIEAANKARDEVIKQLRKLQAQMKDYQ--RELEEARASRDEIfAQSKE 1708
Cdd:PRK00409 566 KLLEEAEKEAQQA--------------------IKEAKKEADEIIKELRQLQKGGYASVkaHELIEARKRLNKA-NEKKE 624
|
170
....*....|....*...
gi 1907083610 1709 SEKKLKSLEAEILQLQEE 1726
Cdd:PRK00409 625 KKKKKQKEKQEELKVGDE 642
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1190-1463 |
3.36e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 42.37 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1190 LDTTAAQQELRTK-RE--QEVAELKKALEdETKNHEAQIQDMRQRHATALEELS---------EQLEQAKRFKANLEKNK 1257
Cdd:COG0497 147 LDAFAGLEELLEEyREayRAWRALKKELE-ELRADEAERARELDLLRFQLEELEaaalqpgeeEELEEERRRLSNAEKLR 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1258 QGLETDNKELA-CEVKVLQQV-KAESE-HKRKKLDAQVQELHAKVSEgdrLRVELAEKANKLQNELDNVSTlleeaekkg 1334
Cdd:COG0497 226 EALQEALEALSgGEGGALDLLgQALRAlERLAEYDPSLAELAERLES---ALIELEEAASELRRYLDSLEF--------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1335 ikfakdaaglesqlqDTQELlqEETRQKLNLssrIRQLeeeknslqeqqeeeeeARK---NLEkQVLALQSQLADTKKKV 1411
Cdd:COG0497 294 ---------------DPERL--EEVEERLAL---LRRL----------------ARKygvTVE-ELLAYAEELRAELAEL 336
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1412 DDDLGTIESLEEAKKKLLKDVEALSQRLEEK-VLAYDKLEKtknRLQQELDDL 1463
Cdd:COG0497 337 ENSDERLEELEAELAEAEAELLEAAEKLSAArKKAAKKLEK---AVTAELADL 386
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
877-1062 |
3.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLL------EEKNILAEQLQAETelFAEAEEMRARLAAKKQE 950
Cdd:COG4942 70 RIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrlGRQPPLALLLSPED--FLDAVRRLQYLKYLAPA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 951 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEqldeeegARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFIK 1030
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEE-------ERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
170 180 190
....*....|....*....|....*....|..
gi 1907083610 1031 EKKLMEDRIAECSSQLAEEEEKAKNLAKIRNK 1062
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1657-1750 |
3.63e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1657 LKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKES--EKKLKSLEAEILQLQEELAsserar 1734
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAiaRKEIKDLQKELEKLNEEYA------ 196
|
90
....*....|....*.
gi 1907083610 1735 RHAEQERDELADEIAN 1750
Cdd:cd22656 197 AKLKAKIDELKALIAD 212
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1009-1247 |
3.82e-03 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 42.45 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1009 AKIKKMEEEVLLLEDqnskFIKEKKLMEDRIAECSSQLAEEEEKAkNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1088
Cdd:pfam18971 567 AKGLSLQEANKLIKD----FLSSNKELAGKALNFNKAVAEAKSTG-NYDEVKKAQK----DLEKSLRKREHLEKEVEKKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1089 RKLDGETTDLQDQiAELQAQVDELKVQLTKKEEELQGALArgddetlHKNNALKVARELQAQIAELQEDFESEKAS---- 1164
Cdd:pfam18971 638 ESKSGNKNKMEAK-AQANSQKDEIFALINKEANRDARAIA-------YTQNLKGIKRELSDKLEKISKDLKDFSKSfdef 709
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1165 RNKAEKQKRDLSEELEALKTELED----------TLDTTAAQQELRTKREQEVAELKKALEDetknHEAQIQD--MRQRH 1232
Cdd:pfam18971 710 KNGKNKDFSKAEETLKALKGSVKDlginpewiskVENLNAALNEFKNGKNKDFSKVTQAKSD----LENSVKDviINQKV 785
|
250
....*....|....*
gi 1907083610 1233 ATALEELSEQLEQAK 1247
Cdd:pfam18971 786 TDKVDNLNQAVSVAK 800
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
997-1255 |
3.84e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 997 RQKlQLEKVTAEAKIKKMEEEVLLLEDQNSKFIKEKKlMEDRIAECssqlaEEEEKAKNLAKI-RNKQEVMISDLEERLK 1075
Cdd:pfam02029 85 RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEK-RDSRLGRY-----KEEETEIREKEYqENKWSTEVRQAEEEGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1076 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARGDDETLHKNNALKVARELQAQIAELQ 1155
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQERE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1156 EDFESEKASRNKAEKQKRDL----SEELEALKTEledtldttaaQQElrtkREQEVAELKKALEDETKNHEAQIQDMRQr 1231
Cdd:pfam02029 238 EEAEVFLEAEQKLEELRRRRqekeSEEFEKLRQK----------QQE----AELELEELKKKREERRKLLEEEEQRRKQ- 302
|
250 260
....*....|....*....|....
gi 1907083610 1232 hATALEELSEQlEQAKRFKANLEK 1255
Cdd:pfam02029 303 -EEAERKLREE-EEKRRMKEEIER 324
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1648-1749 |
4.34e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1648 ASKKKMEID-----LKDLEAQIEAANKARDEVIK-----------QLRKLQAQMKDYQRELEEARASRDEIFAQSKESEK 1711
Cdd:COG0542 399 AARVRMEIDskpeeLDELERRLEQLEIEKEALKKeqdeasferlaELRDELAELEEELEALKARWEAEKELIEEIQELKE 478
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907083610 1712 KLKSLEAEILQLQEELAS-SERARRHAEQERDEL-ADEIA 1749
Cdd:COG0542 479 ELEQRYGKIPELEKELAElEEELAELAPLLREEVtEEDIA 518
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
878-1241 |
4.41e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 878 VTRQEEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETELFAEAEEMRARLAAKKQELeeilHD 957
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEN----SS 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 958 LESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEV------LLLEDQNSKFIKE 1031
Cdd:pfam05557 302 LTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILesydkeLTMSNYSPQLLER 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1032 KKLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKeeKTRQELEKAKRKLDGETTDLQDQIAELQAQVDE 1111
Cdd:pfam05557 382 IEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQA--LRQQESLADPSYSKEEVDSLRRKLETLELERQR 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1112 LKVQLTKKEEELQGALARGDDET-------LHKNNALKVARELQAQIAELQEDFESekasrnkaekqkrdLSEELEALKT 1184
Cdd:pfam05557 460 LREQKNELEMELERRCLQGDYDPkktkvlhLSMNPAAEAYQQRKNQLEKLQAEIER--------------LKRLLKKLED 525
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1185 ELEDTLdttAAQQELRTKREQEVAELKKALEDEtknhEAQIQDMRQRHATALEELSE 1241
Cdd:pfam05557 526 DLEQVL---RLPETTSTMNFKEVLDLRKELESA----ELKNQRLKEVFQAKIQEFRD 575
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1248-1513 |
4.47e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1248 RFKANLEKNKQgLETDNKELACEVKVLQQVK-AESEHKRKKLDAQVQELHAKVsegdrlrVELAEKANKLQNELDNVSTL 1326
Cdd:pfam00038 12 RLASYIDKVRF-LEQQNKLLETKISELRQKKgAEPSRLYSLYEKEIEDLRRQL-------DTLTVERARLQLELDNLRLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1327 LEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLqeqqeeeeeaRKNLEKQVLALQSQLAD 1406
Cdd:pfam00038 84 AEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFL----------KKNHEEEVRELQAQVSD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1407 TKKKVD------DDLGTI-----ESLEEAKKKLLKDVEAL-SQRLEEKVLAYDK----LEKTKNRLQQ---ELDDLTVDL 1467
Cdd:pfam00038 154 TQVNVEmdaarkLDLTSAlaeirAQYEEIAAKNREEAEEWyQSKLEELQQAAARngdaLRSAKEEITElrrTIQSLEIEL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907083610 1468 DHQRQIVSNLEKKqkkfdqlLAEEKgisARYAEERDRAEAEAREKE 1513
Cdd:pfam00038 234 QSLKKQKASLERQ-------LAETE---ERYELQLADYQELISELE 269
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1437-1904 |
4.82e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1437 QRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNLEKKQKKFDQL---LAEEKGISARYAEERDRAEAEAREKE 1513
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIkkqIADDEKSHSITLKEIERLSIEYNNAM 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1514 TKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKDDVGKNVHELEKSKR-----------------ALEQQVEEMR 1576
Cdd:PRK01156 232 DDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiindpvyknrnyindyfKYKNDIENKK 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1577 TQLEELEDELQATEDAKLRLEVnMQAMKAQFERDLQTRDEQNEEKKRL---------LLKQVRELEAELEDERKQRALAV 1647
Cdd:PRK01156 312 QILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELegyemdynsYLKSIESLKKKIEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1648 ASKKKMeidLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIfaqskesEKKLKSLEAEIL------ 1721
Cdd:PRK01156 391 AFISEI---LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL-------SRNMEMLNGQSVcpvcgt 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1722 QLQEElaSSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARiaqleeELEEEQSNMELLNDRFRKTTLQVDTLN 1801
Cdd:PRK01156 461 TLGEE--KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKR------KEYLESEEINKSINEYNKIESARADLE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1802 TELAAERSAAQKSDNARQQLERQNKelkAKLQELEGAVKSKFKATISALEAKIGQLEEQLEQeakeraaANKLVRRTEKK 1881
Cdd:PRK01156 533 DIKIKINELKDKHDKYEEIKNRYKS---LKLEDLDSKRTSWLNALAVISLIDIETNRSRSNE-------IKKQLNDLESR 602
|
490 500
....*....|....*....|...
gi 1907083610 1882 LKEIFMQVEDERRHADQYKEQME 1904
Cdd:PRK01156 603 LQEIEIGFPDDKSYIDKSIREIE 625
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1107-1225 |
5.27e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1107 AQVDELKVQLTKKEEELQgALARGDDETLHKNnalkvARELQAQIAELQEDFESEKAsRNKAEKQkrdLSEELEALKTEL 1186
Cdd:COG0542 411 EELDELERRLEQLEIEKE-ALKKEQDEASFER-----LAELRDELAELEEELEALKA-RWEAEKE---LIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1907083610 1187 EDTLDTTAAQQELRTKREQEVAELKKALEDE-TKNHEAQI 1225
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREEvTEEDIAEV 520
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1560-1768 |
5.30e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 41.75 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELEdeLQATEDAKLRLEVNMQAMKAQFERDLQTRDEQNEEKKRL------LLKQVRELE 1633
Cdd:PRK04778 253 DIEKEIQDLKEQIDENLALLEELD--LDEAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLpdflehAKEQNKELK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1634 AELEderkqralavASKKKMEIDLKDLEAQieaankarDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKESEKKL 1713
Cdd:PRK04778 331 EEID----------RVKQSYTLNESELESV--------RQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1714 KSLEAEILQLQEELASSERARRHAEQERDELadeiansasgKSALLDEKRRLEAR 1768
Cdd:PRK04778 393 EEIEKEQEKLSEMLQGLRKDELEAREKLERY----------RNKLHEIKRYLEKS 437
|
|
| Prefoldin_4 |
cd23165 |
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic ... |
1076-1119 |
5.35e-03 |
|
prefoldin subunit 4; Prefoldin subunit 4 is one of the beta subunits of the eukaryotic prefoldin complex. Prefoldin is a hexameric molecular chaperone complex, found in both eukaryotes and archaea, that binds and stabilizes newly synthesized polypeptides allowing them to fold correctly. The complex contains two alpha and four beta subunits, the two subunits being evolutionarily related. In archaea, there is usually only one gene for each subunit while in eukaryotes there two or more paralogous genes encoding each subunit adding heterogeneity to the structure of the hexamer. The structure of the complex consists of a double beta barrel assembly with six protruding coiled-coils.
Pssm-ID: 467481 [Multi-domain] Cd Length: 103 Bit Score: 38.29 E-value: 5.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1907083610 1076 KEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKK 1119
Cdd:cd23165 60 SLEEAQERLEKAKEELEEEIEKLEEEIDEIEEEMKELKVQLYAK 103
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1054-1409 |
5.37e-03 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 41.92 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1054 KNLAKIRNKQEVMISDLEERLKKE--EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvqltKKEEELQGALARGD 1131
Cdd:NF033838 91 KKLSDIKTEYLYELNVLKEKSEAEltSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAE----KKAKDQKEEDRRNY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1132 DETLHKNNALKVAR-ELQAQIAELQEDFESEKASRNKAE-KQKRDLSEELEALKTELEDtLDTTAAQQELRTKREQEvAE 1209
Cdd:NF033838 167 PTNTYKTLELEIAEsDVEVKKAELELVKEEAKEPRDEEKiKQAKAKVESKKAEATRLEK-IKTDREKAEEEAKRRAD-AK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1210 LKKALEDETKNHEAQIQDMRQRHAtALEELSEqlEQAKRFKANLEKNKQGLET--------DNKELACEVKVLQQVKAES 1281
Cdd:NF033838 245 LKEAVEKNVATSEQDKPKRRAKRG-VLGEPAT--PDKKENDAKSSDSSVGEETlpspslkpEKKVAEAEKKVEEAKKKAK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1282 EHKR-----------KKLDAQVQELHAKVSEGDrlrVELA-EKANKLQNElDNVSTLLEEAEKKgikfAKDAAGLESQLQ 1349
Cdd:NF033838 322 DQKEedrrnyptntyKTLELEIAESDVKVKEAE---LELVkEEAKEPRNE-EKIKQAKAKVESK----KAEATRLEKIKT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1350 DTQELlQEETRQKLNLSSRIRQLEEEK-------------------------NSLQEQQEEEEEARKNLEKQVLALQSQL 1404
Cdd:NF033838 394 DRKKA-EEEAKRKAAEEDKVKEKPAEQpqpapapqpekpapkpekpaeqpkaEKPADQQAEEDYARRSEEEYNRLTQQQP 472
|
....*
gi 1907083610 1405 ADTKK 1409
Cdd:NF033838 473 PKTEK 477
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
1098-1289 |
5.78e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 40.49 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1098 LQDQIAELQAQVDELKVQLTKKEEELQGALARGDD--ETL----HKNNAL--------KVARELQAQIAELQEDFESEKA 1163
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKflENLaslkHENDNLssmlnrkeRRLKDLEDQLSELKNSYEELTE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1164 SRNKAEKQKRDLSEELEALKTELE------DTLdtTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQR---HAT 1234
Cdd:pfam17078 88 SNKQLKKRLENSSASETTLEAELErlqiqyDAL--VDSQNEYKDHYQQEINTLQESLEDLKLENEKQLENYQQRissNDK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1235 ALEELSEQLEQAKRFKANLEKNK-QGLETDNKELACEVKVLQQVKAESEHKRKKLD 1289
Cdd:pfam17078 166 DIDTKLDSYNNKFKNLDNIYVNKnNKLLTKLDSLAQLLDLPSWLNLYPESRNKILE 221
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1043-1287 |
5.84e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1043 SSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL----------------Q 1106
Cdd:pfam15905 72 SKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellkakfsedgtQ 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1107 AQVDELKVQLTKKEEEL----QGALARGDDETLHKNNALKVARELQAQIAELQE---DFESEKASRNKAEKQKRDLSEEL 1179
Cdd:pfam15905 152 KKMSSLSMELMKLRNKLeakmKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEklvSTEKEKIEEKSETEKLLEYITEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1180 EALKTELEDTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDmrqrhataLEELSEQLEQAKRFKANLEKNKQg 1259
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKD--------LNEKCKLLESEKEELLREYEEKE- 302
|
250 260
....*....|....*....|....*...
gi 1907083610 1260 lETDNKELACEVKVLQQVKAESEHKRKK 1287
Cdd:pfam15905 303 -QTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1668-1914 |
5.86e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1668 NKARDEVIKQLRKLQA-QMKDYQRE-----LEEARASRDEI------FAQSKESEKKLKSLEAEIlqlqeELASSERARR 1735
Cdd:PRK05771 15 KSYKDEVLEALHELGVvHIEDLKEElsnerLRKLRSLLTKLsealdkLRSYLPKLNPLREEKKKV-----SVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1736 HAEQERDELADEIansasgkSALLDEKRRLEARIAQLEEELEEEQ------SNMELLNDrFRKTTLQVDTLNTELAAERS 1809
Cdd:PRK05771 90 DVEEELEKIEKEI-------KELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLG-FKYVSVFVGTVPEDKLEELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1810 AAQKSDNA-----------------RQQLERQNKELK-AKLQELEGAVKSKFKATISALEAKIGQLEEQLEqeakeraaa 1871
Cdd:PRK05771 162 LESDVENVeyistdkgyvyvvvvvlKELSDEVEEELKkLGFERLELEEEGTPSELIREIKEELEEIEKERE--------- 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083610 1872 nklvrRTEKKLKEIFMQVEDERRHADQYKEQM-EKANARMKQLK 1914
Cdd:PRK05771 233 -----SLLEELKELAKKYLEELLALYEYLEIElERAEALSKFLK 271
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1070-1244 |
6.45e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 39.55 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1070 LEERLKKEEKTRQELEK-----AKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGALARgddetlhknNALKVA 1144
Cdd:pfam01442 2 LEDSLDELSTYAEELQEqlgpvAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQ---------NVEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1145 RELQAQIAELQEDFesekasRNKAEKQKRDLSEELEALKTELEDTLDTTAAQ-----QELRTKREQEVAELKKALEDETK 1219
Cdd:pfam01442 73 QRLEPYTEELRKRL------NADAEELQEKLAPYGEELRERLEQNVDALRARlapyaEELRQKLAERLEELKESLAPYAE 146
|
170 180
....*....|....*....|....*....
gi 1907083610 1220 NHEAQ----IQDMRQRHATALEELSEQLE 1244
Cdd:pfam01442 147 EVQAQlsqrLQELREKLEPQAEDLREKLD 175
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1661-1762 |
6.86e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1661 EAQIEAANKARDEvikqlrkLQAQMKDYQRELEEARASRDEIFAQSKESEKKLKslEAEILQLQEELAS-SERARRHAEQ 1739
Cdd:COG0711 37 ADGLAEAERAKEE-------AEAALAEYEEKLAEARAEAAEIIAEARKEAEAIA--EEAKAEAEAEAERiIAQAEAEIEQ 107
|
90 100
....*....|....*....|...
gi 1907083610 1740 ERDELADEIANSASGKSALLDEK 1762
Cdd:COG0711 108 ERAKALAELRAEVADLAVAIAEK 130
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1146-1449 |
6.97e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1146 ELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAELKKAledetknheaqi 1225
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1226 qdmRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVlQQVKAESEHKRKKLDAQVQELHAkvsegdrl 1305
Cdd:COG1340 80 ---RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWR-QQTEVLSPEEEKELVEKIKELEK-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1306 RVELAEKANKLQNELDNVSTLLEEAEKKgikfakdAAGLESQLQDTQELLQEETRQKLNLSSRIRQLEEEKNSLQEQQEE 1385
Cdd:COG1340 148 ELEKAKKALEKNEKLKELRAELKELRKE-------AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907083610 1386 EEEARKNLEKQVLALQSQLADTKKKVDDDLGTIESLEEAKKKllKDVEALSQRLEEKVLAYDKL 1449
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKKGEKL 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
972-1127 |
7.15e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 972 LQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEAKIKKMEEEVLLLEDQNSKFikEKKLMEDRIAECSSQLAEEEE 1051
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY--EEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907083610 1052 KAKNLAKIRNKQEVMISDLEERLKKE-EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEELQGAL 1127
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEElAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEL 176
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
913-1122 |
7.26e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 913 HQQLLEEKNILAEQLQAE-----TELFAEAEEMRARLAAKKQELEEILHDLESRVEEEEERNQILQNEKKKMQahiqdle 987
Cdd:PHA02562 200 YNKNIEEQRKKNGENIARkqnkyDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE------- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 988 eqldeeegarqklQLEKV-----------TAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNL 1056
Cdd:PHA02562 273 -------------QFQKVikmyekggvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKL 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907083610 1057 AKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKVQLTKKEEE 1122
Cdd:PHA02562 340 LELKNK----ISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
871-1111 |
7.28e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 871 KVKPLLQVTRQEEELQAKDEELLKVK------------------EKQTKVEGELEEMERKHQQLLEEKNILAEQLQAETE 932
Cdd:PRK03918 474 KERKLRKELRELEKVLKKESELIKLKelaeqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 933 LFAEAEEMRARLAAKKQELEEILHDLESR----VEEEEERNQILQ----------NEKKKMQAHIQDLEEQLDEEEGARQ 998
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneylelkDAEKELEREEKELKKLEEELDKAFE 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 999 KLQLekvtAEAKIKKMEEEvllLEDQNSKFIKEK-KLMEDRIAECSSQLAEEEEKAKNLAKIRNKQEVMISDLEERLKKE 1077
Cdd:PRK03918 634 ELAE----TEKRLEELRKE---LEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
250 260 270
....*....|....*....|....*....|....
gi 1907083610 1078 EKTRQELEKAKRKLDgETTDLQDQIAELQAQVDE 1111
Cdd:PRK03918 707 EKAKKELEKLEKALE-RVEELREKVKKYKALLKE 739
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1208-1479 |
7.57e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1208 AELKKALEDETK--NHEAQIQDMRQRHATaleelsEQLEQAKRFKANLEKnKQGLETDNKELacevKVLQQVKAESEHKr 1285
Cdd:PHA02562 166 SEMDKLNKDKIRelNQQIQTLDMKIDHIQ------QQIKTYNKNIEEQRK-KNGENIARKQN----KYDELVEEAKTIK- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1286 kkldAQVQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKgIKFAKDAA---GLESQLQDTQELLQEETRQK 1362
Cdd:PHA02562 234 ----AEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGvcpTCTQQISEGPDRITKIKDKL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1363 LNLSSRIRQLEEEKNSLQEQQEEEEEARKNLekqvLALQSQLADTKkkvdddlGTIESLEEAkkklLKDVEALSQRLEEK 1442
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIMDEFNEQSKKL----LELKNKISTNK-------QSLITLVDK----AKKVKAAIEELQAE 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1907083610 1443 VLAYDK-LEKtknrLQQELDDLTVDLD------HQRQIVSNLEK 1479
Cdd:PHA02562 374 FVDNAEeLAK----LQDELDKIVKTKSelvkekYHRGIVTDLLK 413
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1712-1961 |
7.61e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1712 KLKSLEAEILQLQEELASSERARRHAEQERDELADEIANSASGKSALLDEKRRLEARIAQLEEELEEEQSNMELLNDRFR 1791
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1792 KTTLQVDTLNTELAAERSAAQKSDNARQQLERQNKELKAKLQELEGAVKSKFKATisALEAKIGQLEEQLEqEAKERAAA 1871
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEK--ELVEKIKELEKELE-KAKKALEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1872 NKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDATEANEGLSRE 1951
Cdd:COG1340 159 NEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|
gi 1907083610 1952 VSTLKNRLRR 1961
Cdd:COG1340 239 LRELRKELKK 248
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
888-1105 |
8.03e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 888 KDEELLKVKEKQTKVEGELEEMErkhqQLLEEKNILAEQLQAETelFAEAEEMRarlaakkQELEEILHDLESRVEEEEE 967
Cdd:PRK05771 41 SNERLRKLRSLLTKLSEALDKLR----SYLPKLNPLREEKKKVS--VKSLEELI-------KDVEEELEKIEKEIKELEE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 968 RNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQNSKFIKEKKLME---------- 1036
Cdd:PRK05771 108 EISELENEIKELEQEIERLEPWGNFDLDLSLLLGFKYVSVFVgTVPEDKLEELKLESDVENVEYISTDKGyvyvvvvvlk 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907083610 1037 DRIAECSSQLAEEEEKAKNLAKIRNKQEVmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQIAEL 1105
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEEEGTPSEL-IREIKEELEEIEKERESLLEELKELAKKYLEELLALYEY 255
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1412-1952 |
8.19e-03 |
|
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: 41.25 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1412 DDDLGTIESLEEAKKKLLKDVEALSQ--------------RLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVSNL 1477
Cdd:pfam05483 67 DSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkqkenKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1478 EKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKETKALSLARALEEALEAKEEFERQNKQLRADMEdlMSSKDDVGKN 1557
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMH--FKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1558 VHELEKSKRAL---EQQVEEMRTQLEELEDELQateDAKLRLEVNMQAMKaQFERDLQTRDEQNEEkkrlLLKQVRELEA 1634
Cdd:pfam05483 225 QHLEEEYKKEIndkEKQVSLLLIQITEKENKMK---DLTFLLEESRDKAN-QLEEKTKLQDENLKE----LIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1635 ELEDERKQRALAVASKKKMEIDLKDLEAQIEAANKARDEVIKQLRKLQAQMKDYQRELEEARASRDEIFAQSKE----SE 1710
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrlekNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1711 KKLKSLEAEILQLQEELASSERARRHAEQERDELADEIANsasgKSALLDEKRRLEaRIAQLEEELEeeQSNMELLNDRF 1790
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE----DEKLLDEKKQFE-KIAEELKGKE--QELIFLLQARE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1791 RkttlQVDTLNTELAAERSAaqksdnaRQQLERQNKELKAKLQelegavKSKFKAT-ISALEAKIGQLEEQLEQEA---- 1865
Cdd:pfam05483 450 K----EIHDLEIQLTAIKTS-------EEHYLKEVEDLKTELE------KEKLKNIeLTAHCDKLLLENKELTQEAsdmt 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1866 ----KERAAANKLVRRTEKKLKEIFMQVEDERRHADQYKEQMEKANARMKQLKRQLEEAEEEATRANASRRKLQRELDDA 1941
Cdd:pfam05483 513 lelkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKIL 592
|
570
....*....|.
gi 1907083610 1942 TEANEGLSREV 1952
Cdd:pfam05483 593 ENKCNNLKKQI 603
|
|
| Taf7 |
COG5414 |
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation ... |
1477-1669 |
8.27e-03 |
|
TATA-binding protein-associated factor Taf7, part of the TFIID transcription initiation complex [Transcription];
Pssm-ID: 227701 Cd Length: 392 Bit Score: 40.84 E-value: 8.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1477 LEKKQKKFDQLLAEEKGISARYAEERDRAEAeAREKETKALSLARALEEALEAKEEFERQNKQLRADMEDLMSSKD-DVG 1555
Cdd:COG5414 202 IEEVEKKVDDLLEKDMKAESVSVVLKDEKEL-ARQERVSSWENFKEEPGEPLSRPALKKEKQGAEEEGEEGMSEEDlDVG 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1556 KNVHELEKSKRALEQQVEEMRTQLEELEDELQATEDAKLrlevnmqamkaQFERDLQTRDEQNEEKKRLLLKQVRELEAE 1635
Cdd:COG5414 281 AAEIENKEVSEGDKEQQQEEVENAEAHKEEVQSDRPDEI-----------GEEKEEDDENEENERHTELLADELNELEKG 349
|
170 180 190
....*....|....*....|....*....|....*.
gi 1907083610 1636 LEDERKQ--RALAVASKKKMEIDLKDLEAQIEAANK 1669
Cdd:COG5414 350 IEEKRRQmeSATNPILQKRFESQLNVLLKELELKRK 385
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1102-1254 |
8.36e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVQLTKKEEELQGALARGDD-ETLHKNNALkvareLQAQIAELQEDFESEKASRNKAEKQKRDLSEELE 1180
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRlQALESELAI-----SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1181 ALKTELED------TLDTT-AAQQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANL 1253
Cdd:pfam00529 128 RRRVLAPIggisreSLVTAgALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDL 207
|
.
gi 1907083610 1254 E 1254
Cdd:pfam00529 208 E 208
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
881-1088 |
8.49e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.09 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 881 QEEELQAKDEELLKVKEKQTKVEGELEEMERKHQ-QLLEEKNILAEQLQAETELFAE--AEEMRARlaakKQELEEilhd 957
Cdd:pfam15709 327 KREQEKASRDRLRAERAEMRRLEVERKRREQEEQrRLQQEQLERAEKMREELELEQQrrFEEIRLR----KQRLEE---- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 958 lESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGARQKLQLEKVTAEA-KIKKMEEEVLLLEDQnskfikeKKLM- 1035
Cdd:pfam15709 399 -ERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAeKQRQKELEMQLAEEQ-------KRLMe 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907083610 1036 --EDRIAECSSQLAEEEEKAKNLAKIRNKQEvmisDLEERLKKEEKTRQELEKAK 1088
Cdd:pfam15709 471 maEEERLEYQRQKQEAEEKARLEAEERRQKE----EEAARLALEEAMKQAQEQAR 521
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1236-1637 |
8.64e-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: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1236 LEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQQVKAESEHKRKKLDAQVQELHAKVSEGDRLRVELAEKANK 1315
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1316 LQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQELLQEETRQKlnlssriRQLEEEKNSLQEQQEEEEEARKNLEK 1395
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR-------KEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1396 QVLALQSQLADTKKKVdddlgtiesleeakkkllkdvealsQRLEEKVLAYDKLEKTKNRLQQELDDLTVDLDHQRQIVS 1475
Cdd:pfam07888 193 EFQELRNSLAQRDTQV-------------------------LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLN 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1476 NLEKKQKKFDQLLAEEKGISARYAEERDRAEAEAREKeTKALSLARALEEALEAKEEFERQNKQLRADMEdlmssKDDVG 1555
Cdd:pfam07888 248 ASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQL-TLQLADASLALREGRARWAQERETLQQSAEAD-----KDRIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1556 KNVHELEKskraLEQQVEEMRTQLEELEDELQATEDAKL----RLEVNMQAMKAQFeRDLQTRDEQNEEKKRLLLKQVRE 1631
Cdd:pfam07888 322 KLSAELQR----LEERLQEERMEREKLEVELGREKDCNRvqlsESRRELQELKASL-RVAQKEKEQLQAEKQELLEYIRQ 396
|
....*.
gi 1907083610 1632 LEAELE 1637
Cdd:pfam07888 397 LEQRLE 402
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
882-1332 |
8.71e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 40.99 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 882 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLleEKNILA-------------EQLQAETELFAEAEEMRAR---LA 945
Cdd:pfam06160 99 EEDIKQILEELDELLESEEKNREEVEELKDKYREL--RKTLLAnrfsygpaideleKQLAEIEEEFSQFEELTESgdyLE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 946 AKK--QELEEILHDLESRVEEEEERNQILQNEKKKmqahiqdleeqldeeegarqklQLEKVtaEAKIKKMEEEVLLLED 1023
Cdd:pfam06160 177 AREvlEKLEEETDALEELMEDIPPLYEELKTELPD----------------------QLEEL--KEGYREMEEEGYALEH 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1024 QNskFIKEKKLMEDRIAECSSQLA--EEEEKAKNLAKIRNKqevmISDLEERLKKEEKTRQELEKAKRKLDGETTDLQDQ 1101
Cdd:pfam06160 233 LN--VDKEIQQLEEQLEENLALLEnlELDEAEEALEEIEER----IDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1102 IAELQAQVDELKVQLTKKEEELQgalargddetlhknnalkVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEa 1181
Cdd:pfam06160 307 NKELKEELERVQQSYTLNENELE------------------RVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELE- 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1182 lktELEDTLDTTAAQQElrtkreqEVAELKKALEDEtknhEAQIQDMrqrhataLEELSEQLEQAKRFkanLEK-NKQGL 1260
Cdd:pfam06160 368 ---EILEQLEEIEEEQE-------EFKESLQSLRKD----ELEAREK-------LDEFKLELREIKRL---VEKsNLPGL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1261 ETDNKELACEVKV-LQQVKAESEHKRKKLDAQVQELHAKVSEGDRLR---------VELAEK----ANKLQNELDNVSTL 1326
Cdd:pfam06160 424 PESYLDYFFDVSDeIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYekteelidnATLAEQliqyANRYRSSNPEVAEA 503
|
....*.
gi 1907083610 1327 LEEAEK 1332
Cdd:pfam06160 504 LTEAEL 509
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1196-1407 |
8.71e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1196 QQELRTKREQEVAELKKALEDETKNHEAQIQDMRQRHATALEELSEQLEQAKRFKANLEKNKQGLETDNKELACEVKVLQ 1275
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1276 QVKAESEHKRKKLDAQ-VQELHAKVSEGDRLRVELAEKANKLQNELDNVSTLLEEAEKKGIKFAKDAAGLESQLQDTQEL 1354
Cdd:COG3883 97 RSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907083610 1355 LQEETRQKLNLSSRIRQLEEEKNSLQEQQEEEEEARKNLEKQVLALQSQLADT 1407
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
882-1125 |
8.93e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 882 EEELQAKDEELLKVKEKQTKVEGELEEMERKHQQLLEEK----NILAEQLQA-------ETELFAEAEEMRARLAAKKQE 950
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvNAGSERLRAvkdikqeRDQLLNEVKTSRNELNSLSED 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 951 LEEILHDLESRVEEEEERNQILQNEKKKMQAHIQDLEEQLDEEEGA-------RQKLQLEKVTAEAKIKKMEEEVLLLED 1023
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghamkvAMGMQKQITAKRGQIDALQSKIQFLEE 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1024 QNSKFIKEKKLMEDRIAECSSQLAEEEEKAKNLAkirNKQEVMISdlEERLKKEEKTRQELEKAKRKLdgETTDLQDQIA 1103
Cdd:pfam15921 756 AMTNANKEKHFLKEEKNKLSQELSTVATEKNKMA---GELEVLRS--QERRLKEKVANMEVALDKASL--QFAECQDIIQ 828
|
250 260
....*....|....*....|..
gi 1907083610 1104 ELQAQVDELKVQLTKKEEELQG 1125
Cdd:pfam15921 829 RQEQESVRLKLQHTLDVKELQG 850
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1005-1209 |
9.18e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1005 VTAEAKIKKMEEEVLLLEDQNSKFIKEKKLMEDRIAECSSQLAEEEEKaknLAKIRNKQEVMISDLEERLKKEEKTRQEL 1084
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1085 EKAKRKL--DGETTD-----------------------LQDQIAELQAQVDELKVQLTKKEEELQGALARGDDEtlhKNN 1139
Cdd:COG3883 89 GERARALyrSGGSVSyldvllgsesfsdfldrlsalskIADADADLLEELKADKAELEAKKAELEAKLAELEAL---KAE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1140 ALKVARELQAQIAELQEDFESEKASRNKAEKQKRDLSEELEALKTELEDTLDTTAAQQELRTKREQEVAE 1209
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
877-1700 |
9.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 877 QVTRQEEELQAKDEELLKVKEKQTKVEGELEEMERK-----------------HQQLLEEKNILAEQLQAETELFAEA-- 937
Cdd:PRK04863 349 KIERYQADLEELEERLEEQNEVVEEADEQQEENEARaeaaeeevdelksqladYQQALDVQQTRAIQYQQAVQALERAkq 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 938 ------------EEMRARLAAKKQELEEILHDLESRVEEEEERNQilQNEK-----KKMQAHIQDLEEQLdeeegarqkl 1000
Cdd:PRK04863 429 lcglpdltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS--QFEQayqlvRKIAGEVSRSEAWD---------- 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1001 qlekvTAEAKIKKMEEEVLLLEDQNSkfikekklMEDRIAECSSQLAEE---EEKAKNLAKIRNKQEVMISDLEERLKKE 1077
Cdd:PRK04863 497 -----VARELLRRLREQRHLAEQLQQ--------LRMRLSELEQRLRQQqraERLLAEFCKRLGKNLDDEDELEQLQEEL 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1078 EKTRQELEKAKRKLDGETTDLQDQIAELQAQVDELKvQLTKKEEELQGALARGDDETlhkNNALKVARELQAQIAELQED 1157
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRLA-ARAPAWLAAQDALARLREQS---GEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1158 FESEKASRNKAEKQKRDLSEELEALkteledTLDTTAAQQELRTKREQEVAELKKALEDETKNHEAQIQDMR---QRHAT 1234
Cdd:PRK04863 640 ERELTVERDELAARKQALDEEIERL------SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYFSALygpARHAI 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1235 ALEELS---EQLEQAKRFKANL---EKNKQ-----GLETDNKELACEVKVLQ------QVKAESEHKRKKLDAQVQELHA 1297
Cdd:PRK04863 714 VVPDLSdaaEQLAGLEDCPEDLyliEGDPDsfddsVFSVEELEKAVVVKIADrqwrysRFPEVPLFGRAAREKRIEQLRA 793
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1298 KVSEGDRLRVELAEKANKLQNELDNVSTLLeeAEKKGIKFAKDAaglESQLQDTQELLQEETR-------QKLNLSSRIR 1370
Cdd:PRK04863 794 EREELAERYATLSFDVQKLQRLHQAFSRFI--GSHLAVAFEADP---EAELRQLNRRRVELERaladhesQEQQQRSQLE 868
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1371 QLEEEKNSLQEQQ-EEEEEARKNLEKQVLALQSQLA---DTKKKVDDDLGTIESLEEAKKKLLKDVEALSQrLEEkvlAY 1446
Cdd:PRK04863 869 QAKEGLSALNRLLpRLNLLADETLADRVEEIREQLDeaeEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQ-LKQ---DY 944
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1447 DKLEKTKNRLQQELDDLTvDLDHQR------QIVSNLEKKQKKFDQLLAEEKgisaRYAEERDRAEAEAREKETKAlsla 1520
Cdd:PRK04863 945 QQAQQTQRDAKQQAFALT-EVVQRRahfsyeDAAEMLAKNSDLNEKLRQRLE----QAEQERTRAREQLRQAQAQL---- 1015
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1521 raleealeakeefeRQNKQLRADmedlmsskddvgknvheLEKSKRALEQQVEEMRTQLEELedELQATEDAKLRLevnm 1600
Cdd:PRK04863 1016 --------------AQYNQVLAS-----------------LKSSYDAKRQMLQELKQELQDL--GVPADSGAEERA---- 1058
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1601 qamkAQFERDLQTRDEQNEEKKRLLLKQVRELEAELEDERKQralavasKKKMEIDLKDLEAQIEAANKARDEVIKQLRK 1680
Cdd:PRK04863 1059 ----RARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKK-------LRKLERDYHEMREQVVNAKAGWCAVLRLVKD 1127
|
890 900
....*....|....*....|....*
gi 1907083610 1681 LQAQMKDYQREL-----EEARASRD 1700
Cdd:PRK04863 1128 NGVERRLHRRELaylsaDELRSMSD 1152
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1560-1771 |
9.60e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1560 ELEKSKRALEQQVEEMRTQLEELED-ELQATEDAKLRLEVNMQAMKAQFERDLQT------RDEQNeekkrlLLKQVREL 1632
Cdd:COG0497 176 ELRADEAERARELDLLRFQLEELEAaALQPGEEEELEEERRRLSNAEKLREALQEalealsGGEGG------ALDLLGQA 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907083610 1633 EAELE-----DERKQRAL-AVASkkkMEIDLKDLEAQIEA------ANKAR-DEVIKQLRKLQAQMKDYQRELEEARASR 1699
Cdd:COG0497 250 LRALErlaeyDPSLAELAeRLES---ALIELEEAASELRRyldsleFDPERlEEVEERLALLRRLARKYGVTVEELLAYA 326
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907083610 1700 DEIfaqskesEKKLKSLEAeilqLQEELASSERARRHAEQERDELADEIanSASGKSALldekRRLEARIAQ 1771
Cdd:COG0497 327 EEL-------RAELAELEN----SDERLEELEAELAEAEAELLEAAEKL--SAARKKAA----KKLEKAVTA 381
|
|
| |
