|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-796 |
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: 1318.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 358
Cdd:cd14930 153 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 359 SLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 438
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 439 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 518
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 519 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 598
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 599 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTV 678
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 679 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 758
Cdd:cd14930 553 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 116284396 759 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14930 633 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-796 |
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: 1292.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIP--------GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ-ERELFQETL 357
Cdd:cd14920 153 DVTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14920 233 EAMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14920 313 AQTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14920 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMF 675
Cdd:cd14920 473 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 676 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 755
Cdd:cd14920 553 RTVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 116284396 756 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14920 633 LTPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
119-796 |
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: 1277.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGK-------KKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQ-ERELFQET 356
Cdd:cd01377 154 GSTGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVdDAEEFKLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd01377 234 DEAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd01377 314 KGQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK-FQRPRH 595
Cdd:cd01377 393 HMFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 596 LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPRRGMF 675
Cdd:cd01377 471 KKSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES---------GGGGGKKKKKGGSF 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 676 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 755
Cdd:cd01377 542 RTVSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSI 621
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 116284396 756 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd01377 622 LAPNAIPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
873-1953 |
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: 1204.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 873 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL 952
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 953 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDR 1032
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1033 LAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGR 1112
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1113 KEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1192
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1193 LRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTAR 1272
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1273 QEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1352
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1353 TRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQR 1432
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1433 LAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALS 1512
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1513 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEV 1592
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1593 TVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQL 1672
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1673 RKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAI 1752
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1753 LEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAG 1832
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1833 ARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1912
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 116284396 1913 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1953
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-796 |
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: 1170.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPAsvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIA----LSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14932 157 DVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14932 237 EAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14932 317 AQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14932 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP-GGRPRRGMFR 676
Cdd:cd14932 477 DDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgAFKTRKGMFR 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 677 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 756
Cdd:cd14932 557 TVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 636
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 116284396 757 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14932 637 TPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
119-796 |
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: 1134.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVPASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHL 596
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 597 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFR 676
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 677 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 756
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 116284396 757 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
119-796 |
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: 1111.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG-----------ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 357
Cdd:cd14919 150 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14919 230 EAMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14919 310 AQTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14919 390 MFILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLK 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP--GGRPRRGMF 675
Cdd:cd14919 470 DKADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgAFKTRKGMF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 676 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 755
Cdd:cd14919 550 RTVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 116284396 756 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14919 630 LTPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
119-796 |
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: 1104.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKD----QNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-RELFQETL 357
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd15896 317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd15896 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRT 677
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 678 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 757
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670
....*....|....*....|....*....|....*....
gi 116284396 758 PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd15896 637 PNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
119-796 |
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: 1097.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSI--------TGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQETL 357
Cdd:cd14921 153 DVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14921 233 EAMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd14921 313 AQTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 518 MFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLR 597
Cdd:cd14921 393 MFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMF 675
Cdd:cd14921 473 DKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKGMF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 676 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 755
Cdd:cd14921 553 RTVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 632
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 116284396 756 LTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14921 633 LAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
108-796 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1074.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 108 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ 187
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 188 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNS 267
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSG------------SAGNVGRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 268 SRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-P 346
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 347 G-QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:pfam00063 230 GiDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 426 PRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQG 585
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 586 GHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVssLGDGP 665
Cdd:pfam00063 467 KHPHFQKPR-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN--ESGKS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 666 PGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 745
Cdd:pfam00063 544 TPKRTKKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRIT 623
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 116284396 746 FQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:pfam00063 624 FQEFVQRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
100-808 |
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: 1001.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 100 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTE 179
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 180 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstvsyGELERQLLQANPILEAFGNA 259
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV--------------GSVEDQILESNPILEAFGNA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 260 KTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT 339
Cdd:smart00242 147 KTLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 340 NGPSSS-PGQE-RELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT-AAQKLCRLLGLGV 416
Cdd:smart00242 227 QGGCLTvDGIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 417 TDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLN 496
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 497 SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSF 576
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTF 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 577 VEKVAQEQGGHPKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgle 656
Cdd:smart00242 463 LEKLNQHHKKHPHFSKPK-KKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS----- 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 657 QVSSLGdgppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIC 736
Cdd:smart00242 537 NAGSKK-----------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIR 605
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116284396 737 RQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERD 808
Cdd:smart00242 606 RAGFPYRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
98-1183 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 917.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 98 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAV 177
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 178 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvSTVSYGELERQLLQANPILEAFG 257
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-------------STVEISSIEKQILATNPILEAFG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 258 NAKTVKNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRF 337
Cdd:COG5022 206 NAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIY 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 338 LTNGPSSSPGQ--ERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLG 415
Cdd:COG5022 286 LSQGGCDKIDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGID 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQL 495
Cdd:COG5022 365 PSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 496 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKS 575
Cdd:COG5022 444 NSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDES 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 576 FVEKVAQ--EQGGHPKFQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIV 653
Cdd:COG5022 522 FTSKLAQrlNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 654 gleqvsslgdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 733
Cdd:COG5022 600 -----------------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETI 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 734 RICRQGFPNRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDL 809
Cdd:COG5022 663 RISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDA 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 810 KVTDIIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRHWQWWRLFTKVKPLLQVTRQDEVLQARAQELQKV 889
Cdd:COG5022 743 KLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKL 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 890 Q--ELQQQSAREvgelqgrvaQLEEERARLAEQLRAEAELCaeaeetrgrLAARKQELELVVSELEARVGEEEECSRQMQ 967
Cdd:COG5022 823 QktIKREKKLRE---------TEEVEFSLKAEVLIQKFGRS---------LKAKKRFSLLKKETIYLQSAQRVELAERQL 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 968 TEKKRLQQHIQELeahleaeegARQKLQLEKVTTEAKmKKFEEDLLL-LEDQNSKLSKERKLLEDRlaEFSSQAAEEEEK 1046
Cdd:COG5022 885 QELKIDVKSISSL---------KLVNLELESEIIELK-KSLSSDLIEnLEFKTELIARLKKLLNNI--DLEEGPSIEYVK 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1047 VKSLNKLRL---KYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQ--QRAEELRAQLGRKEEELQAAL 1121
Cdd:COG5022 953 LPELNKLHEvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSAS 1032
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1122 ARAEDEGGARAQLLKSlreaqaALAEAQEDLESERV-ARTKAEKQRRDLGEELEALRGELEDT 1183
Cdd:COG5022 1033 KIISSESTELSILKPL------QKLKGLLLLENNQLqARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
119-796 |
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: 838.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA---------SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-----PGQE-RE 351
Cdd:cd00124 152 FDPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 352 LFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd00124 232 EFQELLDALDVLGFSDEEQDSIFRILAAILHLGNIefEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:cd00124 312 VGGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHP 588
Cdd:cd00124 392 KLQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 589 KFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleqvsslgdgppgg 668
Cdd:cd00124 469 RFFSKKRKAKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ----------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 669 rprrgmfrtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 748
Cdd:cd00124 519 -------------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDE 585
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 116284396 749 FRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd00124 586 FLKRYRILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
119-796 |
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: 775.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKA--QFLATKTGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14927 159 GPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSMNPYdYHFCSQGVTTVDNmDDGEELMAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14927 239 DHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14927 319 KGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14927 397 HHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 ---HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPR 671
Cdd:cd14927 474 pdkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKRKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 672 RGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 751
Cdd:cd14927 551 AASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQ 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 116284396 752 RYEILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14927 631 RYRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
120-796 |
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: 749.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPasvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMK--------GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQE 355
Cdd:cd14913 154 FGTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLITTNPYdYPFISQGEILVASiDDAEELLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14913 234 TDSAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEY 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd14913 313 VTKGQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 514 FNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQR 592
Cdd:cd14913 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 593 PRHLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRP 670
Cdd:cd14913 468 PKVVKGRAEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKK 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 671 RRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 750
Cdd:cd14913 542 KGSSFQTVSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFK 621
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 116284396 751 QRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14913 622 QRYRVLNASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
119-796 |
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: 738.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpasvsTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEA--------AKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPCSHYRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14909 153 GPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14909 233 DQAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14909 313 QGRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNH 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14909 392 HMFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 596 LR---DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGDGPPGGRPRR 672
Cdd:cd14909 469 PKpgqQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----QSGGGEQAKGGRGKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 673 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 752
Cdd:cd14909 544 GGFATVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 116284396 753 YEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14909 624 YKILNPAGI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
119-796 |
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: 709.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKgrkepgvpasVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGK----------QSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFLTNGPSSSPGQER-ELFQET 356
Cdd:cd14934 151 GTTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPnPKEYHWVSQGVTVVDNMDDgEELQIT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14934 231 DVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14934 311 KGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14934 390 HMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKG 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 596 LRD---QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgppggRPRR 672
Cdd:cd14934 467 GKGkgpEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK-----------QKRG 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 673 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 752
Cdd:cd14934 536 SSFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 116284396 753 YEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14934 616 YQVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
120-796 |
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: 705.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSpkgrkepgvpASVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGS----------SSGET----QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PG-QERELFQET 356
Cdd:cd01380 148 DKNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd01380 228 RKALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd01380 308 KPLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK--FQRP 593
Cdd:cd01380 388 QHVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 594 RhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqvsslgdgppggrprrg 673
Cdd:cd01380 464 R--FSNTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK-------------------------------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 674 mfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 753
Cdd:cd01380 510 --KTVGSQFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRY 587
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 116284396 754 EILTPNAIPKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd01380 588 RVLLPSKEWLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
120-796 |
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: 692.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGK------GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYdYAFISQGETTVASiDDAEELMATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14917 236 NAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14917 315 KGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14917 393 HHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 HLRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRR 672
Cdd:cd14917 470 NIKGkpEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKG 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 673 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 752
Cdd:cd14917 544 SSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR 623
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116284396 753 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14917 624 YRILNPAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
119-796 |
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: 688.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA-----------LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14929 150 GARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14929 230 QAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14929 310 SQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPRH 595
Cdd:cd14929 388 HMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 596 LRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRrg 673
Cdd:cd14929 465 DKKkfEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGAS-- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 674 mFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 753
Cdd:cd14929 540 -FQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRY 618
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 116284396 754 EILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14929 619 CILNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
120-796 |
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: 677.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVAS-SPKGRKEpgvpasVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKE------NPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQET 356
Cdd:cd14916 156 GATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYdYAFVSQGEVSVASiDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 435
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 436 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14916 315 TKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 515 NHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRP 593
Cdd:cd14916 393 NHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKP 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 594 RHL--RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRpr 671
Cdd:cd14916 470 RNVkgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-- 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 672 rgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 751
Cdd:cd14916 548 ---FQTVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQ 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 116284396 752 RYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14916 625 RYRILNPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
120-796 |
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: 674.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGP-SSSPGQERELFQETL 357
Cdd:cd14912 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITTNPYdYPFVSQGEiSVASIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14912 238 SAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14912 317 KGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPR 594
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRR 672
Cdd:cd14912 472 VVKGKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---SGAQTAEGASAGGGAKKGGKKKG 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 673 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 752
Cdd:cd14912 549 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116284396 753 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14912 629 YKVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
121-796 |
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: 673.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGES 200
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 201 GAGKTENTKKVIQYLAHVASSPKGRKEPgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDV 280
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEE------SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 281 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETLE 358
Cdd:cd14918 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 359 SLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14918 316 GQTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPKFQRPRH 595
Cdd:cd14918 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 596 LRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSlgdGPPGGRPRRG 673
Cdd:cd14918 471 VKGKAEahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSG---AKKGAKKKGS 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 674 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 753
Cdd:cd14918 545 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRY 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 116284396 754 EILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14918 625 KVLNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
120-796 |
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: 669.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14910 158 TTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITTNPYdYAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14910 317 KGQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14910 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 HLRD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEqvSSLGDGPPGGRPRR 672
Cdd:cd14910 472 PAKGkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAAAAE--AEEGGGKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 673 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 752
Cdd:cd14910 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116284396 753 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14910 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-796 |
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: 665.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGvPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQQ-PGKMQ----GTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLLEPCSHYRFltngPSSSPGQ-------EREL 352
Cdd:cd14923 157 ATGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLLISTNPFDF----PFVSQGEvtvasidDSEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 353 FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVG 431
Cdd:cd14923 232 LLATDNAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 432 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKL 510
Cdd:cd14923 311 NEYVTKGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 511 QQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGGHPK 589
Cdd:cd14923 389 QQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 590 FQRPRHLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPG 667
Cdd:cd14923 466 FQKPKPAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 668 GRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 747
Cdd:cd14923 542 GKKKGSSFQTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYA 621
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 116284396 748 EFRQRYEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14923 622 DFKQRYRILNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
120-796 |
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: 663.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVStvsyGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKMQ----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSH-YRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14915 158 ATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYdFAFVSQGEITVPSiDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14915 317 KGQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GGHPKFQRPR 594
Cdd:cd14915 395 HHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 HLRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRR 672
Cdd:cd14915 472 PAKGKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGGKKKG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 673 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 752
Cdd:cd14915 547 SSFQTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQR 626
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116284396 753 YEILTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14915 627 YKVLNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
120-796 |
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: 637.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPASVSTVSygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERVK-----DMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd01378 149 FKGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDY 434
Cdd:cd01378 229 NAMKVIGFTEEEQDSIFRILAAILHLGNIQFA-EDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd01378 308 YEVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 515 nhTMFVL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01378 388 --IELTLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 592 RPR-HLRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSlgdgppggr 669
Cdd:cd01378 463 CPSgHFELrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE-----GVDLDSK--------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 670 prrGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 749
Cdd:cd01378 529 ---KRPPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKF 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 116284396 750 RQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd01378 606 LERYKLLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
120-796 |
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: 628.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG-----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QERELFQETL 357
Cdd:cd01383 143 AAGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 437
Cdd:cd01383 223 EALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 438 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 517
Cdd:cd01383 303 KLTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRH 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 518 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRprhlR 597
Cdd:cd01383 383 LFKLEQEEYELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKG----E 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 598 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivGLEQVSSLGDGPPGGRPRRGMFRT 677
Cdd:cd01383 456 RGGAFTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS------KMLDASRKALPLTKASGSDSQKQS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 678 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 757
Cdd:cd01383 530 VATKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLL 609
|
650 660 670
....*....|....*....|....*....|....*....
gi 116284396 758 PNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd01383 610 PEDV-SASQDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
120-796 |
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: 623.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS-----------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPCSHYRFLT-NGPSSSPG-QERELFQE 355
Cdd:cd14883 145 ASGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDH 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKR-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14883 225 LRLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14883 305 TEIPLKVQEARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 515 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPR 594
Cdd:cd14883 384 NHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 HLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQVSSLGDGPPGGRPRRGM 674
Cdd:cd14883 461 RRRWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKG 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 675 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 754
Cdd:cd14883 540 KPTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 116284396 755 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14883 620 CLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
119-796 |
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: 596.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVAsspkGRKepgvpasvSTVsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQH--------SWI-----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPGQ-ERELFQET 356
Cdd:cd01381 144 NKNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALK--RERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd01381 224 RSAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEatVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGET 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 512
Cdd:cd01381 304 VVSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 513 LFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01381 384 FFVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 592 RPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPr 671
Cdd:cd01381 460 KPKS-DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKSP- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 672 rgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 751
Cdd:cd01381 529 -----TLSSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVE 603
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116284396 752 RYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd01381 604 RYRVLVPGIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
119-796 |
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: 589.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVAsspkGRKEPGVpASVstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG----GRAVTEG-RSV--------EQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG--QERELFQE 355
Cdd:cd01384 148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGR 432
Cdd:cd01384 228 TRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 433 D-YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQ 511
Cdd:cd01384 307 DgIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 512 QLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFS 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 592 RPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPR 671
Cdd:cd01384 463 KPK--LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------------VAGLFPPLPREGTS 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 672 RGM-FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFR 750
Cdd:cd01384 525 SSSkFSSIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFL 604
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 116284396 751 QRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 796
Cdd:cd01384 605 DRFGLLAPEV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
119-796 |
3.14e-180 |
|
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: 561.87 E-value: 3.14e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGS----------------GAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPcshyrfLTNGPSSspgqerelFQETL 357
Cdd:cd01382 145 FNEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRI 428
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 429 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd01382 291 GAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYC 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 507 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd01382 367 NEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKN 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 587 HPKFQRPR------H--LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegIVGLEQV 658
Cdd:cd01382 444 HFRLSIPRksklkiHrnLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKF----------IRSLFES 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 659 SSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 738
Cdd:cd01382 514 STNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQG 593
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 739 GFPNRILFQEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd01382 594 GFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
119-796 |
1.09e-178 |
|
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: 558.24 E-value: 1.09e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQ----DREDQS 193
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 194 ILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTVS--YGELERQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASEAIEqtLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-R 350
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 351 ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 427
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 507
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 508 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDEeCWFPKAT--DKSFV------- 577
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 578 ------EKVAQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdveg 651
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 652 ivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 731
Cdd:cd14890 543 --SIREVS------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116284396 732 GIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14890 603 AIQIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
119-796 |
1.98e-173 |
|
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: 543.21 E-value: 1.98e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG-----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAgeqlkadlllEPCSHYRFLTNGPSSSPGQEREL------ 352
Cdd:cd14872 144 DNRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASP----------DPASRGGWGSSAAYGYLSLSGCIevegvd 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 353 ----FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:cd14872 214 dvadFEEVVLAMEQLGFDDADINNVMSLIAAILKLGNIefaSGGGKSLVSGSTVANRDVLKEVATLLGVDAATLEEALTS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 426 PRIKV-GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCIN 504
Cdd:cd14872 294 RLMEIkGCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 505 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQ 584
Cdd:cd14872 374 FTNEKLQQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTH 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 585 GGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslgdg 664
Cdd:cd14872 451 AAKSTFVYAEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG------------- 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 665 ppggrPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 744
Cdd:cd14872 518 -----DQKTSKVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRY 592
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 116284396 745 LFQEFRQRYEILtPNAIPKGFM-DGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14872 593 SHERFLKRYRFL-VKTIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
120-796 |
2.93e-166 |
|
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: 523.38 E-value: 2.93e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVASSPkgrkepgvpasvstvsYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN----------------NRTLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPCSHYRFLTNGPSSSPGQE-----RELF 353
Cdd:cd01379 146 STGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQ----ATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd01379 226 EEIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 507
Cdd:cd01379 306 TRGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIAN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 508 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd01379 386 EQIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 587 HPkFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpp 666
Cdd:cd01379 462 KY-YWRPK--SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ---------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 667 ggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 746
Cdd:cd01379 517 ----------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILF 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 116284396 747 QEFRQRYEILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 796
Cdd:cd01379 587 ADFLKRYYFLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
119-796 |
6.35e-165 |
|
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: 520.47 E-value: 6.35e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPASVStvsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVT--------EQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS-SPGQ-ERELFQET 356
Cdd:cd01387 145 E-GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd01387 224 LAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 514 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRP 593
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKP 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 594 RhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGiVGLEQVSSLGDGPPGGRPRRG 673
Cdd:cd01387 460 R--MPLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA-QTDKAPPRLGKGRFVTMKPRT 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 674 mfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 753
Cdd:cd01387 537 --PTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRY 614
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 116284396 754 EILTPNAIPKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 796
Cdd:cd01387 615 RCLVALKLPRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
119-796 |
1.22e-162 |
|
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: 513.47 E-value: 1.22e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD----------------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE-------- 349
Cdd:cd14897 145 FTENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 350 RELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14897 225 RQMFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14897 305 IRGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQG 585
Cdd:cd14897 385 SNERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 586 GHPKFQRPRHlrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgdgp 665
Cdd:cd14897 462 ESPRYVASPG--NRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT------------------ 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 666 pggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRIL 745
Cdd:cd14897 522 --------------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIK 587
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 116284396 746 FQEFRQRYEILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 796
Cdd:cd14897 588 YEDFVKRYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
119-794 |
1.07e-161 |
|
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: 511.64 E-value: 1.07e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHVYAVTEGAYRSMLQDRE-- 190
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 191 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQ--------NATERENVRDRVLESNPILEAFGNARTNRNNNSS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngpSSSPGQ 348
Cdd:cd14901 153 RFGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 349 ER-------ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIA-LKRERNTDQATMPDNTAAQKLCRLLGLGVTDFS 420
Cdd:cd14901 229 DRrdgvddsVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCfVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 421 RALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFE 499
Cdd:cd14901 309 KTLCTREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 500 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEK 579
Cdd:cd14901 389 QLCINFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 580 VAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVS 659
Cdd:cd14901 466 YYDLLAKHASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF----------------LS 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 660 SlgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQG 739
Cdd:cd14901 530 S----------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSG 593
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 740 FPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LELDPNLYrVGQSKIF 794
Cdd:cd14901 594 YPVRFPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
119-796 |
3.68e-160 |
|
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: 507.78 E-value: 3.68e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpasvSTVsygeleRQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLND----------STI------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 355
Cdd:cd14903 145 FDKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFAR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd14903 223 TKEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 513
Cdd:cd14903 303 VYTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 514 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGGHPKFQR- 592
Cdd:cd14903 382 FTQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDv 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 593 ---PRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGR 669
Cdd:cd14903 455 iefPRTSRTQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRG 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 670 PRRGMfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 749
Cdd:cd14903 533 GALTT-TTVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEF 611
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 116284396 750 RQRYEILTPNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFFR 796
Cdd:cd14903 612 LDKFWLFLPEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
119-796 |
8.48e-160 |
|
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: 507.68 E-value: 8.48e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLahVASSPKGrkepgvpasvstvsYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKG--------------YGSgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL--TNGPSSSPGQERELFQE 355
Cdd:cd01385 145 YRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRD 433
Cdd:cd01385 225 LKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEK 509
Cdd:cd01385 305 TLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 510 LQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 589
Cdd:cd01385 384 LQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKY 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 590 FQRPRhLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQVSSL-------- 661
Cdd:cd01385 461 YEKPQ-VMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF-------VRELIGIDPVAVFrwavlraf 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 662 ----------GDGPPGGRPRRGMFR------------------TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAG 713
Cdd:cd01385 532 framaafreaGRRRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPL 611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 714 KLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKI 793
Cdd:cd01385 612 RFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKV 687
|
...
gi 116284396 794 FFR 796
Cdd:cd01385 688 FLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
119-796 |
8.67e-159 |
|
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: 503.56 E-value: 8.67e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV--------EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG-QERELFQE 355
Cdd:cd14873 153 ICQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFRE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 435
Cdd:cd14873 233 VITAMEVMQFSKEEVREVSRLLAGILHLGNIEFI---TAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 436 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 515
Cdd:cd14873 310 LTPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFN 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 516 HTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRH 595
Cdd:cd14873 388 KHIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 596 LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGMF 675
Cdd:cd14873 464 AVNN--FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRR 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 676 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 755
Cdd:cd14873 533 PTVSSQFKDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKV 612
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 116284396 756 LTPNAIPKGFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14873 613 LMRNLALPEDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
119-758 |
8.69e-158 |
|
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: 501.53 E-value: 8.69e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvSTVsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKR--------SLV-----EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FD---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKAD 326
Cdd:cd14888 147 FSklkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISID 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 327 LLL-EPCSHYRFLT-NGPSSSPG-QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNT 403
Cdd:cd14888 227 MSSfEPHLKFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSAS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 404 AAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS 480
Cdd:cd14888 307 CTDDLekvASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 481 FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLA 560
Cdd:cd14888 387 FCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 561 LLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR 640
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVK--TDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 641 LTAEIWKdvegivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 720
Cdd:cd14888 542 FISNLFS------------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISV 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 116284396 721 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 758
Cdd:cd14888 610 NEQLKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
119-796 |
2.02e-155 |
|
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276857 [Multi-domain] Cd Length: 656 Bit Score: 494.66 E-value: 2.02e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHVYAVTEGAYRSMLQDR----ED 191
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLATASKLAKGASTSKGAANAHE----SIEECVLLSNLILEAFGNAKTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS-PGQER 350
Cdd:cd14892 157 KYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 351 EL-FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNiaLKRERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLT 425
Cdd:cd14892 237 ATeFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 426 PRIKVGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQL 495
Cdd:cd14892 315 QTTSTARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPT 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 496 NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDK 574
Cdd:cd14892 395 NSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 575 SFVEKVAQEQ-GGHPKFQRPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegiv 653
Cdd:cd14892 472 QLLTIYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK-------------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 654 gleqvsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 733
Cdd:cd14892 536 ---------------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVV 587
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116284396 734 RICRQGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM-----IQALELDPNLYRVGQSKIFFR 796
Cdd:cd14892 588 RIRREGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
119-796 |
1.37e-151 |
|
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: 484.53 E-value: 1.37e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHVYAVTEGAYRSMLQDR 189
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 190 EDQSILCTGESGAGKTENTKKVIQYL------AHVASSPKGRKEPGVPASVSTVSygeLERQLLQANPILEAFGNAKTVK 263
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLtqlsqqEQNSEEVLTLTSSIRATSKSTKS---IEQKILSCNPILEAFGNAKTVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 264 NDNSSRFGKFIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYRFLTNG 341
Cdd:cd14907 158 NDNSSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 342 PSSSPGQER----ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALK-RERNTDQATMPDNTAA-QKLCRLLGLG 415
Cdd:cd14907 238 KSNCYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGID 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIA 488
Cdd:cd14907 318 EEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 489 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEEC 566
Cdd:cd14907 398 GFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSC 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 567 WFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIW 646
Cdd:cd14907 475 KLATGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 647 KDVEGivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRC 726
Cdd:cd14907 554 SGEDG--------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRY 625
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 727 NGVLEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqacekmiqaleldpnlYRVGQSKIFFR 796
Cdd:cd14907 626 LGVLESIRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
121-796 |
7.02e-142 |
|
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: 457.06 E-value: 7.02e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 121 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSML----QDREDQSILC 196
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 197 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 276
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ--------------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 277 NFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPcSHYRFLTN--GPSSSPGQERELF 353
Cdd:cd14889 146 RFR-NGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALkrERNTDQA---TMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKV 430
Cdd:cd14889 224 DEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 431 GRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd14889 302 RGEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 507 NEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGG 586
Cdd:cd14889 380 NEQLQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKG 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 587 HPKFQRPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP 666
Cdd:cd14889 457 NSYYGKSR--SKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAG 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 667 GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 746
Cdd:cd14889 535 SDNFNSTRKQSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSF 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 116284396 747 QEFRQRYEIL--TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQSKIFFR 796
Cdd:cd14889 615 AEFAERYKILlcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
120-756 |
1.18e-138 |
|
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: 447.06 E-value: 1.18e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHVYAVTEGAYRSM-- 185
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 186 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgVPASVSTVSYGE-LERQLLQANPILEAFGNAKTV 262
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNN-------LAASVSMGKSTSgIAAKVLQTNILLESFGNARTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 263 KNDNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepcshyrfltngp 342
Cdd:cd14900 155 RNDNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK----------------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 343 ssspgqeRELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD-QATMPDNTAAQKL------CRLLGLG 415
Cdd:cd14900 218 -------RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 416 VTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFE 491
Cdd:cd14900 291 ATKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 492 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKA 571
Cdd:cd14900 371 VFPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKG 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 572 TDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDplndnvaaLLHQstdrltaeiwkdveg 651
Cdd:cd14900 448 SDTTLASKLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ--------------- 504
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 652 ivglEQVSslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 731
Cdd:cd14900 505 ----EAVD--------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVME 565
|
650 660
....*....|....*....|....*
gi 116284396 732 GIRICRQGFPNRILFQEFRQRYEIL 756
Cdd:cd14900 566 AVRVARAGFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
119-796 |
9.49e-136 |
|
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: 439.76 E-value: 9.49e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAHVASspkGRKEpgvpasvSTVSygelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKD-------KTIA------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSS--PG-QERELFQ 354
Cdd:cd14904 145 FDGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 355 ETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDY 434
Cdd:cd14904 225 STQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFD-KSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNES 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 435 VQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 514
Cdd:cd14904 304 VTVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 515 NHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGGHPKFQ 591
Cdd:cd14904 384 TTDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESID 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 592 RPRHLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgLEQVSSLGDGPPGGRPR 671
Cdd:cd14904 460 FPKVKRTQ--FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGTKAP 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 672 rgmfRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 751
Cdd:cd14904 534 ----KSLGSQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELAT 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 116284396 752 RYEILTPNAIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 796
Cdd:cd14904 610 RYAIMFPPSMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
119-796 |
7.14e-134 |
|
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: 434.09 E-value: 7.14e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE---D 191
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTVSYG--ELERQLLQANPILEAFGNAKTVKNDNSSR 269
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLSvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 270 FGKFIRINFDVAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPG 347
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 348 -QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrERNTDQ-----ATMPDNTAAQKLCRLLGLGVTDFSR 421
Cdd:cd14891 236 iDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFD-EEDTSEgeaeiASESDKEALATAAELLGVDEEALEK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 422 ALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSFE 499
Cdd:cd14891 315 VITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 500 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDKS 575
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDAK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 576 FVEKVAQEQGGHPKFQRPrHLRDQAD-FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdvegivg 654
Cdd:cd14891 466 LNETLHKTHKRHPCFPRP-HPKDMREmFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS----------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 655 leqvsslgdgppggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIR 734
Cdd:cd14891 528 -------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCE 582
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 735 ICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14891 583 VLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
119-758 |
2.38e-129 |
|
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: 423.92 E-value: 2.38e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHVYAVTEGAYRSMLQ-D 188
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 189 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASvstvsygELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAV-------EIGKRILQTNPILESFGNAQTIRNDNSS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFL-TNGPSSSPG 347
Cdd:cd14902 154 RFGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 348 QER-----ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKL---CRLLGLGVTDF 419
Cdd:cd14902 234 RAVadkyaQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 420 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFE 491
Cdd:cd14902 314 ETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 492 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKA 571
Cdd:cd14902 394 SLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKG 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 572 TDKSFVEKVAQEQGGhpkfqrprhlRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEG 651
Cdd:cd14902 471 SNQALSTKFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV-------VVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 652 IVGLEQVSSLG-DGPPGGRPRRGMFRT--VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 728
Cdd:cd14902 532 IGADENRDSPGaDNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVG 611
|
650 660 670
....*....|....*....|....*....|
gi 116284396 729 VLEGIRICRQGFPNRILFQEFRQRYEILTP 758
Cdd:cd14902 612 VLEAVRIARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
119-796 |
1.26e-127 |
|
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: 417.77 E-value: 1.26e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHVYAVTEGAYRSMLQD- 188
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 189 REDQSILCTGESGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSS 268
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTL-----GNGEEGAPNEGEELGKLSIMDRVLQSNPILEAFGNARTLRNDNSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 269 RFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKA--------DLLLEPCSHYRFLTN 340
Cdd:cd14908 156 RFGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEkyefhdgiTGGLQLPNEFHYTGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 341 G--PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQK----LCRLLGL 414
Cdd:cd14908 236 GgaPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 415 GVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIF 493
Cdd:cd14908 315 DVDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 494 QLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KAT 572
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 573 DKSFVEKV--------AQEQGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLM-KNMDPLNdnvaallhqstdrLTA 643
Cdd:cd14908 472 DANYASRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTA 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 644 EIwkdvegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQ 723
Cdd:cd14908 539 DS----------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQ 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 724 LRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM-------DGKQACEKMI----------QALELDPNL- 785
Cdd:cd14908 590 LRYGGVLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVKKMckdlvkgvlsPAMVSMKNIp 668
|
730
....*....|....
gi 116284396 786 ---YRVGQSKIFFR 796
Cdd:cd14908 669 edtMQLGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
117-842 |
5.42e-127 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 420.98 E-value: 5.42e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 117 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 196 CTGESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 275
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---------------SSKSGNMDLKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 276 INFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 354
Cdd:PTZ00014 253 LQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFE 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 355 ETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALK-RERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:PTZ00014 333 EVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEgKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTY 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:PTZ00014 413 AGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGGHP 588
Cdd:PTZ00014 491 MLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 589 KFQRPRhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE---GIVGLEQVsslgdg 664
Cdd:PTZ00014 568 KYKPAK--VDSnKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvekGKLAKGQL------ 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 665 ppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 744
Cdd:PTZ00014 640 -------------IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRR 706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 745 LFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR---AGVLAQLEEERDLKVTDIIVSFQAA 821
Cdd:PTZ00014 707 TFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEAL 786
|
730 740
....*....|....*....|....*
gi 116284396 822 ARGYLARRAFQKR----QQQQSALR 842
Cdd:PTZ00014 787 ILKIKKKRKVRKNikslVRIQAHLR 811
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
119-796 |
5.08e-125 |
|
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: 409.17 E-value: 5.08e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpasvstvsygelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR----------------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSS--SPGQERELFQET 356
Cdd:cd14896 145 Q-HGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRD 433
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 434 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQ 511
Cdd:cd14896 303 RVSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQ 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 512 QLFNHTMFVLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQ 591
Cdd:cd14896 382 LFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYA 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 592 RPRhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrpr 671
Cdd:cd14896 459 KPQ--LPLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 672 rgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQ 751
Cdd:cd14896 526 -----TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLA 600
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116284396 752 RYEILTpNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14896 601 RFGALG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
119-792 |
2.68e-121 |
|
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: 400.89 E-value: 2.68e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDREDQSILC 196
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 197 TGESGAGKTENTKKVIQYLAHVASSPKGRKepgvpaSVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 276
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQN------NNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 277 NFDVAGYIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-CSHYRFL-------------TN 340
Cdd:cd14906 155 EFRSSDGKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 341 GPSSSPGQEREL---FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQAT--MPDNTAA-QKLCRLLGL 414
Cdd:cd14906 235 NKNSNHNNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 415 GVTDFSRALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFL 482
Cdd:cd14906 315 IESVFKQALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFI 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 483 GILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALL 562
Cdd:cd14906 395 GVLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLL 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 563 DEECWFPKATDKSFVEKVAQEQGGHPK-FQRPrhlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRL 641
Cdd:cd14906 472 DDECIMPKGSEQSLLEKYNKQYHNTNQyYQRT---LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 642 taeiwkdvegIVGLEQVSSLGDGPPGGRPRRGMfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVL 721
Cdd:cd14906 549 ----------KKSLFQQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVL 616
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 722 DQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 792
Cdd:cd14906 617 SQLRNVGVLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
119-794 |
5.17e-121 |
|
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: 397.82 E-value: 5.17e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHVYAVTEGAYRSMLQDREDQSILCT 197
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAhvasspkgrkepgvpASVSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIn 277
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---------------SAKSGNMDLRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 fDVA--GYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQ 354
Cdd:cd14876 145 -DVAseGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 355 ETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRErntDQATMPDntAA----------QKLCRLLGLGVTDFSRALL 424
Cdd:cd14876 224 EVLESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGK---TEQGVDD--AAaisneslevfKEACSLLFLDPEALKRELT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 425 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCI 503
Cdd:cd14876 299 VKVTKAGGQEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 504 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQE 583
Cdd:cd14876 377 NITNEMLQKNFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSK 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 584 QGGHPKFQRPRHLRDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgd 663
Cdd:cd14876 454 LKSNGKFKPAKVDSNI-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSL-- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 664 gppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNR 743
Cdd:cd14876 531 --------------IGSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYR 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 116284396 744 ILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 794
Cdd:cd14876 597 RPFEEFLYQFKFLDLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
120-757 |
2.44e-120 |
|
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: 397.79 E-value: 2.44e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQ----- 187
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 188 --DREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepGVPASVSTVSYGElerQLLQANPILEAFGNAKTVKND 265
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAESSKHTTA----TSSSKRRRAISGS---ELLSANPILESFGNARTLRND 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 266 NSSRFGKFIRINF-----DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFL 338
Cdd:cd14895 148 NSSRFGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 339 TNG---PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDQ-------------ATMP 400
Cdd:cd14895 228 SGGqcyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVlfVASSEDEGEEdngaasapcrlasASPS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 401 DNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR---- 473
Cdd:cd14895 308 SLTVQQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 474 -SPRQGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCID 547
Cdd:cd14895 388 lNPNKAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 548 LIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRhlRDQAD--FSVLHYAGKVDYKANEWLMKNMDP 625
Cdd:cd14895 467 MLE--QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 626 LNDNVAALLHQSTDRLTAEIWKDVEGIVglEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIV 705
Cdd:cd14895 543 PNAELFSVLGKTSDAHLRELFEFFKASE--SAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIK 620
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 116284396 706 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 757
Cdd:cd14895 621 PNDESASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
119-796 |
1.02e-118 |
|
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: 392.83 E-value: 1.02e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSPKGRkepgvpasvstVSYGELErqllQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGV-----------LSVEKLN----AALTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPC--SHYRFLTngPSSSPGQEREL---F 353
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaF 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL---------- 423
Cdd:cd01386 224 SKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpq 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 424 --LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFeifQLN----- 496
Cdd:cd01386 304 qsTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF---QNPahsgs 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 497 ----SFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLA 560
Cdd:cd01386 380 qrgaTFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLW 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 561 LLDEECWFPKATDKSFVEKV--AQEQGGHPKFQRPRHLRDQA-DFSVLHYAGK--VDYKANEWLMK-NMDPLNDNVAALL 634
Cdd:cd01386 460 LLDEEALYPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 635 HQSTDRLTAEIWKDVegivgleqvsslgdgppggrprrgmfrtVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEkrAGK 714
Cdd:cd01386 540 QESQKETAAVKRKSP----------------------------CLQI-KFQVDALIDTLRRTGLHFVHCLLPQHN--AGK 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 715 LEPR--------------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-----MDGKQACEKM 775
Cdd:cd01386 589 DERStsspaagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEEL 668
|
730 740
....*....|....*....|.
gi 116284396 776 IQALELDPNLYRVGQSKIFFR 796
Cdd:cd01386 669 LEELDLEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
119-796 |
1.83e-111 |
|
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: 370.37 E-value: 1.83e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHVYAVTEGAYRSMLQDREDQ 192
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 193 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST----------------SSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 273 FIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPS-SSPG-QER 350
Cdd:cd14886 145 FIKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 351 ELFQETLESLRVLgFSHEEIISMLRMVSAVLQFGNIALKRERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPR 427
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAqeqg 585
Cdd:cd14886 381 ANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSSCK---- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 586 ghpkfqrpRHLRD---------QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLE 656
Cdd:cd14886 454 --------SKIKNnsfipgkgsQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNM 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 657 QvsslgdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIC 736
Cdd:cd14886 526 K-----------------GKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTI 588
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116284396 737 RQGFPNRILFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14886 589 HRGFAYNDTFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
119-758 |
9.17e-111 |
|
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: 368.79 E-value: 9.17e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHVYAVTEGAYRSMLQDRE--DQSI 194
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 195 LCTGESGAGKTENTKKVIQYLAHVASSPkgrkepgvpASVSTVSYGE-LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 273
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP---------TSWESHKIAErIEQRILNSNPVMEAFGNACTLRNNNSSRFGKF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 274 IRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLtngPSSSPGQERELF 353
Cdd:cd14880 152 IQLQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 354 QETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKV 430
Cdd:cd14880 229 EVTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 431 GRDYV--QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNE 508
Cdd:cd14880 309 GKQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 509 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGGH 587
Cdd:cd14880 389 KLQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGN 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 588 PKFQRPRhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppg 667
Cdd:cd14880 466 PCLGHNK-LSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 668 grPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 747
Cdd:cd14880 538 --QSRAPVLTVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQ 615
|
650
....*....|.
gi 116284396 748 EFRQRYEILTP 758
Cdd:cd14880 616 NFVERYKLLRR 626
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
119-796 |
1.27e-103 |
|
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: 348.34 E-value: 1.27e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHVYAVTEGAYRSM-LQDREDQSIL 195
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 196 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKepgvpaSVSTvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQR------SIAD----KIDENLKWSNPVMESFGNARTVRNDNSSRFGK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 273 FIRINFD-VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPCSHYR-------FLTNGPS 343
Cdd:cd14875 151 YIKLYFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 344 SSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 423
Cdd:cd14875 231 GKTLDDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 424 LtprIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQ 500
Cdd:cd14875 310 L---VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 501 LCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKV 580
Cdd:cd14875 385 LCINYANESLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNL 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 581 AQEQGG-HPKFQRPRH-LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQv 658
Cdd:cd14875 462 WDQWANkSPYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 659 sslgdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 738
Cdd:cd14875 539 ------------------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQ 600
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116284396 739 GFPNRILFQEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE-----LDPNlYRVGQSKIFFR 796
Cdd:cd14875 601 GYPVRRPIEQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
119-753 |
5.22e-102 |
|
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: 345.54 E-value: 5.22e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHVYAVTEGAYRSM 185
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVS-TVSYGELERQLLQANPILEAFGNAKTVKN 264
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISPPaSPSRTTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 265 DNSSRFGKFIRINF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPCSHYRFL 338
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 339 TNGPSSSPG---QERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIAL-----KRERNT--DQATMPDNTAA--- 405
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 406 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 475
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 476 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 549
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 550 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGGHPKFQRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPL 626
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 627 NDNVAALLHQSTDRLTAEIW--KDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCI 704
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 116284396 705 VPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 753
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
120-760 |
2.10e-97 |
|
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: 327.24 E-value: 2.10e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHVYAVTEGAYRSMLQdREDQSILCTGE 199
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHvasspkgrkepgvpasvSTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----------------RTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 vaGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLlepcsHYRFLTnGPSSSPGQERELFQETLES 359
Cdd:cd14898 141 --GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI-----DTSSTA-GNKESIVQLSEKYKMTCSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 360 LRVLGFSHEEIISMLRMvsAVLQFGNIALKRERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 439
Cdd:cd14898 213 MKSLGIANFKSIEDCLL--GILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 440 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 519
Cdd:cd14898 288 TLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 520 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGhpkfqrprHLRDQ 599
Cdd:cd14898 365 RAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIKKYLNG--------FINTK 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 600 AD--FSVLHYAGKVDYKANEWLMKNmdplndnvaallhqsTDRLTAEIWKDvEGIVGLEQVSSLgdgppggrprrgmfrt 677
Cdd:cd14898 433 ARdkIKVSHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-LLINDEGSKEDL---------------- 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 678 vGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 757
Cdd:cd14898 481 -VKYFKDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILG 559
|
...
gi 116284396 758 PNA 760
Cdd:cd14898 560 ITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
119-796 |
2.38e-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: 326.22 E-value: 2.38e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpasvstvsygeLERQLLQANPILEAFGNAKTVKNDNSSRF 270
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG------------LEARLLQSGPVLEAFGNAHTVLNANSSRF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 271 GKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPCSHYRFLTNgpssspgqeR 350
Cdd:cd14887 149 GKMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD---------L 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 351 ELFQETLESLRVLGFSHEEIISMLrmvSAVLQFGNIALKRERNTDQATMPDNTA--------AQKLCRLL-------GLG 415
Cdd:cd14887 218 RRITAAMKTVGIGGGEQADIFKLL---AAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 416 VTDFSRALLT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP 475
Cdd:cd14887 295 VTEASRKHLKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 476 R-------------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI-------- 531
Cdd:cd14887 375 KpsesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsa 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 532 -PWTF-LDFGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQEQGGHPKF 590
Cdd:cd14887 455 fPFSFpLASTLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKY 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 591 --QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLhQSTDRLTAEIwkdvegivgleqvssLGDGPPGG 668
Cdd:cd14887 535 knITPALSRENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLV---------------GSKKNSGV 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 669 RPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 748
Cdd:cd14887 599 RAISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVE 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*...
gi 116284396 749 FRQRYEILTPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 796
Cdd:cd14887 679 LWRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
116-795 |
1.99e-92 |
|
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: 315.26 E-value: 1.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 116 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHVYAVTEGAYRSM 185
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 186 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpasvstvsygeLERQLLQANPILEAFGNAKTVKN 264
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK---------------LSSQISAAEFVLDSFGNAKTLTN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 265 DNSSRFGKFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG--- 341
Cdd:cd14879 144 PNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgch 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 342 --PSSSPGQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI--ALKRERNTDqATMPDNTAA-QKLCRLLGLGV 416
Cdd:cd14879 224 plPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 417 TDFsRALLTPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFE 491
Cdd:cd14879 303 EDL-ETSLTYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 492 ifQL-----NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC 566
Cdd:cd14879 378 --NRsstggNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQT 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 567 -WFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQAD---FSVLHYAGKVDYKANEWLMKNMDPLndnvaallhqSTDRLT 642
Cdd:cd14879 453 rRMPKKTDEQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPDFVN 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 643 aeiwkdvegivgleqvsslgdgppggrprrgMFRTVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 722
Cdd:cd14879 523 -------------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKA 570
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 723 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGKQACEKMIQALELDPNLYRVGQSKIFF 795
Cdd:cd14879 571 QIRSLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
119-796 |
3.09e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 314.83 E-value: 3.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHVYAVTEGAYRSMLQDREDQSIL 195
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 196 CTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstvSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 275
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS----------------SRTTFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 276 INF-DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNG-PSSSPGQERELF 353
Cdd:cd14878 145 LQFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 354 QETL----ESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14878 225 REKLavlkQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYT 506
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 507 NEKLQQLFNHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----F 568
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 569 PK-------ATDKSFVEKVAQEQGGHPKFqrprhlRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDR 640
Cdd:cd14878 453 PKklqslleSSNTNAVYSPMKDGNGNVAL------KDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENV 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 641 LTAEIWKdvegivgleqvSSLGdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLV 720
Cdd:cd14878 527 VINHLFQ-----------SKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYV 581
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116284396 721 LDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 796
Cdd:cd14878 582 SAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
119-796 |
2.10e-84 |
|
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: 291.53 E-value: 2.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpasvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN-----------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIEL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETL 357
Cdd:cd14937 140 DEYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEiDDAKDFGNLM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 358 ESLRVLGFsHEEIISMLRMVSAVLQFGNI---ALKRERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGR 432
Cdd:cd14937 220 ISFDKMNM-HDMKDDLFLTLSGLLLLGNVeyqEIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIAN 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 433 DYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQ 512
Cdd:cd14937 299 QKIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 513 LFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQR 592
Cdd:cd14937 378 IYLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYAS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 593 PRhlRD-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVS-SLGdgppggRP 670
Cdd:cd14937 454 TK--KDiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE-------VSeSLG------RK 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 671 RRGMFRtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIcRQGFPNRILFQEFR 750
Cdd:cd14937 519 NLITFK-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFL 592
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 116284396 751 QRYEILTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 796
Cdd:cd14937 593 SYFEYLDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
119-748 |
7.51e-81 |
|
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: 282.57 E-value: 7.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHVYAVTEGAYRSMLQDRE 190
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 191 DQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepgvpasvstVSYGELERQLLQANPILEAFGNAKTVKNDNSSRF 270
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTD---------------SQMTERIDKLIYINNILESMSNATTIKNNNSSRC 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 271 GKFIRINFD---------VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPCSHYRFL-- 338
Cdd:cd14884 146 GRINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnp 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 339 ------------------TNGPSSSPGQEREL-FQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKrerntdqatm 399
Cdd:cd14884 226 deshqkrsvkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK---------- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 400 pdntAAqklCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-------- 471
Cdd:cd14884 296 ----AA---AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekde 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 472 ---DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDL 548
Cdd:cd14884 369 sdnEDIYSINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIF 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 549 IERpanppgLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGGHPKFQRPRHLRDQAD---------FSVLHYAG 609
Cdd:cd14884 448 IAK------IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYGFVLNHDADGTAkkqnikkniFFIRHYAG 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 610 KVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpPGGRPRRGMFRTVGQLYKESLSRL 689
Cdd:cd14884 522 LVTYRINNWIDKNSDKIETSIETLISCSSNRFLRE---------------------ANNGGNKGNFLSVSKKYIKELDNL 580
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 116284396 690 MATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 748
Cdd:cd14884 581 FTQLQSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
120-795 |
1.06e-70 |
|
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: 251.19 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHVYA-------VTEGAYRSMLQDREDQ 192
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 193 SILCTGESGAGKTENTKKVIQYLAHVASspkgrkepGVPASvstvsygELERQLLQANPILEAFGNAKTVKNDNSSRFGK 272
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAG--------GGPET-------DAFKHLAAAFTVLRSLGSAKTATNSESSRIGH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 273 FIRINFdVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCS--HYRFLTNGPSSSPGQER 350
Cdd:cd14881 135 FIEVQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 351 EL-FQETLESLRVLGFSHEEIIsmlRMVSAVLQFGNIALKrERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIK 429
Cdd:cd14881 214 AArFQAWKACLGILGIPFLDVV---RVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHN 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 430 VGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQL 501
Cdd:cd14881 290 ARGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 502 CINYTNEKLQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKV 580
Cdd:cd14881 366 CINLCAETMQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKI 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 581 AQEQGGHPKFQRPRHLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQstdrltaeiwkdvegivgleQVSS 660
Cdd:cd14881 442 KVQHRQNPRLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------------QNCN 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 661 LGdgppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGF 740
Cdd:cd14881 501 FG------------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGY 568
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116284396 741 PNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL-------YRVGQSKIFF 795
Cdd:cd14881 569 PHRMRFKAFNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
119-761 |
3.42e-68 |
|
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: 243.62 E-value: 3.42e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 119 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHVYAVTEGAYRSMLQDRED-QSILCT 197
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 198 GESGAGKTENTKKVIQYLAhvaSSPKgrkepgvpASVSTVSYGELERqllqanpILEAFGNAKTVKNDNSSRFGKFIRIN 277
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPK--------SKVTTKHSSAIES-------VFKSFGCAKTLKNDEATRFGCSIDLL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 278 FDvAGYIVGANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQER-ELFQE 355
Cdd:cd14874 133 YK-RNVLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 356 TLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKV 430
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSED 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 431 GrdyvqKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKL 510
Cdd:cd14874 290 G-----TTIDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 511 QQLFNHTMFVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPK 589
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 590 FQRPRHlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSslgdgppggr 669
Cdd:cd14874 441 YGKARN-KERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS---------- 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 670 prrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 749
Cdd:cd14874 510 --------QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
650
....*....|..
gi 116284396 750 RQRYEILTPNAI 761
Cdd:cd14874 582 ARQYRCLLPGDI 593
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
120-756 |
4.63e-68 |
|
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: 243.49 E-value: 4.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGE 199
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 200 SGAGKTENTKKVIQYLAHVasspkGRKEPGVPASVstvsygelerqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 279
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYL-----GDGNRGATGRV------------ESSIKAILALVNAGTPLNADSTRCILQYQLTFG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 280 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPCSHYRFLTNGPSSSPGQER------- 350
Cdd:cd14882 145 STGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpe 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 351 ---ELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIALKreRNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPR 427
Cdd:cd14882 224 gnvERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFR--QNGGYAELENTEIASRVAELLRLDEKKFMWALTNYC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 428 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINY 505
Cdd:cd14882 302 LIKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNT 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 506 TNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQ 584
Cdd:cd14882 382 LNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKH 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 585 GGHPKfqrprhLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSLgdg 664
Cdd:cd14882 457 SQFVK------KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM--- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 665 ppggrprrgmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGF 740
Cdd:cd14882 521 -----------RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGF 589
|
650
....*....|....*.
gi 116284396 741 PNRILFQEFRQRYEIL 756
Cdd:cd14882 590 SYRIPFQEFLRRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
120-796 |
2.74e-65 |
|
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: 236.14 E-value: 2.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLahvasspkgrkepgVPASVSTVSYgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 278
Cdd:cd14905 80 ESGSGKSENTKIIIQYL--------------LTTDLSRSKY--LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 279 DVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQ--ERELFQET 356
Cdd:cd14905 144 SLYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 357 LESLRVLGFSHEEIISMLRMVSAVLQFGNIALKRERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 436
Cdd:cd14905 224 KMSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 437 KAqtkeqadfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 516
Cdd:cd14905 302 NR----------DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQ 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 517 TMFVLEQEEYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGGHPKF-QRPR 594
Cdd:cd14905 370 TVLKQEQREYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFgKKPN 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 595 hlrdqaDFSVLHYAGKVDYKANEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDvEGIVGLEQVSSlgdgppggrPRRGM 674
Cdd:cd14905 443 ------KFGIEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSR-DGVFNINATVA---------ELNQM 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 675 FRTVGQLYKESLS--RLMATLSNTNPS-----------------------------------------------FVRCIV 705
Cdd:cd14905 504 FDAKNTAKKSPLSivKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfhFIRCIK 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 706 PNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMIQALE 780
Cdd:cd14905 584 PNSKKTHLTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDINIDS 657
|
730
....*....|....*.
gi 116284396 781 LDPNLYRVGQSKIFFR 796
Cdd:cd14905 658 ILPPPIQVGNTKIFLR 673
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
122-754 |
4.84e-63 |
|
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: 231.01 E-value: 4.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 122 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHVYAVTEGAYRSMLQDRED 191
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 192 QSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEpGVPASVSTVSYGElerQLLQANPILEAFGNAKTVKNDNSSRFG 271
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETEPRPD-SEGASGVLHPIGQ---QILHAFTILEAFGNAATRQNRNSSRFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 272 KFIRINFDVAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ--LKADLLLEPCSH-YRFLTNGP--SSSP 346
Cdd:cd14893 160 KMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDptLRDSLEMNKCVNeFVMLKQADplATNF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 347 GQERELFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNIAL-------KRERNTDQATMPDNTAaqklCRLLGLGVTDF 419
Cdd:cd14893 240 ALDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggKSVGGANSTTVSDAQS----CALKDPAQILL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 420 SRALLTPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPR--- 476
Cdd:cd14893 316 AAKLLEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKsni 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 477 ----QGasfLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQ 543
Cdd:cd14893 396 vinsQG---VHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 544 PCIDLIERPanPPGLLALLDEECWFPKATDKSFVEK---VAQEQGGhpkFQRPRHLRDQAD------------FSVLHYA 608
Cdd:cd14893 473 KCLQLFEDK--PFGIFDLLTENCKVRLPNDEDFVNKlfsGNEAVGG---LSRPNMGADTTNeylapskdwrllFIVQHHC 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 609 GKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkDVEGIVGLEQVSSL-----GDGPPGGRPRRGMFRTVGQLYK 683
Cdd:cd14893 548 GKVTYNGKGLSSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAAssekaAKQTEERGSTSSKFRKSASSAR 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 684 ESLS--------------RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEF 749
Cdd:cd14893 620 ESKNitdsaatdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHF 699
|
....*
gi 116284396 750 RQRYE 754
Cdd:cd14893 700 FRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
141-283 |
9.90e-59 |
|
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: 200.26 E-value: 9.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 141 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 219
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116284396 220 SSPKGRKEPGVPASVsTVSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGY 283
Cdd:cd01363 81 FNGINKGETEGWVYL-TEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
120-794 |
3.17e-53 |
|
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: 200.83 E-value: 3.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 120 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 198
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 199 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPASVSTVSYGELERQ---------LLQANPILEAFGNAKTVKNDNSSR 269
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKG--SRRLPTNLNDQEEDNIHNEENTdyqfnmsemLKHVNVVMEAFGNAKTVKNNNSSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 270 FGKFIRINFDvAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQE 349
Cdd:cd14938 160 FSKFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 350 RE-LFQETLESLRVLGFSHEEIISMLRMVSAVLQFGNI---------ALKRERNTDQATMPDNTAAQKL----------- 408
Cdd:cd14938 239 YSgKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTeivkafrkkSLLMGKNQCGQNINYETILSELensediglden 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 409 -------CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 479
Cdd:cd14938 319 vknlllaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 480 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 559
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 560 ALLDEECwFPKATDKSFVEKVAQEQGGH-PKF-QRPRHLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQS 637
Cdd:cd14938 477 SLLENVS-TKTIFDKSNLHSSIIRKFSRnSKYiKKDDITGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 638 TDRLTAEIWK----DVEGIVGLEQ-----VSSLGDGPPGGRPRRGMFRTvgqLYKESLSRLMATLSNTNPSFVRCIVPNH 708
Cdd:cd14938 556 ENEYMRQFCMfynyDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 709 EKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipkgfmDGKQACEKMIQALELDPNLYR 787
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 116284396 788 VGQSKIF 794
Cdd:cd14938 705 IGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1192-1822 |
1.46e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 122.35 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1192 ELRSKREQEVTELKKTLEEETRIhEAAVQELRQRhgqaLGELAEQLEQARRGKG-AWEKTRLALEA---EVSELRAELSS 1267
Cdd:COG1196 169 KYKERKEEAERKLEATEENLERL-EDILGELERQ----LEPLERQAEKAERYRElKEELKELEAELlllKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1268 LQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQE 1347
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1348 LLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAE 1427
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1428 ALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraeaegreRE 1507
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA---------------EL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1508 ARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAAnDLRAQVTELEDELTAAEDAK 1587
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVA-VLIGVEAAYEAALEAALAAA 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1588 LRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEE 1667
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1668 AVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNL 1747
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116284396 1748 SKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERsfsAKAESGRQQLERQIQEL 1822
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL---EELERELERLEREIEAL 779
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
125-737 |
7.60e-26 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 116.38 E-value: 7.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 125 LRERYYSGLIYTYSGLFCV-VINPYKQL------PIYTEAIVEMYRGKKRHE--VPPHVYAV------------------ 177
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIakqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 178 --TEGAYRSMLQDReDQSILCTGESGAGKTENTKKVIQYLAHVASSP--KGRKE----------PGVPASVST------- 236
Cdd:cd14894 87 psTISSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAQPAlsKGSEEtckvsgstrqPKIKLFTSStkstiqm 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 237 ----------------------------------------------------------VSYGELERQL------------ 246
Cdd:cd14894 166 rteeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekLEHLEDEEQLrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 247 ----LQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDVAGY---IVGANIETYLLEKSRAIRQA------KDECSFHI 311
Cdd:cd14894 246 lsivLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 312 FYQLLGGAG-----EQLKADLLLE--PCSHYRFLTNGPSSSPG---------QERELFQETLESLRVLGFSHEEIISMLR 375
Cdd:cd14894 326 LYAMVAGVNafpfmRLLAKELHLDgiDCSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 376 MVSAVLQFGNIALKRERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALE 449
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 450 ALAKATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQql 513
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY-- 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 514 fnhtmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQE 583
Cdd:cd14894 564 ---------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDR 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 584 QGGH-PKFQR-----PRH---LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GI 652
Cdd:cd14894 635 NSSRlPEPPRvlsnaKRHtpvLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlGW 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 653 VGLEQVSSLGDGPPGGRPRRGMfrtVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 732
Cdd:cd14894 715 SPNTNRSMLGSAESRLSGTKSF---VGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 116284396 733 IRICR 737
Cdd:cd14894 791 MEICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1076-1708 |
6.01e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 113.88 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1076 QELEKLKRRLDGESSELQEQmvEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE 1155
Cdd:COG1196 216 RELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1156 RVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAE 1235
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1236 QLEQARRGKGAWEKtRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELE 1315
Cdd:COG1196 374 LAEAEEELEELAEE-LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1316 NVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQ 1395
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1396 AQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKtETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQ 1475
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR-ATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1476 RKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddvgksvhel 1555
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE------------- 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1556 eracRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEErK 1635
Cdd:COG1196 679 ----AELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA-L 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1636 QRTLAVAARKKLEGELEELKAQMASAG-------QGKEEAVKQLRKMQAQMKELWREVEETRTSREEIfsqNRESEKRLK 1708
Cdd:COG1196 754 EELPEPPDLEELERELERLEREIEALGpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEEI---DRETRERFL 830
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
900-1467 |
1.41e-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: 1.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 900 VGELQGRVAQLEEErARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEEEEcsRQMQTEKKRLQQHIQE 979
Cdd:COG1196 195 LGELERQLEPLERQ-AEKAERYR--------------ELKEELKELEAELLLLKLRELEAEL--EELEAELEELEAELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 980 LEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEA 1059
Cdd:COG1196 258 LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1060 TIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLR 1139
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1140 EAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV 1219
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1220 QELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVS---ELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDG 1296
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaalEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1297 ERARAEAAEKLQRAQAELENVSGALNEAEsktirlskELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQ 1376
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVAS--------DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1377 LEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDD 1456
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570
....*....|.
gi 116284396 1457 ATMDLEQQRQL 1467
Cdd:COG1196 730 LEAEREELLEE 740
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1159-1737 |
4.83e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 110.80 E-value: 4.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1159 RTKAEKqRRDLGEELEALRGELE-DTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQL 1237
Cdd:COG1196 209 AEKAER-YRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1238 EQARRgkgawektrlaLEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV 1317
Cdd:COG1196 288 AEEYE-----------LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1318 SGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLeeeaaareragrelQTAQAQ 1397
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL--------------ERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1398 LSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRK 1477
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1478 FDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDdvGKSVHELER 1557
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1558 ACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQR 1637
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1638 TLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRL 1717
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
570 580
....*....|....*....|
gi 116284396 1718 QEELAASDRARRQAQQDRDE 1737
Cdd:COG1196 741 LLEEEELLEEEALEELPEPP 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1002-1723 |
1.36e-22 |
|
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: 106.29 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1002 EAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKL 1081
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1082 KRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTK 1161
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1162 AEKQRRDLGEELEALRGELEDTldSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRqRHGQALGELAEQLEQAR 1241
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERL--QQEIEELLKKLEEAELKELQAELEELEEELEELQEELE-RLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1242 RgkgawekTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERA--RAEAAEKLQRAqaeLENVSG 1319
Cdd:TIGR02168 475 Q-------ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLseLISVDEGYEAA---IEAALG 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1320 AlneaesktiRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLS 1399
Cdd:TIGR02168 545 G---------RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1400 EW-------RRRQEEEAGALEAGEEARRRAA---------REAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQ 1463
Cdd:TIGR02168 616 KAlsyllggVLVVDDLDNALELAKKLRPGYRivtldgdlvRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1464 QRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLS 1543
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1544 SKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEERRRQLAKQL 1623
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA-ATERRLEDLEEQIEELSEDI 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1624 RDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIfsqnres 1703
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL------- 927
|
730 740
....*....|....*....|
gi 116284396 1704 EKRLKGLEAEVLRLQEELAA 1723
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
993-1898 |
3.29e-22 |
|
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: 105.14 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 993 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLskERKLleDRLAEFSSQAAEEEEKVKSLNKLRLKYEAtiadmeDRLRKEE 1072
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNEL--ERQL--KSLERQAEKAERYKELKAELRELELALLV------LRLEELR 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1073 KGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL 1152
Cdd:TIGR02168 239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1153 ESERVARTKAEKQRRDLGEELEALRGELEDTldstnaqqelrskrEQEVTELKKTLEEEtrihEAAVQELRQRhgqaLGE 1232
Cdd:TIGR02168 319 EELEAQLEELESKLDELAEELAELEEKLEEL--------------KEELESLEAELEEL----EAELEELESR----LEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1233 LAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQ-----TARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKL 1307
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEdrrerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1308 QRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEetraKLALGSRVRAMEAEA---AGLREQLEEEAAAR 1384
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALLKNQsglSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1385 ERAGRELQTA-----QAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATM 1459
Cdd:TIGR02168 533 EGYEAAIEAAlggrlQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1460 DLE-------QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnr 1532
Cdd:TIGR02168 613 KLRkalsyllGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILER----------------- 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1533 alRAELEallsskdDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRDEAG 1612
Cdd:TIGR02168 676 --RREIE-------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR-LEAEVEQL 745
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1613 EERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTS 1692
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1693 REEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVAngnlskaAILEEKRQLEGRLgqleeelee 1772
Cdd:TIGR02168 826 LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE-------ALLNERASLEEAL--------- 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1773 eqsnsELLNDRYRKLLLQVESLttelsaersfsakaESGRQQLERQIQELRGRLGEEDAgARARHKMTIAALESKLAqAE 1852
Cdd:TIGR02168 890 -----ALLRSELEELSEELREL--------------ESKRSELRRELEELREKLAQLEL-RLEGLEVRIDNLQERLS-EE 948
|
890 900 910 920
....*....|....*....|....*....|....*....|....*.
gi 116284396 1853 EQLEQETrerilsgklvrrAEKRLKEVVLQVEEERRVADQLRDQLE 1898
Cdd:TIGR02168 949 YSLTLEE------------AEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1300-1912 |
5.26e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1300 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKElsstEAQLHDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQle 1378
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLEPLERQ----AEKAERYRELKEELKELEAELlLLKLRELEAELEELEAE-- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1379 eeaaareragreLQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1458
Cdd:COG1196 248 ------------LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1459 MDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1538
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1539 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRrQ 1618
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA-L 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1619 LAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFS 1698
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1699 QNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE--MADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1776
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1777 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1856
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1857 QETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLE 1912
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELE 770
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
879-1407 |
5.31e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 104.25 E-value: 5.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 879 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGE 958
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 959 EEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS 1038
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1039 QAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQ 1118
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1119 AALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQR----------------RDLGEELEALRGEL-- 1180
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlagavavligveaayeAALEAALAAALQNIvv 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1181 EDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARrgkgawektRLALEAEVSE 1260
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADAR---------YYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1261 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1340
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116284396 1341 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE 1407
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1156-1955 |
4.27e-21 |
|
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: 101.29 E-value: 4.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1156 RVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKTLEEETRIhEAAVQ 1220
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEELQEE-LKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1221 ELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERAR 1300
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1301 AEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA-------KLALGSRVRAMEAEAAGL 1373
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlelqIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1374 REQLEEEAAARERAGRELQTAQaqLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQE 1453
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1454 LDDATMDLEQQRQL---VSTLEKKQRKF--------DQLLAEEK-----AAVLRAVEERERAEAEGREREARAlSLTRAL 1517
Cdd:TIGR02168 491 LDSLERLQENLEGFsegVKALLKNQSGLsgilgvlsELISVDEGyeaaiEAALGGRLQAVVVENLNAAKKAIA-FLKQNE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1518 EEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAK-LRLEVTVQA 1596
Cdd:TIGR02168 570 LGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKkLRPGYRIVT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1597 LktqhERDLQGRD--EAGEERRRQLAKQLRDAEVERDEERKQR-----TLAVAARKKLEGELEELKAQMASAGQGKEEAV 1669
Cdd:TIGR02168 650 L----DGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEEleekiAELEKALAELRKELEELEEELEQLRKELEELS 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1670 KQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVangNLSK 1749
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL---KALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1750 AAILEEKRQLEgrlgqleeeleeeqsnseLLNDRYRKLLLQVESLTTELSAersfsakaesgrqqLERQIQELRGRLGEE 1829
Cdd:TIGR02168 803 EALDELRAELT------------------LLNEEAANLRERLESLERRIAA--------------TERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1830 dAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1909
Cdd:TIGR02168 851 -SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 116284396 1910 QLEEAEEEASR-AQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:TIGR02168 930 RLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1530-2000 |
3.54e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.00 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1530 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERdLQGRD 1609
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1610 EAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEET 1689
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1690 RTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEE 1769
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1770 LEEEQSNSELLNDRYRKLLLQVESLT----TELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALE 1845
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAarllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1846 SKLAQaEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR--VKQLKRQLEEAEEEASRAQA 1923
Cdd:COG1196 545 AAALQ-NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlVASDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1924 GRRRLQRELEDVTESAESMN---REVTTLRNRLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQPGSGPSPEPEGSPPA 2000
Cdd:COG1196 624 GRTLVAARLEAALRRAVTLAgrlREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1030-1760 |
7.26e-18 |
|
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: 90.90 E-value: 7.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1030 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEaTIADMEDRLRKEE-----KGRQELEKLKRRLDGESSELQEQMVEQQQRAE 1104
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTEEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1105 ELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTK-AEKQRRDLGEELEALRGELEDT 1183
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAEERLAKLEAEIDKLLAEIEEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1184 LDSTNAQQELRSKREQEVTELKKTLEE-ETRIHE--AAVQELRQRHGQalgeLAEQLEQARRGKGAWEKTRLALEAEVSE 1260
Cdd:TIGR02169 342 EREIEEERKRRDKLTEEYAELKEELEDlRAELEEvdKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1261 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEA 1340
Cdd:TIGR02169 418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEA 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1341 QLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEE-EAAARERAGRELQ--------TAQAQLSEWRRRQEEEAGA 1411
Cdd:TIGR02169 498 QARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERyATAIEVAAGNRLNnvvveddaVAKEAIELLKRRKAGRATF 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1412 LEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATM--DLEQQRQLVS-----TLEKKqrkfdqlLAE 1484
Cdd:TIGR02169 578 LPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRLMGkyrmvTLEGE-------LFE 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1485 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQ 1564
Cdd:TIGR02169 651 KSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1565 AANDLRAQVTELEDELTAAEDAKLRLEVTVQAL---KTQHERDL-QGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLA 1640
Cdd:TIGR02169 731 EEEKLKERLEELEEDLSSLEQEIENVKSELKELearIEELEEDLhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRI 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1641 VAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQ-------NRESEKRLKGLEAE 1713
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEleeleaaLRDLESRLGDLKKE 890
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 116284396 1714 VLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1760
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
960-1760 |
2.25e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 960 EECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RKLLEDRLAE 1035
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1036 FSSQA-----AEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEklkrrldgesselqEQMVEQQQRAEELRaql 1110
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAED--------------AKKAEAVKKAEEAK--- 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1111 gRKEEELQaalaRAEDEggaraqllkSLREAQAALAEAQEDLESERVARTKAEKQRRdlgeelealRGELEDTLDSTNAQ 1190
Cdd:PTZ00121 1237 -KDAEEAK----KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1191 QELRSKREQEVTELKKTLEEETRIHEAAVQ-ELRQRHGQALGELAEQLEQARRGKGAWEKTRlALEAEVSELRAELSSLQ 1269
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAA-ADEAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1270 TARQEGEQRrrrlELQLQEVQGRAGDGERARAE----AAEKLQRAQAELENVSGALNEAESKtiRLSKELSSTEAQLHDA 1345
Cdd:PTZ00121 1373 KEEAKKKAD----AAKKKAEEKKKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1346 QELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAARE 1425
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1426 AealtqRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLraveereraEAEGRE 1505
Cdd:PTZ00121 1527 A-----KKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA---------KKAEEA 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1506 REARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAED 1585
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE 1672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1586 AKLRLEVTVQALKTQHERDLQGRDEAGEER-----RRQLAKQLRDAEVERDEERKQRTLAVAARKklEGELEELKAQMAS 1660
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKK--EAEEDKKKAEEAK 1750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1661 AGQGKEEAVKQLRKMQAQMKELWREVEET---RTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDE 1737
Cdd:PTZ00121 1751 KDEEEKKKIAHLKKEEEKKAEEIRKEKEAvieEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDS 1830
|
810 820
....*....|....*....|...
gi 116284396 1738 MADEVAngnLSKAAILEEKRQLE 1760
Cdd:PTZ00121 1831 AIKEVA---DSKNMQLEEADAFE 1850
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1613-1923 |
3.76e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 3.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1613 EERRRQLAKQLRDA----EVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEE 1688
Cdd:COG1196 199 ERQLEPLERQAEKAeryrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1689 TRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEE 1768
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1769 ELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRlgeedagaRARHKMTIAALESKL 1848
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER--------LERLEEELEELEEAL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116284396 1849 AQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQA 1923
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
870-1481 |
9.41e-17 |
|
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: 87.05 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 870 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVV 949
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 950 SELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLL 1029
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1030 EDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLD---GESSELQEQMVEQQQRAEEL 1106
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEervRGGRAVEEVLKASIQGVHGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1107 RAQLGRKEEELQAALARA----------EDEGGARA--QLLKSLREAQAA----LAEAQEDLESERVARTKAEKQRRDLG 1170
Cdd:TIGR02169 527 VAQLGSVGERYATAIEVAagnrlnnvvvEDDAVAKEaiELLKRRKAGRATflplNKMRDERRDLSILSEDGVIGFAVDLV 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1171 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV----QELRQRHGQALGELAEqLEQARRGKGA 1246
Cdd:TIGR02169 607 EFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggsRAPRGGILFSRSEPAE-LQRLRERLEG 685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1247 WEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1326
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1327 KTIRLSKELSSTEAQL-----HDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEW 1401
Cdd:TIGR02169 766 RIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1402 -------RRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTL-EK 1473
Cdd:TIGR02169 846 keqiksiEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkAK 925
|
....*...
gi 116284396 1474 KQRKFDQL 1481
Cdd:TIGR02169 926 LEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
871-1485 |
1.51e-16 |
|
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: 86.26 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 871 QVTRQDEVLQARAQEL-QKVQELQQQSAR---EVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELE 946
Cdd:TIGR02168 313 NLERQLEELEAQLEELeSKLDELAEELAEleeKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 947 LVVSELEARVGEEEecSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER 1026
Cdd:TIGR02168 393 LQIASLNNEIERLE--ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1027 KLLEDRLAEFSSQAAEEEEKVKSLNklrlkyeatiaDMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEEL 1106
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLE-----------RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1107 RAQLG---------RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEkqrrDLGEELEALR 1177
Cdd:TIGR02168 540 EAALGgrlqavvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK----DLVKFDPKLR 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1178 GELE---------DTLDSTNAQQEL----------------------------------RSKREQEVTELKKTLEEETRI 1214
Cdd:TIGR02168 616 KALSyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssileRRREIEELEEKIEELEEKIAE 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1215 HEAAVQELRQrhgqALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAG 1294
Cdd:TIGR02168 696 LEKALAELRK----ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1295 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR 1374
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1375 EQLEEEAAARERAGRELQTAQAQLSEW--RRRQEEEAGALEAGEEARrraareaeaLTQRLAEKTETVDRLERGRRRLQQ 1452
Cdd:TIGR02168 852 EDIESLAAEIEELEELIEELESELEALlnERASLEEALALLRSELEE---------LSEELRELESKRSELRRELEELRE 922
|
650 660 670
....*....|....*....|....*....|...
gi 116284396 1453 ELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEE 1485
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1550-1955 |
2.16e-14 |
|
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: 79.45 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1550 KSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAgEERRRQLAKQLRDAEVE 1629
Cdd:pfam01576 201 KGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNA-LKKIRELEAQISELQED 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1630 RDEERKQRTLAVAARKKLEGELEELKAQMASAgQGKEEAVKQLR-KMQAQMKELWREVEETRTSREEIFSQNRESEKR-L 1707
Cdd:pfam01576 280 LESERAARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQaL 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1708 KGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKL 1787
Cdd:pfam01576 359 EELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1788 LLQVESLTTELSAERSFSAKAESGRQQLERQIQELRgRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGK 1867
Cdd:pfam01576 439 QSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQ-ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1868 LVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVT 1947
Cdd:pfam01576 518 QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVS 597
|
....*...
gi 116284396 1948 TLRNRLRR 1955
Cdd:pfam01576 598 NLEKKQKK 605
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1569-1984 |
2.65e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1569 LRAQVTELEDEltaAEDAKLRLEVTVQALKTQHERDLQgrdeageeRRRQLAKQLRDAEVERDEERKQRTLAVAARKKLE 1648
Cdd:COG1196 198 LERQLEPLERQ---AEKAERYRELKEELKELEAELLLL--------KLRELEAELEELEAELEELEAELEELEAELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1649 GELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRAR 1728
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1729 RQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKA 1808
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1809 ESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1888
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1889 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAqAGRRRLQRELEDVTESAESMNREVTTLRNRlRRGPLTFTTRTVRQV 1968
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA-LEAALAAALQNIVVEDDEVAAAAIEYLKAA-KAGRATFLPLDKIRA 584
|
410
....*....|....*.
gi 116284396 1969 FRLEEGVASDEEAEEA 1984
Cdd:COG1196 585 RAALAAALARGAIGAA 600
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
882-1490 |
3.32e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.03 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 882 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSEL----EARV 956
Cdd:PTZ00121 1183 KAEEVRKAEELRKaEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeEARM 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 957 GEEEECSRQMQTEKKRLQQHIQELEAHLEAEEG--ARQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRL 1033
Cdd:PTZ00121 1263 AHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKKKAEeAKKADEAKKKAEEAKKKADAAKKKAEEAK 1342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1034 AEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgeSSELQEQMVEQQQRAEELRAqlgRK 1113
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKK---AA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1114 EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERvartKAEKQRRDLGEELEAlrGELEDTLDSTNAQQEL 1193
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KAEEAKKKAEEAKKA--DEAKKKAEEAKKADEA 1488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1194 RSKREQ---EVTELKKTLEEETRIHEA-------AVQELRQRHGQALGELAEQLEQARRG---KGAWEKTRLALEAEVSE 1260
Cdd:PTZ00121 1489 KKKAEEakkKADEAKKAAEAKKKADEAkkaeeakKADEAKKAEEAKKADEAKKAEEKKKAdelKKAEELKKAEEKKKAEE 1568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1261 LRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGAlnEAESKTIRLSKELSSTEA 1340
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEAEEK 1646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1341 QlhDAQELLQEETRAKLALGSRVRAMEAEaaglreqleeeaAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARR 1420
Cdd:PTZ00121 1647 K--KAEELKKAEEENKIKAAEEAKKAEED------------KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1421 RAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDlEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1490
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1300-1985 |
5.22e-14 |
|
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: 78.17 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1300 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEaqlhDAQELLQEETRAKLAL-GSRVRAMEAEAAGLREQLE 1378
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1379 EEAAARERAGRELQTAQAQLSEWRRRQEEeagaleageearrrAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAt 1458
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSE--------------LEEEIEELQKELYALANEISRLEQQKQILRERLANL- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1459 mdLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsLTRALEEEQEAREELERQNRALRAEL 1538
Cdd:TIGR02168 315 --ERQLEELEAQLEELESKLDELAEELAE-------------------------LEEKLEELKEELESLEAELEELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1539 EALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHER----DLQGRDEAGEE 1614
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaelkELQAELEELEE 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1615 RRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEavkqLRKMQAQMKELWreveetrtsre 1694
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQEN----LEGFSEGVKALL----------- 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1695 eifsQNRESEKRLKGLEAEVLRLQEE----LAASDRARRQAQQDRDEMADEVA-----NGNLSKAAILEEK----RQLEG 1761
Cdd:TIGR02168 513 ----KNQSGLSGILGVLSELISVDEGyeaaIEAALGGRLQAVVVENLNAAKKAiaflkQNELGRVTFLPLDsikgTEIQG 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1762 RLGQLEEELEEEQSNSELL---NDRYRKLL-------LQVESLTT------ELSAERSF-----------------SAKA 1808
Cdd:TIGR02168 589 NDREILKNIEGFLGVAKDLvkfDPKLRKALsyllggvLVVDDLDNalelakKLRPGYRIvtldgdlvrpggvitggSAKT 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1809 ESGRQQLERQIQELRGRLgEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERR 1888
Cdd:TIGR02168 669 NSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1889 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQV 1968
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
730
....*....|....*..
gi 116284396 1969 FRLEEGVASDEEAEEAQ 1985
Cdd:TIGR02168 828 SLERRIAATERRLEDLE 844
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
998-1878 |
6.42e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 77.70 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 998 KVTTEAKMKKFEEDLLLLEDqnSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQE 1077
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEE--AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1078 -LEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESER 1156
Cdd:pfam02463 220 eLEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1157 VARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRhgqaLGELAEQ 1236
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE----EEEEEELEKL----QEKLEQL 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1237 LEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEvqgRAGDGERARAEAAEKLQRAQAELEN 1316
Cdd:pfam02463 372 EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKE---EKKEELEILEEEEESIELKQGKLTE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1317 VSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEA-----------EAAGLREQLEEEAAARE 1385
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQkeskarsglkvLLALIKDGVGGRIISAH 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1386 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLE--- 1462
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaql 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1463 QQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL 1542
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1543 SSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELT------AAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERR 1616
Cdd:pfam02463 689 LAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVqeaqdkINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1617 RQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMasagqgKEEAVKQLRKMQAQMKELWREVEETRTSREEI 1696
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL------KEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1697 FsqnrESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSN 1776
Cdd:pfam02463 843 K----EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1777 SELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLE 1856
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900
....*....|....*....|...
gi 116284396 1857 QETRERI-LSGKLVRRAEKRLKE 1878
Cdd:pfam02463 999 RLEEEKKkLIRAIIEETCQRLKE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
940-1242 |
1.82e-13 |
|
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: 76.25 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 940 ARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKL---QLEKVTTEAKMKKFEEDLLLLE 1016
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLARLEAEVEQLEERIAQLS 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1017 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLnklrlkyEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQE-- 1094
Cdd:TIGR02168 754 KELTELEAEIEELEERLEEAEEELAEAEAEIEEL-------EAQIEQLKEELKALREALDELRAELTLLNEEAANLRErl 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1095 -----QMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDL 1169
Cdd:TIGR02168 827 eslerRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1170 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARR 1242
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1151-1969 |
4.90e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1151 DLESERVARTKAEkqRRDLGEELEALRGELEDtldstNAQQELRSKREQEVTELKKTLEEETRIHEA--AVQELRQRHGQ 1228
Cdd:PTZ00121 1049 DEDIDGNHEGKAE--AKAHVGQDEGLKPSYKD-----FDFDAKEDNRADEATEEAFGKAEEAKKTETgkAEEARKAEEAK 1121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1229 ALGELAEQLEQARRGkgawEKTRLALEAEVSELRAELSSLQTARqegeqrrrrlELQLQEVQGRAGDGERAR-AEAAEKL 1307
Cdd:PTZ00121 1122 KKAEDARKAEEARKA----EDARKAEEARKAEDAKRVEIARKAE----------DARKAEEARKAEDAKKAEaARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1308 QRAQaELENVSGALNEAESKtiRLSKELSSTEAQLHDAQELLQEETRAKLAlgsRVRAMEAEAAGLREQLEEEAAARERA 1387
Cdd:PTZ00121 1188 RKAE-ELRKAEDARKAEAAR--KAEEERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1388 GRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAtmdleqqRQL 1467
Cdd:PTZ00121 1262 MAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA-------DAA 1334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1468 VSTLEKKQRKFDQLLAEEKAAvlraveereraeaegrerearalsltraleeeQEAREELERQNRALRAELEALLSSKDD 1547
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAA--------------------------------ADEAEAAEEKAEAAEKKKEEAKKKADA 1382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1548 VGKSVHELERACRVAEQAANDLRA--QVTELEDELTAAEDAKLRLEVTVQA----LKTQHERDLQGRDEAGEERRRQLAK 1621
Cdd:PTZ00121 1383 AKKKAEEKKKADEAKKKAEEDKKKadELKKAAAAKKKADEAKKKAEEKKKAdeakKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1622 QLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVK--QLRKMQAQMK-ELWREVEETRTSREEifs 1698
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKadEAKKAEEAKKaDEAKKAEEAKKADEA--- 1539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1699 qnRESEKRLKgleAEVLRLQEELAASDRARRQAQQDRDEmadEVANGNLSKAAIL---EEKRQLEGRLGQLEEELEEEQS 1775
Cdd:PTZ00121 1540 --KKAEEKKK---ADELKKAEELKKAEEKKKAEEAKKAE---EDKNMALRKAEEAkkaEEARIEEVMKLYEEEKKMKAEE 1611
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1776 NSELLNDRyrkllLQVESLTTElSAERSFSAKAESGRQQLERQIQELRGRlgEEDAGARARHKMTIAALESKlaQAEEQL 1855
Cdd:PTZ00121 1612 AKKAEEAK-----IKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKK--KAEEAK 1681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1856 EQETRERILSGKLVRRAE--KRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR----------QLEEAEEEASRAQA 1923
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKeaeedkkkaeEAKKDEEEKKKIAH 1761
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 116284396 1924 GRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 1969
Cdd:PTZ00121 1762 LKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
898-1261 |
1.09e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 898 REVGELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHI 977
Cdd:TIGR02168 677 REIEELEEKIEELEEKIAELEKALA--------------ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 978 QELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKY 1057
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1058 EATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE---LQAALARAEDEGGARAQL 1134
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNErasLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1135 LKSLREAQAALAEAQEDLESERVA-RTKAEKQRRDLGEELEALRGELEDTLD----STNAQQELRSKREQEVTELKKTLE 1209
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQlELRLEGLEVRIDNLQERLSEEYSLTLEeaeaLENKIEDDEEEARRRLKRLENKIK 982
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 116284396 1210 EETRIHEAAVQELRQRHGQaLGELAEQLEQARRGKGAWEKTRLALEAEVSEL 1261
Cdd:TIGR02168 983 ELGPVNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
889-1373 |
2.53e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 889 VQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV---VSELEARVGEEEECSRQ 965
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRKLEEKIRELEERIEE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 966 MQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1045
Cdd:PRK03918 271 LKKEIEELEEKVKELKEL--------KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1046 KVKSLNKLRLKYEAtiadMEDRLRKEEKGRQ---ELEKLKRRLDGESSELQEQMVEQQQRAEElraQLGRKEEELQAALA 1122
Cdd:PRK03918 343 LKKKLKELEKRLEE----LEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1123 RAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAE---------KQRRDLGEELEALRGELEDTLDSTNAQQEL 1193
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEytaelkrieKELKEIEEKERKLRKELRELEKVLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1194 RskREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQ--LEQARRGKGAWEKTRLALEAEVSELRAELS 1266
Cdd:PRK03918 496 I--KLKELAEQLKELEEKLKKYnleelEKKAEEYEKLKEKLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELEEELA 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1267 SLQTARQEGE-QRRRRLELQLQEVQG------RAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSstE 1339
Cdd:PRK03918 574 ELLKELEELGfESVEELEERLKELEPfyneylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE--E 651
|
490 500 510
....*....|....*....|....*....|....
gi 116284396 1340 AQLHDAQELLQEETRAKLALGSRVRAMEAEAAGL 1373
Cdd:PRK03918 652 LEKKYSEEEYEELREEYLELSRELAGLRAELEEL 685
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
995-1741 |
5.02e-12 |
|
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: 71.64 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 995 QLEKVTTEaKMKKFEEDLLLLEDQNSK---LSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKE 1071
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyeLLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1072 EKgrqeleKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALAEAQED 1151
Cdd:TIGR02169 278 NK------KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER-------LAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1152 LESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQaLG 1231
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE-LA 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1232 ELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGER------ARAEAAE 1305
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1306 KLQRAQAELENVSGALNEAESKTI--------------------RLSKELSSTEAQLHDAQELLQEE--TRAKLALGSRV 1363
Cdd:TIGR02169 504 ERVRGGRAVEEVLKASIQGVHGTVaqlgsvgeryataievaagnRLNNVVVEDDAVAKEAIELLKRRkaGRATFLPLNKM 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1364 RAMEAEAAGLREQLEEEAA------------------ARERAGRELQTAQAQLSEWRR-----RQEEEAGALEAGEEARR 1420
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfGDTLVVEDIEAARRLMGKYRMvtlegELFEKSGAMTGGSRAPR 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1421 RAAREAEALTQRLAEKTETVDRLERGRRRLQQE--------------LDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEK 1486
Cdd:TIGR02169 664 GGILFSRSEPAELQRLRERLEGLKRELSSLQSElrrienrldelsqeLSDASRKIGEIEKEIEQLEQEEEKLKERLEELE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1487 AAVLRAVEERERAEAEGREREARALSLTRALEEEQEAReelerqnralrAELEALLSskddvgksvheleracrvaeqaa 1566
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL-----------NDLEARLS----------------------- 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1567 ndlRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKK 1646
Cdd:TIGR02169 790 ---HSRIPEIQAELSKLEEEVSRIEARLREIE-QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1647 LEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREeifsqnrESEKRLKGLEAEVLRLQEELAASDR 1726
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIED 938
|
810
....*....|....*
gi 116284396 1727 ARRQAQQDRDEMADE 1741
Cdd:TIGR02169 939 PKGEDEEIPEEELSL 953
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
874-1335 |
8.13e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 874 RQDEVLQARAQELQKVQELQQQsAREVGELQGRVAQLEEERARlAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 953
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKK-AEEDKKKADELKKAAAAKKK-ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 954 ARVGEE----EECSRQMQTEKKRLQQhiqeleahleaeegARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKLL 1029
Cdd:PTZ00121 1456 AKKAEEakkkAEEAKKADEAKKKAEE--------------AKKADEAKKKAEEAKKKA--DEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1030 EDRLAEfSSQAAEEEEKVKSLNKLRLKYEAtiadmeDRLRKEEKGRQELEKLKrrldgesselqeqmVEQQQRAEELRAQ 1109
Cdd:PTZ00121 1520 EAKKAD-EAKKAEEAKKADEAKKAEEKKKA------DELKKAEELKKAEEKKK--------------AEEAKKAEEDKNM 1578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1110 LGRKEEELQAAlaraedeggARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNA 1189
Cdd:PTZ00121 1579 ALRKAEEAKKA---------EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA 1649
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1190 QQELRSKREQEV--TELKKTLEEETRIHEAAVQELRQRHGQalgelAEQLEQARRGKGAWEKTRLALEAEVSelRAElsS 1267
Cdd:PTZ00121 1650 EELKKAEEENKIkaAEEAKKAEEDKKKAEEAKKAEEDEKKA-----AEALKKEAEEAKKAEELKKKEAEEKK--KAE--E 1720
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1268 LQTARQEGEQRRRRLELQLQEVQGRAgdgERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1335
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAKKEAEEDKKKA---EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
818-1354 |
8.48e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 818 FQAAARGYLARRAFQKRQQQQSALRVMqrncaaylKLRHWQWWRLFTKVKPLLQVTRQDEVlqaRAQELQKVQELQQ-QS 896
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAE--------EERNNEEIRKFEEARMAHFARRQAAI---KAEEARKADELKKaEE 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 897 AREVGELQgrvaqlEEERARLAEQL-------RAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTE 969
Cdd:PTZ00121 1289 KKKADEAK------KAEEKKKADEAkkkaeeaKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 970 KKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKmKKFEEDLLLLEDQNSKLSK-------ERKLLEDRLAEFSSQAAE 1042
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK-KKAEEDKKKADELKKAAAAkkkadeaKKKAEEKKKADEAKKKAE 1441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1043 EEEKVKSLNKlrlKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELR--AQLGRKEEELQAA 1120
Cdd:PTZ00121 1442 EAKKADEAKK---KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKKA 1518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1121 LARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRdlgeeLEALRGELEDTLDSTNAQQELRSKREQE 1200
Cdd:PTZ00121 1519 EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-----AEEAKKAEEDKNMALRKAEEAKKAEEAR 1593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1201 VTELKKTLEEETRIheaAVQELRQRHGQALGelAEQLEQARRGKGAWEKTRLALEAEV---SELRAELSSLQTARQEGEQ 1277
Cdd:PTZ00121 1594 IEEVMKLYEEEKKM---KAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAK 1668
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116284396 1278 RRRRLELQLQEVQgRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETR 1354
Cdd:PTZ00121 1669 KAEEDKKKAEEAK-KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
874-1210 |
1.29e-11 |
|
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: 70.10 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 874 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELE 953
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIE----KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLE 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 954 ARVGEEE-----ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKL 1028
Cdd:TIGR02169 779 EALNDLEarlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1029 LEDRLAEFSSQAAEeeekvkslnklrlkYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA 1108
Cdd:TIGR02169 859 LNGKKEELEEELEE--------------LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1109 QLGRKEEELqAALARAEDEGGARAQLLKSLReaqaalaeaqedleservartKAEKQRRDLGEELEALRG-------ELE 1181
Cdd:TIGR02169 925 KLEALEEEL-SEIEDPKGEDEEIPEEELSLE---------------------DVQAELQRVEEEIRALEPvnmlaiqEYE 982
|
330 340
....*....|....*....|....*....
gi 116284396 1182 DTLDSTNAQQELRSKREQEVTELKKTLEE 1210
Cdd:TIGR02169 983 EVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1192-1949 |
1.44e-11 |
|
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: 70.10 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1192 ELRSKREQEVTELKkTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTA 1271
Cdd:TIGR02169 167 EFDRKKEKALEELE-EVEENIERLDLIIDEKRQQ----LERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1272 RQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALNEAESKTIRLSKELSSTEAQLHDAQELLQ 1350
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1351 EETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRaareaeaLT 1430
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-------YR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1431 QRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLaEEKAAVLRAveereraeaegrereara 1510
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-EDKALEIKK------------------ 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1511 lsLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTEL-------------- 1576
Cdd:TIGR02169 453 --QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLkasiqgvhgtvaql 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1577 ------------------------EDELTAAEDAKLRLEVTVQALK-------TQHERDLQGRDEAG-----------EE 1614
Cdd:TIGR02169 531 gsvgeryataievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRATflplnkmRDERRDLSILSEDGvigfavdlvefDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1615 RRRQLAKQ-LRDAEVERDEERKQRTLAVAARKKLEGELEE---------------------LKAQMASAGQGKEEAVKQL 1672
Cdd:TIGR02169 611 KYEPAFKYvFGDTLVVEDIEAARRLMGKYRMVTLEGELFEksgamtggsraprggilfsrsEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1673 RKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQ----DRDEMAD---EVANG 1745
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienVKSELKEleaRIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1746 NLSKAAILEEKRQLEGRLGQLEEELEEEQSNSelLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGR 1825
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSRIPEIQAELSK--LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1826 LGEEDAgararhkmTIAALESKLAQAEEQLEQ-ETRERILSGKLVRRAEKRlKEVVLQVEEERRVADQLRDQLEKGNLRV 1904
Cdd:TIGR02169 849 IKSIEK--------EIENLNGKKEELEEELEElEAALRDLESRLGDLKKER-DELEAQLRELERKIEELEAQIEKKRKRL 919
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 116284396 1905 KQLKRQLEEAEEEASRAQAGRRRLQRE------LEDVTESAESMNREVTTL 1949
Cdd:TIGR02169 920 SELKAKLEALEEELSEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRAL 970
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1561-1955 |
1.06e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.25 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1561 VAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEeRKQRtla 1640
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE-RERR--- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1641 vaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTsreEIFSQNRESEKRLKGLEAEVLRLQ-- 1718
Cdd:COG4913 361 ---RARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAEIASLErr 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1719 ------EELAASDRARRQAQQDRDEM----------ADE-------------------VANGNLSKAAILEEKRQLEGRL 1763
Cdd:COG4913 435 ksnipaRLLALRDALAEALGLDEAELpfvgelievrPEEerwrgaiervlggfaltllVPPEHYAAALRWVNRLHLRGRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1764 GQLEEELEEEQSNSELLNDR--YRKLLLQVESLTTELSAE--RSFS-AKAESGRQ--QLERQIQE-----LRGRLGEEDA 1831
Cdd:COG4913 515 VYERVRTGLPDPERPRLDPDslAGKLDFKPHPFRAWLEAElgRRFDyVCVDSPEElrRHPRAITRagqvkGNGTRHEKDD 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1832 ----------GARARHKmtIAALESKLAQAEEQLEQ-ETRERILSGKL-----VRRAEKRLKEV------VLQVEEERRV 1889
Cdd:COG4913 595 rrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEALEAELdalqeRREALQRLAEYswdeidVASAEREIAE 672
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1890 ADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:COG4913 673 LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1083-1853 |
1.21e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 67.09 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1083 RRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKA 1162
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAE 1149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1163 EKQRRDLGEELEALRgELEDTLDSTNAQQELRSKREQEV---TELKKTlEEETRIHEA-AVQELRQRHGQALGELAEQLE 1238
Cdd:PTZ00121 1150 DAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVrkaEELRKA-EDARKAEAArKAEEERKAEEARKAEDAKKAE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1239 QARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlelqlqevqgrAGDGERARaeAAEKLQRAqaelENVS 1318
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQA-----------AIKAEEAR--KADELKKA----EEKK 1290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1319 GALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKlalgSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQl 1398
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----KKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK- 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1399 SEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERgRRRLQQELDDATMDLEQQRQLVSTLEKKQRKF 1478
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK-AAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1479 DQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERA 1558
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1559 --CRVAEQA--ANDLR-AQVTELEDELTAAEDAKLRLEVtvqalKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEE 1633
Cdd:PTZ00121 1525 deAKKAEEAkkADEAKkAEEKKKADELKKAEELKKAEEK-----KKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMK 1599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1634 RKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK---ELWREVEETRTSREEIFSQNRESEKR---- 1706
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKKAEEDKKkaee 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1707 LKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRK 1786
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKA--EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116284396 1787 LLLQVeslttelsaERSFSAKAESGRQQLERQIQElrgRLGEEDAGARARHKMTIAALESKLAQAEE 1853
Cdd:PTZ00121 1758 KIAHL---------KKEEEKKAEEIRKEKEAVIEE---ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
937-1340 |
1.43e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 937 RLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLqlEKVTTEAK-MKKFEEDLLLL 1015
Cdd:PRK03918 166 NLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREEL--EKLEKEVKeLEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1016 EDQNSKLSKERKLLEDRLAEFSSQAAEE-------EEKVKSLNKLRLKYEATIAdMEDRLRKEEKGRQELEKLKRRLDGE 1088
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELkkeieelEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1089 SSELQEQMVEQQQRAEELRaQLGRKEEELQAALARAEDeggaRAQLLKSLREAQAalaeaqedlESERVARTKAEKQRRD 1168
Cdd:PRK03918 323 INGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEE----RHELYEEAKAKKE---------ELERLKKRLTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1169 LGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEE---ETRIHEAAVQELRQRHGQALgelaeqLEQARRGKG 1245
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkAKGKCPVCGRELTEEHRKEL------LEEYTAELK 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1246 AWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLEL--QLQEVQgragdgERARAEAAEKLQRAQAELENVSGALNE 1323
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELE------EKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
410
....*....|....*..
gi 116284396 1324 AESKTIRLSKELSSTEA 1340
Cdd:PRK03918 537 LKGEIKSLKKELEKLEE 553
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1074-1884 |
4.94e-10 |
|
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: 65.14 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1074 GRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSlreaqaalaeaqedle 1153
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRR---------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1154 sERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKTLEEetriHEAAVQELRQrhgqalgeL 1233
Cdd:pfam15921 136 -ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMMLS----HEGVLQEIRS--------I 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1234 AEQLEQARrGKGAWEKTRLA------LEAEVSELraeLSSLQTARQEGEQRRRRLELQLqevqgragdgERARAEAAEK- 1306
Cdd:pfam15921 193 LVDFEEAS-GKKIYEHDSMStmhfrsLGSAISKI---LRELDTEISYLKGRIFPVEDQL----------EALKSESQNKi 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1307 ---LQRAQAELENVsgaLNEAESKTIRLSKELSSTEAQLHDAQ---ELLQEETRAKLALGSR-VRAMEAEAAGLREQLEE 1379
Cdd:pfam15921 259 ellLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRSELRE 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1380 EAAARERAGRELQT----AQAQLSEWRRRQEE---EAGALE-----------AGEEARRRAAREAEALTQRLAEKTETVD 1441
Cdd:pfam15921 336 AKRMYEDKIEELEKqlvlANSELTEARTERDQfsqESGNLDdqlqklladlhKREKELSLEKEQNKRLWDRDTGNSITID 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1442 RLERgrrrlqqELDDATMDLEQQRQLVSTLEKK-QRKFDQLLAEEKAavlraveereraeaegrerearalsltraleee 1520
Cdd:pfam15921 416 HLRR-------ELDDRNMEVQRLEALLKAMKSEcQGQMERQMAAIQG--------------------------------- 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1521 qeaREELERQNRALRAELEallSSKDDVGKSVHEL---ERACRVAEQAANDLRAQVTELED--ELTAAEDAKLRLEVTVQ 1595
Cdd:pfam15921 456 ---KNESLEKVSSLTAQLE---STKEMLRKVVEELtakKMTLESSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLK 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1596 ALKTQHerdLQGRDEageerrrqlakQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKM 1675
Cdd:pfam15921 530 LQELQH---LKNEGD-----------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1676 QAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEE 1755
Cdd:pfam15921 596 EKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSED 675
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1756 KRQLEGRLGQLEEELEEEQsnsellndryRKLLLQVESLTTELSAERSFSAKAESGRQQ-------LERQIQELRGRLG- 1827
Cdd:pfam15921 676 YEVLKRNFRNKSEEMETTT----------NKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQIDa 745
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116284396 1828 --------EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE 1884
Cdd:pfam15921 746 lqskiqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
899-1262 |
2.05e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.16 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 899 EVGELQGRVAQLEEERARLAEQLRAEAELCAEAeetRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQ 978
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRLDEL---SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 979 eleahleaeegarqklqlEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEfsSQAAEEEEKVKSLNKLRLKYE 1058
Cdd:TIGR02169 752 ------------------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1059 ATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAqllksl 1138
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG------ 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1139 reaqaalaeaqeDLESErvaRTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAA 1218
Cdd:TIGR02169 886 ------------DLKKE---RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1219 -----VQELRQRHGQALGELA-------EQLEQARRGKGAWEKTRLALEAEVSELR 1262
Cdd:TIGR02169 951 lsledVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
964-1262 |
2.60e-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: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 964 RQMQTEKKRLQQH-IQELEAHLEAEEGARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSKERKL----LEDRLAEF-- 1036
Cdd:pfam17380 287 RQQQEKFEKMEQErLRQEKEEKAREVERRRKLEEAEKARQAEMDR--QAAIYAEQERMAMERERELerirQEERKRELer 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1037 --SSQAAEEEEKVKSLNKLRLkyeatiadmeDRLRKEEKGRQELE---KLKRRLDGESSELQEQMVEQQQ-RAEELRA-- 1108
Cdd:pfam17380 365 irQEEIAMEISRMRELERLQM----------ERQQKNERVRQELEaarKVKILEEERQRKIQQQKVEMEQiRAEQEEArq 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1109 -QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEElealrgELEDTLDST 1187
Cdd:pfam17380 435 rEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEK------ELEERKQAM 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1188 NAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawEKTRL-ALEAEVSELR 1262
Cdd:pfam17380 509 IEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATE-----ERSRLeAMEREREMMR 579
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1535-1952 |
2.77e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1535 RAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHErDLQGRDEAGEE 1614
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE-ELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1615 RrrqlakqLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSRE 1694
Cdd:PRK02224 329 R-------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1695 EIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNL----------SKAAILEEKRQ----LE 1760
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRErveeLE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1761 GRLGQLEEELEEEQSNSELLNDrYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKM- 1839
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAa 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1840 ------------TIAALESKLAQAEEQLEQ-ETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1906
Cdd:PRK02224 561 aeaeeeaeeareEVAELNSKLAELKERIESlERIRTLLA--AIADAEDEIERLREKREALAELNDERRERLAEKRERKRE 638
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 116284396 1907 LKRQLeeAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNR 1952
Cdd:PRK02224 639 LEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1094-1864 |
3.80e-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: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1094 EQMVEQQQRAEELRAQLgRKEEELQAALARAEDEGGARAQLLKSLREAqaalaeaqeDLESERVARTKAEKQRRDLGEEL 1173
Cdd:COG4913 228 DALVEHFDDLERAHEAL-EDAREQIELLEPIRELAERYAAARERLAEL---------EYLRAALRLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1174 EALRGELEDTldstnaqqelrskrEQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLA 1253
Cdd:COG4913 298 EELRAELARL--------------EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1254 LEAEVSELRAEL----SSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENV-SGALN-EAESK 1327
Cdd:COG4913 364 LEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLeRRKSNiPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1328 TIR--LSKELSSTEAQLHDAQELLQ---EETR----AKLALGSRVRAM------EAEAAglreqleeEAAARERAGRELQ 1392
Cdd:COG4913 444 ALRdaLAEALGLDEAELPFVGELIEvrpEEERwrgaIERVLGGFALTLlvppehYAAAL--------RWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1393 TAQAQLS-EWRRRQEEEAGALEAGEEARRRAARE--AEALTQRLA-EKTETVDRLERGRRRLQQ-----------ELDDA 1457
Cdd:COG4913 516 YERVRTGlPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDyVCVDSPEELRRHPRAITRagqvkgngtrhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1458 TmDLEQQRQL-VSTLEKKQRKFDQL-LAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALR 1535
Cdd:COG4913 596 R-RIRSRYVLgFDNRAKLAALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1536 AELEALLSSKDDVGksvhELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDlqgRDEAGEER 1615
Cdd:COG4913 675 AELERLDASSDDLA----ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLEL 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1616 RRQLAKQLRDAEVERDEERkqrtlavaARKKLEGELEELKAQMAsagqgkeEAVKQLRKMQAQMKELWR-EVEETRTSRE 1694
Cdd:COG4913 748 RALLEERFAAALGDAVERE--------LRENLEERIDALRARLN-------RAEEELERAMRAFNREWPaETADLDADLE 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1695 EifsqNRESEKRLKGLEAEVL-RLQEELAasDRARRQAQQDRdemadevanGNLSkAAILEEKRQLEGRLGQleeeleee 1773
Cdd:COG4913 813 S----LPEYLALLDRLEEDGLpEYEERFK--ELLNENSIEFV---------ADLL-SKLRRAIREIKERIDP-------- 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1774 qsnselLNDRYRKL------LLQVESLTTELSAERSFsakaesgrqqlERQIQELRGRLGEEDAGARARHKMTIAALESK 1847
Cdd:COG4913 869 ------LNDSLKRIpfgpgrYLRLEARPRPDPEVREF-----------RQELRAVTSGASLFDEELSEARFAALKRLIER 931
|
810
....*....|....*..
gi 116284396 1848 LAQAEEQLEQETRERIL 1864
Cdd:COG4913 932 LRSEEEESDRRWRARVL 948
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
884-1187 |
4.12e-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: 61.68 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 884 QELQKVQELQQQSAREVGElQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAA-----------RKQELELVVSEL 952
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKME-QERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermameRERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 953 EAR----VGEEE---ECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1025
Cdd:pfam17380 358 RKRelerIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1026 RKLLEDRLAEFSSQAAEEEEKVKSLNKLRlKYEATIADMEDRLRKEEKGRQELEKLKRR-LDGESSELQEQMVEQQQRae 1104
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKiLEKELEERKQAMIEEERK-- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1105 elRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEEL---EALRGELE 1181
Cdd:pfam17380 515 --RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIvesEKARAEYE 592
|
....*.
gi 116284396 1182 DTLDST 1187
Cdd:pfam17380 593 ATTPIT 598
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
879-1316 |
1.41e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.08 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 879 LQARAQELQKVQELQQQSAREVGELQGRVAQLE---EERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEAR 955
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 956 VGEEEECSRqmqtEKKRLQQHIQELEAHLEAEEGARQKL----QLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLED 1031
Cdd:PRK03918 337 EERLEELKK----KLKELEKRLEELEERHELYEEAKAKKeeleRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1032 RLAEFSSQAAEEEEKVKSLNK-------------------LRLKYEATIADMEDRLR----KEEKGRQELEKLKRRLDGE 1088
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKakgkcpvcgrelteehrkeLLEEYTAELKRIEKELKeieeKERKLRKELRELEKVLKKE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1089 S----------------SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDL 1152
Cdd:PRK03918 493 SeliklkelaeqlkeleEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEEL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1153 ES-ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRS---KREQEVTELKKTLEEETRIhEAAVQELRQRHGQ 1228
Cdd:PRK03918 573 AElLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEReekELKKLEEELDKAFEELAET-EKRLEELRKELEE 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1229 ALGELAEQLEQARRGKgawektRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVqgragdgERARAEaAEKLQ 1308
Cdd:PRK03918 652 LEKKYSEEEYEELREE------YLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-------EKAKKE-LEKLE 717
|
....*...
gi 116284396 1309 RAQAELEN 1316
Cdd:PRK03918 718 KALERVEE 725
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1017-1254 |
1.44e-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: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1017 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQM 1096
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1097 VEQQQR-AEELRAQLGRKEEELQAALARAEDEGGA--RAQLLKSL-REAQAALAEAQEDLESERVARTKAEKQRrdlgEE 1172
Cdd:COG4942 100 EAQKEElAELLRALYRLGRQPPLALLLSPEDFLDAvrRLQYLKYLaPARREQAEELRADLAELAALRAELEAER----AE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1173 LEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1252
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
..
gi 116284396 1253 AL 1254
Cdd:COG4942 256 PW 257
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1567-1949 |
2.06e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1567 NDLRAQVTELEDELTAAEDAKLRLEVTVQALK---TQHERDLQGRDEAGEERRrQLAKQLRDAEVERDEERKQRTLAVAA 1643
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIE-DLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1644 RKKLEGELEELKAQmASAGQGKEEAVKQLRK-MQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELA 1722
Cdd:PRK02224 288 LEELEEERDDLLAE-AGLDDADAEAVEARREeLEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1723 ASDRARRQAQQDRDEMADEVAngnlskaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAER 1802
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIE-------ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1803 SFSAKAESGR---------QQLERQ-----IQELRGRLGEEDAgARARHKMTIAALESKLAQAEEQLEQETRerilsgkl 1868
Cdd:PRK02224 440 ERVEEAEALLeagkcpecgQPVEGSphvetIEEDRERVEELEA-ELEDLEEEVEEVEERLERAEDLVEAEDR-------- 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1869 VRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEE----ASRAQAGRRR---LQRELEDVTESAES 1941
Cdd:PRK02224 511 IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEAREEvaeLNSKLAELKERIES 590
|
....*...
gi 116284396 1942 MNREVTTL 1949
Cdd:PRK02224 591 LERIRTLL 598
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
934-1334 |
4.32e-08 |
|
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: 58.54 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 934 TRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1013
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1014 LLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKslnklrlKYEATIADMEDRLRKEEkgrqeleklKRRLDGESSELQ 1093
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-------KLEEALNDLEARLSHSR---------IPEIQAELSKLE 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1094 EQMVEQQQRAEELRAQLGRKEEELQAalarAEDEggaraqllkslreaqaalaeaQEDLESERVArtkAEKQRRDLGEEL 1173
Cdd:TIGR02169 805 EEVSRIEARLREIEQKLNRLTLEKEY----LEKE---------------------IQELQEQRID---LKEQIKSIEKEI 856
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1174 EALRGELEDtldsTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQARRGKGAWEKTRLA 1253
Cdd:TIGR02169 857 ENLNGKKEE----LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK----IEELEAQIEKKRKRLSELKAKLEA 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1254 LEAEVSELRAELSSLQTaRQEGEQRRRRLELQLQEVQgragdgerARAEAAEKLQ-RAQAELENVSGALNEAESKTIRLS 1332
Cdd:TIGR02169 929 LEEELSEIEDPKGEDEE-IPEEELSLEDVQAELQRVE--------EEIRALEPVNmLAIQEYEEVLKRLDELKEKRAKLE 999
|
..
gi 116284396 1333 KE 1334
Cdd:TIGR02169 1000 EE 1001
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1023-1361 |
7.66e-08 |
|
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: 57.77 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1023 SKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQR 1102
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1103 AEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVartkaeKQRRDLGEELEALRGELED 1182
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI------PEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1183 TLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRgkgawektrlaLEAEVSELR 1262
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-----------LEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1263 AELSSLQtarqegeQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAEsKTIRLSKELSSTEAQL 1342
Cdd:TIGR02169 882 SRLGDLK-------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-DPKGEDEEIPEEELSL 953
|
330
....*....|....*....
gi 116284396 1343 HDAQELLQEETRAKLALGS 1361
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEP 972
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1359-1907 |
7.67e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1359 LGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEA---GALEAGEEARRRAAREAEALTQRLAE 1435
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1436 KTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEEREraeaegrerearalSLTR 1515
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE--------------SLRE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1516 ALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ 1595
Cdd:PRK02224 350 DADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1596 ALKTqherDLQGRDEAGEERRRQLA--------KQLRDAE-VERDEERKQRtlavaaRKKLEGELEELKAQMASAGQgKE 1666
Cdd:PRK02224 430 ELEA----TLRTARERVEEAEALLEagkcpecgQPVEGSPhVETIEEDRER------VEELEAELEDLEEEVEEVEE-RL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1667 EAVKQLRKMQAQMKELwrevEETRTSREEIFSQNRES--EKRLKgleAEVLRLQ-EELAASDRARRQAQQDRDEMADEVA 1743
Cdd:PRK02224 499 ERAEDLVEAEDRIERL----EERREDLEELIAERRETieEKRER---AEELRERaAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1744 ngnlskaailEEKRQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVESLTTELSAERS-FSAKAESGRQQLERqIQEL 1822
Cdd:PRK02224 572 ----------EEVAELNSKLAELKERIESL--------ERIRTLLAAIADAEDEIERLREkREALAELNDERRER-LAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1823 RGR---LGEEDAGARarhkmtIAALESKLAQAEEQLEQetreriLSGKLVRRAEKR--LKEVVLQVEEERRVADQLRDQL 1897
Cdd:PRK02224 633 RERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREERddLQAEIGAVENELEELEELRERR 700
|
570
....*....|
gi 116284396 1898 EKGNLRVKQL 1907
Cdd:PRK02224 701 EALENRVEAL 710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1021-1480 |
1.19e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1021 KLSKERKLLEdRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEkgRQELEKLKRRLDGESSELQEQMVEQQ 1100
Cdd:COG4913 246 DAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAE--LEELRAELARLEAELERLEARLDALR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1101 QRAEELRAQL----GRKEEELQAALARAEDEGGARAQLLKSL----------------------REAQAALAEAQEDLES 1154
Cdd:COG4913 323 EELDELEAQIrgngGDRLEQLEREIERLERELEERERRRARLeallaalglplpasaeefaalrAEAAALLEALEEELEA 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1155 ERVARTKAEKQRRDLGEELEALRGELEdtldstnaqqELRSKR---EQEVTELKKTLEEETRIHEAAVQ------ELRQR 1225
Cdd:COG4913 403 LEEALAEAEAALRDLRRELRELEAEIA----------SLERRKsniPARLLALRDALAEALGLDEAELPfvgeliEVRPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1226 ------------HGQALGEL--AEQLEQARRgkgAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQG 1291
Cdd:COG4913 473 eerwrgaiervlGGFALTLLvpPEHYAAALR---WVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1292 -----------------------------RAG-----------DGERARAE-------AAEKLQRAQAELENVSGALNEA 1324
Cdd:COG4913 550 wleaelgrrfdyvcvdspeelrrhpraitRAGqvkgngtrhekDDRRRIRSryvlgfdNRAKLAALEAELAELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1325 ESKTIRLSKELSSTEAQLHDAQELLQ------------------EETRAKLALGS-RVRAMEAEAAGLREQLEEEAAARE 1385
Cdd:COG4913 630 EERLEALEAELDALQERREALQRLAEyswdeidvasaereiaelEAELERLDASSdDLAALEEQLEELEAELEELEEELD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1386 RAGRELQTAQAQLSEWRRRQEEEAGALeaGEEARRRAAREAEALTQRLAEKTETvDRLERGRRRLQQELDDATmdlEQQR 1465
Cdd:COG4913 710 ELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEERFAAALGD-AVERELRENLEERIDALR---ARLN 783
|
570
....*....|....*
gi 116284396 1466 QLVSTLEKKQRKFDQ 1480
Cdd:COG4913 784 RAEEELERAMRAFNR 798
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1010-1742 |
1.81e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1010 EDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEeeKVKSLNKLRLKYEATIADMEDRLRK----EEKGRQELEKLKRRL 1085
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1086 DGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQ 1165
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1166 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQevteLKKTLEEETRIHeaAVQELRQRHGQALGELAEQLEQARRGKG 1245
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI----SCQQHTLTQHIH--TLQQQKTTLTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1246 awekTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAE 1325
Cdd:TIGR00618 411 ----TIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1326 SKtirlskelssteAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLsewRRRQ 1405
Cdd:TIGR00618 487 RK------------KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDV---YHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1406 EEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDdatMDLEQQRQLVSTLEKKQRKFDQLLA-E 1484
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE---KLSEAEDMLACEQHALLRKLQPEQDlQ 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1485 EKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELER---ACRV 1561
Cdd:TIGR00618 629 DVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQcqtLLRE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1562 AEQAANDLRAQVTELEDELTAAedaklrlevtvqalktqhERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAV 1641
Cdd:TIGR00618 709 LETHIEEYDREFNEIENASSSL------------------GSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1642 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEK----RLKGLEAEVLRL 1717
Cdd:TIGR00618 771 TAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLsrleEKSATLGEITHQ 850
|
730 740
....*....|....*....|....*
gi 116284396 1718 QEELAASDRARRQAQQDRDEMADEV 1742
Cdd:TIGR00618 851 LLKYEECSKQLAQLTQEQAKIIQLS 875
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1029-1836 |
6.48e-07 |
|
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: 54.74 E-value: 6.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1029 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYE----ATIADMEDRLRKEEKGRQELEKLKRRldgesselqeqmveQQQRAE 1104
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRR--------------ESQSQE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1105 ELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQR------------------ 1166
Cdd:pfam15921 142 DLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKiyehdsmstmhfrslgsa 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1167 -----RDLGEELEALRGEL---EDTLDSTNAqqELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGE---LAE 1235
Cdd:pfam15921 222 iskilRELDTEISYLKGRIfpvEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1236 QLE----QARRGKGAWEKTRLALEAEVSELRAELsslQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAE------ 1305
Cdd:pfam15921 300 QLEiiqeQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnld 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1306 -KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAAR 1384
Cdd:pfam15921 377 dQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGK 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1385 ERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQ 1464
Cdd:pfam15921 457 NESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1465 RQLVSTLEKKQRKFD--QLLAEEKAAVLRAVEERERAEAEGREREaralslTRALEEEQEAREELERQNRALRAELEALL 1542
Cdd:pfam15921 537 KNEGDHLRNVQTECEalKLQMAEKDKVIEILRQQIENMTQLVGQH------GRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1543 SSKDDVGKSVHELEraCRVAE----------------QAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtqheRDLQ 1606
Cdd:pfam15921 611 ILKDKKDAKIRELE--ARVSDlelekvklvnagserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK----RNFR 684
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1607 GRDEAGEERRRQLAKQLRDAEVERDEERKQ-----------RTLAVAARKKLEGELEELKAqMASAGQGKEEAVKQLRKM 1675
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTlksmegsdghaMKVAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKE 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1676 QAQMKElwrevEETRTSRE--EIFSQNRESEKRLKGLEAEVLRLQEELA----ASDRARRQAQQDRDEMADEVANGNLSK 1749
Cdd:pfam15921 764 KHFLKE-----EKNKLSQElsTVATEKNKMAGELEVLRSQERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1750 AAILEEKRQLEGRlGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAE-RSFSAKAESGRQQLERQIQELRGRLGE 1828
Cdd:pfam15921 839 LQHTLDVKELQGP-GYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFLSHHsRKTNALKEDPTRDLKQLLQELRSVINE 917
|
....*...
gi 116284396 1829 EDAGARAR 1836
Cdd:pfam15921 918 EPTVQLSK 925
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1000-1242 |
7.46e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 7.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1000 TTEAKMKKFEEDLLLLED-------QNSKLSKERKLLEDRLAEFS--SQAAEEEEKVKSLnklrlkyEATIADMEDRLRK 1070
Cdd:COG4913 607 DNRAKLAALEAELAELEEelaeaeeRLEALEAELDALQERREALQrlAEYSWDEIDVASA-------EREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1071 EEKGRQELEKLKRRLDG---ESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLlksLREAQAALAE 1147
Cdd:COG4913 680 LDASSDDLAALEEQLEEleaELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---LRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1148 AQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSK-------REQEVTELKKTLEEEtRIHEAAVQ 1220
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETAdldadleSLPEYLALLDRLEED-GLPEYEER 835
|
250 260
....*....|....*....|....*
gi 116284396 1221 ELRQRH---GQALGELAEQLEQARR 1242
Cdd:COG4913 836 FKELLNensIEFVADLLSKLRRAIR 860
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1659-1899 |
9.14e-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: 53.23 E-value: 9.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1659 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1738
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1739 adevangnlsKAAILEEKRQLEGRLGQLEEELEEEqsnsellndrYRKLLLQVESLTTELSAERSFSAKAESGRQQLErQ 1818
Cdd:COG4942 96 ----------RAELEAQKEELAELLRALYRLGRQP----------PLALLLSPEDFLDAVRRLQYLKYLAPARREQAE-E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1819 IQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQETRERilsGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLE 1898
Cdd:COG4942 155 LRADLAELAALRAELEAERA-ELEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
.
gi 116284396 1899 K 1899
Cdd:COG4942 231 R 231
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
871-1486 |
9.82e-07 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 54.20 E-value: 9.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 871 QVTRQDEVLQARaqelQKVQELQQQSAREVGELQGRVAQLEEER---------ARLAEQLRAEAELCAEAEETRGRLAAR 941
Cdd:TIGR00618 244 YLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 942 KQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQleKVTTEAKMKKFEEDLLLLEDQ--- 1018
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQKTTLTQKlqs 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1019 -NSKLSKERKLLEDRLAEFSSQAAEEEEKV--KSLNKLRLKYEATIADMEDRLRKEEKGRQ-ELEKLKRRLDGESSELQ- 1093
Cdd:TIGR00618 398 lCKELDILQREQATIDTRTSAFRDLQGQLAhaKKQQELQQRYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQt 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1094 -EQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLL-------KSLREAQAALAEAQEDLESERVARTKAEKQ 1165
Cdd:TIGR00618 478 kEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQ 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1166 RRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH-----EAAVQELRQRHGQALGELAEQLEQA 1240
Cdd:TIGR00618 558 RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEdmlacEQHALLRKLQPEQDLQDVRLHLQQC 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1241 RRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGA 1320
Cdd:TIGR00618 638 SQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1321 LNEAESKTIRLSKELSSTEAQLHDAQELLQE-ETRAKLALGSRVRAMEaeaaglreQLEEEAAARERAGRELQTAQAQLS 1399
Cdd:TIGR00618 717 DREFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLKARTEAHF--------NNNEEVTAALQTGAELSHLAAEIQ 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1400 EWRRRQEEEAGALeageeaRRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFD 1479
Cdd:TIGR00618 789 FFNRLREEDTHLL------KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
....*..
gi 116284396 1480 QLLAEEK 1486
Cdd:TIGR00618 863 QLTQEQA 869
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
991-1760 |
1.07e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 991 RQKLQLEKVTTEAK-MKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLR 1069
Cdd:PRK03918 152 RQILGLDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1070 KEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEELRAqlgrKEEELQAALARaedeggaraqlLKSLREAQAALA 1146
Cdd:PRK03918 232 ELEELKEEIEELEKElesLEGSKRKLEEKIRELEERIEELKK----EIEELEEKVKE-----------LKELKEKAEEYI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1147 EAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQ---EVTELKKTLE--EETRIHEAAVQE 1221
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKElekRLEELEERHElyEEAKAKKEELER 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1222 LRQRH-GQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQegeqrrrrlelQLQEVQGRAGDGERAR 1300
Cdd:PRK03918 377 LKKRLtGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE-----------ELKKAKGKCPVCGREL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1301 AEAAEK--LQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLalgsrVRAMEAEAAGLREqle 1378
Cdd:PRK03918 446 TEEHRKelLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYNL--- 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1379 eeaaareragrelqtaqaqlsewrrrqeeeagaleageearrraareaealtQRLAEKTETVDRLERGRRRLQQELDDAT 1458
Cdd:PRK03918 518 ----------------------------------------------------EELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1459 MDLEQQRQLVSTLEKKQRKFDQLlaEEKAAVLraveereraeaegrerearalsltraleeeqeareelerqnraLRAEL 1538
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDEL--EEELAEL-------------------------------------------LKELE 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1539 EALLSSKDDVGKSVHELERACRvaeqAANDLRAQVTELEDELTAAEDAKLRLEvtvqalktQHERDLQGRDEAGEERRrq 1618
Cdd:PRK03918 581 ELGFESVEELEERLKELEPFYN----EYLELKDAEKELEREEKELKKLEEELD--------KAFEELAETEKRLEELR-- 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1619 laKQLRDAEVERDEERkqrtlavaaRKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFS 1698
Cdd:PRK03918 647 --KELEELEKKYSEEE---------YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 116284396 1699 QNRESEkRLKGLEAEVLRLQEELAasDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLE 1760
Cdd:PRK03918 716 LEKALE-RVEELREKVKKYKALLK--ERALSKVGEIASEIFEELTEGKYSGVRVKAEENKVK 774
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1614-1937 |
1.40e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1614 ERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMK------------- 1680
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRqqekieryqedle 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1681 ELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARrQAQQDRdemadevangnlskaAIleEKRQLE 1760
Cdd:COG3096 358 ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAL-DVQQTR---------------AI--QYQQAV 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1761 GRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGE---EDAGARARH 1837
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1838 KMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEkgnlrvkQLKRQLEEAEEE 1917
Cdd:COG3096 500 LLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQ 572
|
330 340
....*....|....*....|
gi 116284396 1918 ASRAQAGRRRLQRELEDVTE 1937
Cdd:COG3096 573 AAEAVEQRSELRQQLEQLRA 592
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1029-1444 |
1.47e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1029 LEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA 1108
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNE 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1109 QLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTN 1188
Cdd:PRK02224 343 EAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1189 AQQELRSKREQEVTELKKTLEEETRIHEA-----------------AVQELRQRhgqaLGELAEQLEQARRGKGAWEK-- 1249
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRER----VEELEAELEDLEEEVEEVEErl 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1250 TRL----ALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGD----GERARAEAAEKLQRAQAELENVS--- 1318
Cdd:PRK02224 499 ERAedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleaeAEEKREAAAEAEEEAEEAREEVAeln 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1319 ---GALNEAESKTIRLSKELSSTEAQLHDAQEL---------LQEETRAKLA-LGSRVRAMEAEAAGlreqleEEAAARE 1385
Cdd:PRK02224 579 sklAELKERIESLERIRTLLAAIADAEDEIERLrekrealaeLNDERRERLAeKRERKRELEAEFDE------ARIEEAR 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 116284396 1386 RAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLE 1444
Cdd:PRK02224 653 EDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALE 711
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1534-1955 |
1.52e-06 |
|
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: 53.58 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1534 LRAELEALLSSKDDvgkSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQ------ALKTQHERDLQG 1607
Cdd:pfam15921 329 LRSELREAKRMYED---KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHkrekelSLEKEQNKRLWD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1608 RDEAGEERRRQLAKQL--RDAEVERDEerkqrTLAVAARKKLEGELEElkaQMAsAGQGKEEAVKQLRKMQAQM---KEL 1682
Cdd:pfam15921 406 RDTGNSITIDHLRRELddRNMEVQRLE-----ALLKAMKSECQGQMER---QMA-AIQGKNESLEKVSSLTAQLestKEM 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1683 WREVEETRTSRE-----------EIFSQNRESEKRLKGLEAEV--------LRLQE-----------------------E 1720
Cdd:pfam15921 477 LRKVVEELTAKKmtlessertvsDLTASLQEKERAIEATNAEItklrsrvdLKLQElqhlknegdhlrnvqtecealklQ 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1721 LAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQsnseLLNDRYRKLLLQVESLTTELSA 1800
Cdd:pfam15921 557 MAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK----ILKDKKDAKIRELEARVSDLEL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1801 ERSFSAKAESGRQQLERQIQELRGRLGEEDAGARA----------------RHK-----MTIAALESKLAQAEEQLEQeT 1859
Cdd:pfam15921 633 EKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNelnslsedyevlkrnfRNKseemeTTTNKLKMQLKSAQSELEQ-T 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1860 RERIlsgKLVRRAEKRLKEVVLQVEEERRVAdqlRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESA 1939
Cdd:pfam15921 712 RNTL---KSMEGSDGHAMKVAMGMQKQITAK---RGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEK 785
|
490
....*....|....*.
gi 116284396 1940 ESMNREVTTLRNRLRR 1955
Cdd:pfam15921 786 NKMAGELEVLRSQERR 801
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1076-1366 |
2.09e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has 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: 52.38 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1076 QELEKLKRRLdgesSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE 1155
Cdd:pfam19220 41 RELPQAKSRL----LELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1156 RVARTKAEKQ-------RRDLGEELEALRGEL----EDTLDSTNAQQELRSKR---EQEVTELKKTLEE---ETRIHEAA 1218
Cdd:pfam19220 117 TAQAEALERQlaaeteqNRALEEENKALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAELTRR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1219 VQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQtarqegeqrrrrleLQLQEVQGRAGDGER 1298
Cdd:pfam19220 197 LAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLR--------------MKLEALTARAAATEQ 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1299 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAM 1366
Cdd:pfam19220 263 LLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
875-1267 |
5.00e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.43 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 875 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 954
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 955 RVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLA 1034
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1035 EFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqMVEQQQR--AEELRAQLGR 1112
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSS-MAAQRDRtqAELHQARLQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1113 KEEELQAALAR-AEDEGGAR-AQLLKSLReaqaalaeAQEDLESERVARTKAEKQRRD--LGEEL---EALRGELEDTLD 1185
Cdd:pfam07888 282 AQLTLQLADASlALREGRARwAQERETLQ--------QSAEADKDRIEKLSAELQRLEerLQEERmerEKLEVELGREKD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1186 STNAQqelRSKREQEVTELKKTLEEETRiheaaVQELRQRHGQALGELAEQLEQaRRGKGAWEKTRLALEAEVSELRAEL 1265
Cdd:pfam07888 354 CNRVQ---LSESRRELQELKASLRVAQK-----EKEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDSPL 424
|
..
gi 116284396 1266 SS 1267
Cdd:pfam07888 425 SD 426
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
993-1352 |
5.23e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 51.50 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 993 KLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADME---DRLR 1069
Cdd:COG5185 177 KKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAqtsDKLE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1070 ---------KEEKGRQELEKLKR------RLDGESSELQEQMVEQQQRAEELRAQLgRKEEELQAALARAEDEGGARAQl 1134
Cdd:COG5185 257 klveqntdlRLEKLGENAESSKRlnenanNLIKQFENTKEKIAEYTKSIDIKKATE-SLEEQLAAAEAEQELEESKRET- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1135 LKSLREAQAALAEAQEDLEsERVARTKAEKQRRDLGEELEALRGELEdtldstNAQQELRSKREqEVTELKKTLEEETRI 1214
Cdd:COG5185 335 ETGIQNLTAEIEQGQESLT-ENLEAIKEEIENIVGEVELSKSSEELD------SFKDTIESTKE-SLDEIPQNQRGYAQE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1215 HEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRlelqlQEVQGRAG 1294
Cdd:COG5185 407 ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEIN-----RSVRSKKE 481
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1295 DGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEE 1352
Cdd:COG5185 482 DLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
884-1216 |
6.70e-06 |
|
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: 51.17 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 884 QELQKVQELQQQsarevgeLQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECS 963
Cdd:TIGR04523 398 SKIQNQEKLNQQ-------KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 964 RQMQTEKKRLQQhiqeleahleaeegarqklQLEKVTTEAKMKkfeedllllEDQNSKLSKERKLLEDRLAEFSSQAAEE 1043
Cdd:TIGR04523 471 KVLSRSINKIKQ-------------------NLEQKQKELKSK---------EKELKKLNEEKKELEEKVKDLTKKISSL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1044 EEKVKSLNKLRLKYEATIADMEDRLRK--EEKGRQELEKLKRRLDGESSEL---QEQMVEQQQRAEELRAQLGRKEEELQ 1118
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLI 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1119 AALARAEdeggaraQLLKSLREAQAALAEAQEDLESErvaRTKAEKQRRDLGEELEALRGELEDTLDSTN----AQQELR 1194
Cdd:TIGR04523 603 KEIEEKE-------KKISSLEKELEKAKKENEKLSSI---IKNIKSKKNKLKQEVKQIKETIKEIRNKWPeiikKIKESK 672
|
330 340
....*....|....*....|..
gi 116284396 1195 SKrEQEVTELKKTLEEETRIHE 1216
Cdd:TIGR04523 673 TK-IDDIIELMKDWLKELSLHY 693
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1642-1878 |
6.97e-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: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1642 AARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1721
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1722 AASDRAR-RQAQQDRDEMAdevangnLSKAAILEEKRQLEgrlgqleeeleeeqsnseLLNDRYRKLLLQVESLTTELSA 1800
Cdd:COG4942 107 AELLRALyRLGRQPPLALL-------LSPEDFLDAVRRLQ------------------YLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1801 ERSFSAKAESGRQQLERQIQELRGRLgEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKE 1878
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEER-AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
879-1369 |
8.25e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.89 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 879 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLA-EQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVG 957
Cdd:pfam05557 53 LQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLnEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 958 EEEECSRQMQTEKKRLQQHIQELEAHleaeegarQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEdRLAEFS 1037
Cdd:pfam05557 133 ELEELQERLDLLKAKASEAEQLRQNL--------EKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELA-RIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1038 SQAAEEEEKVKSLNKLR---LKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRA--QLGR 1112
Cdd:pfam05557 204 KELERLREHNKHLNENIenkLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpeDLSR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1113 KEEELQAALARAEDEGGARAQLLKSLReaqaalaEAQEDLESE-RVARTKAEKQRRDLgEELEALRGELEDTLDSTNAQ- 1190
Cdd:pfam05557 284 RIEQLQQREIVLKEENSSLTSSARQLE-------KARRELEQElAQYLKKIEDLNKKL-KRHKALVRRLQRRVLLLTKEr 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1191 ---QELRSKREQEVTELKKTLEEETRIHEAAvqELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSS 1267
Cdd:pfam05557 356 dgyRAILESYDKELTMSNYSPQLLERIEEAE--DMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1268 LQTARQEGEQRRRRLELQLQEvqgragdGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKE-LSSTEAQLHDAQ 1346
Cdd:pfam05557 434 ADPSYSKEEVDSLRRKLETLE-------LERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNpAAEAYQQRKNQL 506
|
490 500
....*....|....*....|...
gi 116284396 1347 ELLQEETRaklALGSRVRAMEAE 1369
Cdd:pfam05557 507 EKLQAEIE---RLKRLLKKLEDD 526
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1562-1985 |
8.42e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 8.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1562 AEQA--ANDLR-AQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDA----EVERDEER 1634
Cdd:PTZ00121 1274 AEEArkADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAkkaaEAAKAEAE 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1635 KQRTLAVAARKKLEGEleELKAQMAsagQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEK--RLKGlEA 1712
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAA--EKKKEEA---KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKadEAKK-KA 1427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1713 EVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAilEEKRQLEgrlgqleeeLEEEQSNSELLNDRYRKLLLQVE 1792
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA--EEAKKAD---------EAKKKAEEAKKADEAKKKAEEAK 1496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1793 SLTTELSAERSFSAKAESGRQQLE-RQIQELRGrlGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERIlsgKLVRR 1871
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEaKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKA---EEAKK 1571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1872 AEKRlKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRN 1951
Cdd:PTZ00121 1572 AEED-KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
410 420 430
....*....|....*....|....*....|....
gi 116284396 1952 RLRRGPLTFTTRTVRQVFRLEEGVASDEEAEEAQ 1985
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1252-1477 |
8.90e-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: 50.15 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1252 LALEAEVSELRAELSSLQtarqegeQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRL 1331
Cdd:COG4942 16 AAQADAAAEAEAELEQLQ-------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1332 SKELSSTEAQLHDAQELLQEETRAKLALGSRVRAME----AEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEE 1407
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1408 EAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRK 1477
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1532-1748 |
9.29e-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: 50.15 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1532 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHERDLQGRDEA 1611
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1612 GeerRRQLAKQLRDAEVERDEERKQRTLAVAAR------KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWRE 1685
Cdd:COG4942 117 G---RQPPLALLLSPEDFLDAVRRLQYLKYLAParreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1686 VEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLS 1748
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1718-1960 |
1.17e-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: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1718 QEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTE 1797
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1798 LSAERSFSAKAESGRQQLERQiQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLK 1877
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1878 EVVLQVEEERRVADQLRDQLEKgnlRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1957
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 116284396 1958 LTF 1960
Cdd:COG4942 255 LPW 257
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
814-1056 |
1.18e-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: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 814 IIVSFQAAARGYLARRAFQKRQQQQSALRVMQRNCAAYLKlrhwqwwrlfTKVKPLLQVTRQDEVLQARAQELQKVQELQ 893
Cdd:COG4942 9 LLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK----------EEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 894 QQSAREVGELQGRVAQLEEE----RARLAEQLRAEAELCAEAEETR-------GRLAARKQELELVVSELEARVGEEEEC 962
Cdd:COG4942 79 AALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 963 SRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAE 1042
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....
gi 116284396 1043 EEEKVKSLNKLRLK 1056
Cdd:COG4942 239 AAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1282-1735 |
1.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1282 LELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGS 1361
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1362 RVRAMEAEAagLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREA-EALTQRLAEKTETV 1440
Cdd:COG4717 131 YQELEALEA--ELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1441 DRLERGRRRLQQELDDATMDLEQ-QRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEE 1519
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1520 EQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAE----QAANDLRAQVTELEDELTAAEDAKLRLEvtVQ 1595
Cdd:COG4717 289 LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspEELLELLDRIEELQELLREAEELEEELQ--LE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1596 ALKTQHERDLQGRDEAGEERRRQLAKQLRD-----AEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVK 1670
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELRAALEQAEEyqelkEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116284396 1671 QLRKMQAQMKELWREVEETRTSRE--EIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDR 1735
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGElaELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
872-1262 |
1.47e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 872 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLA--EQLRAEAELCAEAEETRGRLAA--RKQELEL 947
Cdd:PRK03918 326 IEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEelERLKKRLTGLTPEKLEKELEELekAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 948 VVSELEARVGEeeecsrqMQTEKKRLQQHIQELEAHLEAEEGARQKLQ-------LEKVTteAKMKKFEEDLLLLEDQNS 1020
Cdd:PRK03918 406 EISKITARIGE-------LKKEIKELKKAIEELKKAKGKCPVCGRELTeehrkelLEEYT--AELKRIEKELKEIEEKER 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1021 KLSKERKLLEDRLAEFSS---------QAAEEEEKVKSLNKLRLKYEAtiadmedrlRKEEKGRQELEKLKRRLDGESSE 1091
Cdd:PRK03918 477 KLRKELRELEKVLKKESEliklkelaeQLKELEEKLKKYNLEELEKKA---------EEYEKLKEKLIKLKGEIKSLKKE 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1092 LqEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLK--------------SLREAQAALAEAQEDLESERV 1157
Cdd:PRK03918 548 L-EKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEerlkelepfyneylELKDAEKELEREEKELKKLEE 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1158 ARTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREqEVTELKKTLEE-ETRIHEAavQELRQRHGQALGELAEQ 1236
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKELEE-LEKKYSEEEYEELRE-EYLELSRELAGlRAELEEL--EKRREEIKKTLEKLKEE 702
|
410 420
....*....|....*....|....*.
gi 116284396 1237 LEQARRGKGAWEKTRLALEaEVSELR 1262
Cdd:PRK03918 703 LEEREKAKKELEKLEKALE-RVEELR 727
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
911-1320 |
1.72e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 911 EEERARLAEQlraEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEEcsrqmqtekkrLQQHIQELEahleaeegA 990
Cdd:PRK04863 278 ANERRVHLEE---ALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESD-----------LEQDYQAAS--------D 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 991 RQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRK 1070
Cdd:PRK04863 336 HLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1071 EEKGRQELEKLKRRLDGES------SELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEdeggARAQLLKSLREAQAA 1144
Cdd:PRK04863 416 YQQAVQALERAKQLCGLPDltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFE----QAYQLVRKIAGEVSR 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1145 LAEAQEDLESERVARTKaekqrRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEetrihEAAVQELRQ 1224
Cdd:PRK04863 492 SEAWDVARELLRRLREQ-----RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDELEQLQE 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1225 RHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAE----------LSSLQTARQEGEQRRRRLELQLQEVQGRAG 1294
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaaqdaLARLREQSGEEFEDSQDVTEYMQQLLERER 641
|
410 420
....*....|....*....|....*.
gi 116284396 1295 DGERARAEAAEKLQRAQAELENVSGA 1320
Cdd:PRK04863 642 ELTVERDELAARKQALDEEIERLSQP 667
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
879-1237 |
1.78e-05 |
|
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: 49.95 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 879 LQARAQELQKVQE-LQQQsarevGELQGRVAQLEEERARLAEQlraeAELCAEAEETRGRLAARKQELELVVSELEARVG 957
Cdd:COG3096 329 YQAASDHLNLVQTaLRQQ-----EKIERYQEDLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 958 EEEECSRQMQTEKKRLQQHIQELEAhleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERKLLEDRLAEFS 1037
Cdd:COG3096 400 DYQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLSVAD 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1038 SQAAEEEEKVKSLNKlrlkyeatIADMEDRLRKEEKGRQ------ELEKLKRRLDGESSELQE--QMVEQQQRAEELRAQ 1109
Cdd:COG3096 469 AARRQFEKAYELVCK--------IAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEE 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1110 LGRK-------EEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELED 1182
Cdd:COG3096 541 FCQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 1183 TLDSTNAQQELRSK---REQEVTELKKTLEEETRIHEAAVQELRQRHGQA---LGELAEQL 1237
Cdd:COG3096 621 ALADSQEVTAAMQQlleREREATVERDELAARKQALESQIERLSQPGGAEdprLLALAERL 681
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1055-1176 |
2.14e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1055 LKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLgrkEEELQAALARAEDEGgarAQL 1134
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEI 589
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 116284396 1135 LKSLReaqaalaeAQEDLESERVARTKAEKQRRDLGEELEAL 1176
Cdd:PRK00409 590 IKELR--------QLQKGGYASVKAHELIEARKRLNKANEKK 623
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
964-1180 |
2.14e-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: 48.99 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 964 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1043
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1044 EEKVKSLNKL------------------------RLKYEATIAD-MEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVE 1098
Cdd:COG4942 103 KEELAELLRAlyrlgrqpplalllspedfldavrRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1099 QQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALaeaqedlesERVARTKAEKQRRDLGEELEALRG 1178
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI---------ARLEAEAAAAAERTPAAGFAALKG 253
|
..
gi 116284396 1179 EL 1180
Cdd:COG4942 254 KL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
875-1408 |
2.26e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.53 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 875 QDEVLQARAQE--LQKVQELQQQSArevgELQGRVAQLEEERARLaeqlraeaelcaeaeetrgRLAARKQELELvvseL 952
Cdd:COG4913 241 HEALEDAREQIelLEPIRELAERYA----AARERLAELEYLRAAL-------------------RLWFAQRRLEL----L 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 953 EARVGEEEECSRQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVtteakmKKFEEDLLLLEDQNSKLSKERKLLEDR 1032
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1033 LAEFSSQAAEEEEKVKSLNK----LRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMV----EQQQRAE 1104
Cdd:COG4913 368 LAALGLPLPASAEEFAALRAeaaaLLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSnipaRLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1105 ELRAQLGRKEEELQAAlA-----RAEDE----------GGAR----------AQLLKSLREAQAALAeaqedLESERVAR 1159
Cdd:COG4913 448 ALAEALGLDEAELPFV-GelievRPEEErwrgaiervlGGFAltllvppehyAAALRWVNRLHLRGR-----LVYERVRT 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1160 TKAEKQRRDLGEelEALRGELEdtLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHG------------ 1227
Cdd:COG4913 522 GLPDPERPRLDP--DSLAGKLD--FKPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGngtrhekddrrr 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1228 ------------QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQrrrrlELQLQEVQGRAGD 1295
Cdd:COG4913 598 irsryvlgfdnrAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWD-----EIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1296 GERARAEAAE---KLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAG 1372
Cdd:COG4913 673 LEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
570 580 590
....*....|....*....|....*....|....*.
gi 116284396 1373 LREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEE 1408
Cdd:COG4913 753 ERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1532-1681 |
2.27e-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: 48.00 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1532 RALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1610
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEyEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 1611 AGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKE 1681
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1162-1937 |
2.75e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1162 AEKQRRDLGEELEALRGELEDTLDSTNAQQELR---SKREQEVTELKKTLEEE---TRIHEAAVQE-LRQ-----RHGQA 1229
Cdd:PRK04863 277 HANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaASDHLNLVQTaLRQqekieRYQAD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1230 LGELAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrLELQlqevQGRAG---DGERA 1299
Cdd:PRK04863 357 LEELEERLEEqnevveeADEQQEENEARAEAAEEEVDELKSQLADYQQA----------LDVQ----QTRAIqyqQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1300 RAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLR-EQLE 1378
Cdd:PRK04863 423 LERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVaRELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1379 EEAAARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQELDDAT 1458
Cdd:PRK04863 503 RRLREQRHLAEQLQQLRMRLSELEQRLRQQQRA-----------ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1459 MDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraveereraeaegrerearalsltraleeeqeareeLERQNRALRAEL 1538
Cdd:PRK04863 572 ESVSEARERRMALRQQLEQLQARIQRLAA---------------------------------------RAPAWLAAQDAL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1539 EALLS-SKDDVGKSvheleracrvaeQAANDLRAQVTELEDELTAAEDaklRLEVTVQALKTQHERdLQGRDEAGEERRR 1617
Cdd:PRK04863 613 ARLREqSGEEFEDS------------QDVTEYMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPRLN 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1618 QLAK---------------------------QLRDAEVERDEERKQRTLAvaarkKLEGELEEL------KAQMASAGQG 1664
Cdd:PRK04863 677 ALAErfggvllseiyddvsledapyfsalygPARHAIVVPDLSDAAEQLA-----GLEDCPEDLyliegdPDSFDDSVFS 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1665 KEEAVKQLrkmqaQMKELWREVEETRTSREEIFSQnRESEKRLKGLEAEVLRLQEELAASDRaRRQAQQDRDEMADEVAN 1744
Cdd:PRK04863 752 VEELEKAV-----VVKIADRQWRYSRFPEVPLFGR-AAREKRIEQLRAEREELAERYATLSF-DVQKLQRLHQAFSRFIG 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1745 GNLSKA------AILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELS--AERSFSAKAESGRQQLE 1816
Cdd:PRK04863 825 SHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLD 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1817 RqiqelrgrlGEEDAGARARHKMTIAALE---SKLAQAEEQLEQETRERILSGKLVRRAEKR---LKEVVlqveeERRVA 1890
Cdd:PRK04863 905 E---------AEEAKRFVQQHGNALAQLEpivSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQafaLTEVV-----QRRAH 970
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 116284396 1891 ---DQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTE 1937
Cdd:PRK04863 971 fsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
990-1324 |
2.97e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.53 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 990 ARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLN------KLRLK-YEATIA 1062
Cdd:pfam19220 42 ELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEaakeelRIELRdKTAQAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1063 DMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEG------GAR-AQLL 1135
Cdd:pfam19220 122 ALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAaelaelTRRlAELE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1136 KSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIH 1215
Cdd:pfam19220 202 TQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1216 EAAVQEL---RQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGR 1292
Cdd:pfam19220 282 ERRLKEAsieRDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSDRIAELTKR 361
|
330 340 350
....*....|....*....|....*....|....*.
gi 116284396 1293 ----AGDGERARAEAAEKLQRAQAELENVSGALNEA 1324
Cdd:pfam19220 362 feveRAALEQANRRLKEELQRERAERALAQGALEIA 397
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1532-1955 |
3.06e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1532 RALRAELEALLSSKDDVGKSVHELERAcrvaEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQHE-RDLQGRDE 1610
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1611 AGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKL----EGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREV 1686
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1687 EETRTSREEIFSQNRESEKR-----------LKGLEAEVLRLQEELAA---------------SDRARRQAQQDRDEMAD 1740
Cdd:COG4717 230 EQLENELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGvlflvlgllallfllLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1741 EVANGNLSKAAILEEKRQLEgrlgqleeeleeeqSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAEsgRQQLERQIQ 1820
Cdd:COG4717 310 LPALEELEEEELEELLAALG--------------LPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1821 ELRGRLG---EEDAGARARHKMTIAALESKLAQAEEQLEQETRERILSgkLVRRAEKRLKEVVLQVEEERRVADQLRDQL 1897
Cdd:COG4717 374 ALLAEAGvedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEEL--LEALDEEELEEELEELEEELEELEEELEEL 451
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1898 EKGNLRVKQLKRQLeEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:COG4717 452 REELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1151-1371 |
3.28e-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: 48.61 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1151 DLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQAL 1230
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1231 GELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRA 1310
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 1311 QAELENVSGALNEAESKTIRLSKELSSTEAQLhdaQELLQEETRAKLALGSRVRAMEAEAA 1371
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAEL---AELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1061-1245 |
3.53e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1061 IADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDeggARAQL--LKSL 1138
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1139 REAQAALAeaqeDLESERVARTKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKTLEEETRIHEAA 1218
Cdd:COG1579 89 KEYEALQK----EIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170 180 190
....*....|....*....|....*....|.
gi 116284396 1219 VQELRQRHGQALGELAEQL----EQARRGKG 1245
Cdd:COG1579 158 LEELEAEREELAAKIPPELlalyERIRKRKN 188
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1600-1910 |
4.92e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1600 QHERDLQGRDEAGEERRRQL--AKQLRDAEVERDEE-RKQRTLAVAARKKLEGELEELKAQMASAgQGKEEAVKQLRKMQ 1676
Cdd:PRK04863 276 RHANERRVHLEEALELRRELytSRRQLAAEQYRLVEmARELAELNEAESDLEQDYQAASDHLNLV-QTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1677 AQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRA----------RRQAQQDRDEM-----ADE 1741
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALERAkqlcgLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1742 VANGNLSkaAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSF-----------SAKAES 1810
Cdd:PRK04863 435 LTADNAE--DWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvarellrrlrEQRHLA 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1811 GR-QQLERQIQELRGRLGEEdagararhkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRV 1889
Cdd:PRK04863 513 EQlQQLRMRLSELEQRLRQQ------------QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARER 580
|
330 340
....*....|....*....|.
gi 116284396 1890 ADQLRDQLEKGNLRVKQLKRQ 1910
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAAR 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1093-1347 |
5.20e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 5.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1093 QEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLReaqaalaeaqedleservartKAEKQRRDLGEE 1172
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---------------------ALARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1173 LEALRGELEDTldsTNAQQELRSKREQEVTELKKTLeeetriheAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRL 1252
Cdd:COG4942 78 LAALEAELAEL---EKEIAELRAELEAQKEELAELL--------RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1253 ALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLS 1332
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
250
....*....|....*
gi 116284396 1333 KELSSTEAQLHDAQE 1347
Cdd:COG4942 227 ALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1532-1955 |
5.48e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1532 RALRAELEALLSSKDDVGKSVHELERACRVAEQAAND--------LRAQVTELEDELTAAEDAKLRLEVTVQALKTQHER 1603
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1604 DLqgrdEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGK---EEAVKQLRKMQA--- 1677
Cdd:COG4913 378 SA----EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDALAeal 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1678 --------------QMKEL---WRE--------------------------VEET------RTSREEIFSQNRESEKRLK 1708
Cdd:COG4913 454 gldeaelpfvgeliEVRPEeerWRGaiervlggfaltllvppehyaaalrwVNRLhlrgrlVYERVRTGLPDPERPRLDP 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1709 G----------------LEAEVLRL--------QEELAASDRA-----------RRQAQQDRDEMADEVANG--NLSKAA 1751
Cdd:COG4913 534 DslagkldfkphpfrawLEAELGRRfdyvcvdsPEELRRHPRAitragqvkgngTRHEKDDRRRIRSRYVLGfdNRAKLA 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1752 ILEEKR-QLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAersfsakaesgrQQLERQIQELRGRLGEED 1830
Cdd:COG4913 614 ALEAELaELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV------------ASAEREIAELEAELERLD 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1831 AGararhKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGnlRVKQLKRQ 1910
Cdd:COG4913 682 AS-----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE--LRALLEER 754
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 116284396 1911 LEEAEEEASRAQAgRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:COG4913 755 FAAALGDAVEREL-RENLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
823-1237 |
7.42e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 823 RGYLARRAFQKRQQQQSALRVMQRNCAAYLKLRHwqwwRLFTKVKPLLQVTRQDEVLQARAQELQKVQELQ------QQS 896
Cdd:COG4717 62 QGRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLEKLLQLLplyqelEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 897 AREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELV----VSELEARVGEEEECSRQMQTEKKR 972
Cdd:COG4717 138 EAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAteeeLQDLAEELEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 973 LQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL--------------------------LLEDQNSKLSKER 1026
Cdd:COG4717 218 AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlallglggsllsliltiagvlflvlgLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1027 KLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRA--- 1103
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAlla 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1104 -------EELRAQLGRKEE--ELQAALARAEDEGGARAQLLKSLrEAQAALAEAQEDLESERVARTKAEKQRRDLGEELE 1174
Cdd:COG4717 378 eagvedeEELRAALEQAEEyqELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116284396 1175 ALRGELEDtLDSTNAQQELRSKREQEVTELKKTLEEETRIH------EAAVQELRQRHGQALGELAEQL 1237
Cdd:COG4717 457 ELEAELEQ-LEEDGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPPVLERASEY 524
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1115-1484 |
8.01e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1115 EELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLES--ERVARTKAEKQRRDLGEELEALRGELEDT---LDSTNA 1189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1190 QQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQ 1269
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1270 TARQEGEQRRRRLELQ-----------LQEVQGRAGDGERARAEAA-----------EKLQRAQAELENVSGALNEAESK 1327
Cdd:COG4717 234 NELEAAALEERLKEARlllliaaallaLLGLGGSLLSLILTIAGVLflvlgllallfLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1328 TIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQE- 1406
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1407 --------------EEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQlVSTLE 1472
Cdd:COG4717 394 aeeyqelkeeleelEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELA 472
|
410
....*....|..
gi 116284396 1473 KKQRKFDQLLAE 1484
Cdd:COG4717 473 ELLQELEELKAE 484
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
826-1357 |
9.19e-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: 47.81 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 826 LARRAFQKRQQQ---QSALRVMQRNCAAYLKLRHWQWWRLFTKVKPLlqvtrQDEVLQARAQELQKVQELQQQ---SARE 899
Cdd:pfam15921 283 LTEKASSARSQAnsiQSQLEIIQEQARNQNSMYMRQLSDLESTVSQL-----RSELREAKRMYEDKIEELEKQlvlANSE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 900 VGELQGRVAQLEEERARLAEQLRAEAELcaeaeetrgrLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQE 979
Cdd:pfam15921 358 LTEARTERDQFSQESGNLDDQLQKLLAD----------LHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNME 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 980 LEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLrlkyea 1059
Cdd:pfam15921 428 VQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDL------ 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1060 tIADMEDRLRKEEKGRQELEKLKRRLDGESSELQE--------------------QMVEQQQRAEELRAQL--------- 1110
Cdd:pfam15921 502 -TASLQEKERAIEATNAEITKLRSRVDLKLQELQHlknegdhlrnvqtecealklQMAEKDKVIEILRQQIenmtqlvgq 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1111 -GRKEEELQAALARAEDEGGARAQLLKSLR-------EAQAALAEAQEDLESERVARTKAEKQR----RDLGEELEALRG 1178
Cdd:pfam15921 581 hGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLELEKVKLVNAGSERlravKDIKQERDQLLN 660
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1179 ELEDTLDSTNAQQElrskrEQEVteLKKTLEEETRIHEAAVQELRQRHGQALGELAE---QLEQARRGKGAWEKTRLALE 1255
Cdd:pfam15921 661 EVKTSRNELNSLSE-----DYEV--LKRNFRNKSEEMETTTNKLKMQLKSAQSELEQtrnTLKSMEGSDGHAMKVAMGMQ 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1256 AEVSELRAELSSLQTarqegeqRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKEL 1335
Cdd:pfam15921 734 KQITAKRGQIDALQS-------KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKV 806
|
570 580 590
....*....|....*....|....*....|...
gi 116284396 1336 SSTEAQLHDA-----------QELLQEETRAKL 1357
Cdd:pfam15921 807 ANMEVALDKAslqfaecqdiiQRQEQESVRLKL 839
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1530-1721 |
9.73e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.44 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1530 QNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKtQHERDLQGRD 1609
Cdd:COG1340 51 QVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIE-RLEWRQQTEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1610 EAGEERRR------QLAKQLRDAEVERDEERKQRTLavaarkklEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELW 1683
Cdd:COG1340 130 LSPEEEKElvekikELEKELEKAKKALEKNEKLKEL--------RAELKELRKEAEEIHKKIKELAEEAQELHEEMIELY 201
|
170 180 190
....*....|....*....|....*....|....*...
gi 116284396 1684 REVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEEL 1721
Cdd:COG1340 202 KEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1563-1702 |
1.05e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 46.88 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1563 EQAANDLRAQVTELEDELTAAEDAKLRLEVTVQALK-----TQHERD-LQGRDEAGEERRRQLAKQLRDAEVERDEERKQ 1636
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRaslsaAEAERSrLQALLAELAGAGAAAEGRAGELAQELDSEKQV 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116284396 1637 RTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWR--------EVEETRTSREEIFSQNRE 1702
Cdd:PRK09039 132 SARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRrlnvalaqRVQELNRYRSEFFGRLRE 205
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1705-1955 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1705 KRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADevangnlskaaiLEEKRQLEGRLgqleeELEEEQSNSELLNDRY 1784
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEPIRELAERYAAARER------------LAELEYLRAAL-----RLWFAQRRLELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1785 RKLLLQVESLTTELSAersfsakAESGRQQLERQIQELRGRLgEEDAGARarhkmtIAALESKLAQAEEQLEQETRERil 1864
Cdd:COG4913 298 EELRAELARLEAELER-------LEARLDALREELDELEAQI-RGNGGDR------LEQLEREIERLERELEERERRR-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1865 sgklvRRAEKRLKEVVLQVEEER----RVADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAE 1940
Cdd:COG4913 362 -----ARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
250
....*....|....*
gi 116284396 1941 SMNREVTTLRNRLRR 1955
Cdd:COG4913 437 NIPARLLALRDALAE 451
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
894-1359 |
1.68e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 894 QQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEeeecsrqmqtekkrl 973
Cdd:pfam12128 237 MKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKE--------------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 974 qqhiqeleahleaeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER----KLLEDRLAEFSSQAAEEEEKVKS 1049
Cdd:pfam12128 302 ----------------KRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADietaAADQEQLPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1050 L----NKLRLKYEATIAdmedrLRKEEKGRqELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLgrkEEELQAALARAE 1125
Cdd:pfam12128 366 LtgkhQDVTAKYNRRRS-----KIKEQNNR-DIAGIKDKLAKIREARDRQLAVAEDDLQALESEL---REQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1126 DEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRrdlgEELEALRGELEdtlDSTNAQQELRSKREQEVTELk 1205
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAR----EEQEAANAEVE---RLQSELRQARKRRDQASEAL- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1206 ktleeetRIHEAAVQELRQRHGQALGELAEQ----LEQARRGKGAWEKTRLALEAEVSELRAELS-SLQTARQEGEQRRR 1280
Cdd:pfam12128 509 -------RQASRRLEERQSALDELELQLFPQagtlLHFLRKEAPDWEQSIGKVISPELLHRTDLDpEVWDGSVGGELNLY 581
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116284396 1281 RLELQLQEVQgragdgeraRAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQellQEETRAKLAL 1359
Cdd:pfam12128 582 GVKLDLKRID---------VPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKAS---REETFARTAL 648
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1165-1487 |
1.69e-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: 46.87 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1165 QRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAV------------QELRQRHGQALGE 1232
Cdd:COG3096 279 ERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASdhlnlvqtalrqQEKIERYQEDLEE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1233 LAEQLEQ-------ARRGKGAWEKTRLALEAEVSELRAELSSLQTArqegeqrrrrlelqLQEVQGRAGDGERAR---AE 1302
Cdd:COG3096 359 LTERLEEqeevveeAAEQLAEAEARLEAAEEEVDSLKSQLADYQQA--------------LDVQQTRAIQYQQAVqalEK 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1303 AAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAA-GLREQLEEEA 1381
Cdd:COG3096 425 ARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVERSQAwQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1382 AARERAGRELQTAQAQLSEWRRRQEEEAGAleageearrraAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDL 1461
Cdd:COG3096 505 RSQQALAQRLQQLRAQLAELEQRLRQQQNA-----------ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQA 573
|
330 340 350
....*....|....*....|....*....|
gi 116284396 1462 ----EQQRQLVSTLEKKQRKFDQLLAEEKA 1487
Cdd:COG3096 574 aeavEQRSELRQQLEQLRARIKELAARAPA 603
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1429-1662 |
1.88e-04 |
|
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: 45.91 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1429 LTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEekaavlraveereraeaegREREA 1508
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-------------------LEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1509 RALSLTRALEEEQEAREELERQNRALRAELEALLSSKD--DVGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDA 1586
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1587 KLRLEVTVQALKTQHERdLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAG 1662
Cdd:COG4942 173 RAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1698-1933 |
1.90e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1698 SQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEvangnlskaailEEKRQLEGRLGQLEEELEEEQSNS 1777
Cdd:COG3206 168 LRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS------------EEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1778 ELLNDRYRKLLLQVESLTTELSAersfsAKAESGRQQLERQIQELRGRLGEEDAGARARHKmTIAALESKLAQAEEQLEQ 1857
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPE-----LLQSPVIQQLRAQLAELEAELAELSARYTPNHP-DVIALRAQIAALRAQLQQ 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1858 ETRerilsgklvrraeKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLkrqleeaeeeaSRAQAGRRRLQRELE 1933
Cdd:COG3206 310 EAQ-------------RILASLEAELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVE 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1333-1955 |
1.91e-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: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1333 KELSSTEAQLHDAQEllQEETRAKL-ALGSRVRAMEAEAAGLREQLEEEAAARERAGRELqtAQAQLSEWRRRQEEEAGA 1411
Cdd:COG4913 235 DDLERAHEALEDARE--QIELLEPIrELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1412 LEAGEEARRRAAREAEALTQRLAE-KTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEkkqrkfdqLLAEEKAAVL 1490
Cdd:COG4913 311 LERLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALG--------LPLPASAEEF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1491 RAVEERERAEAEGREREARALSLTRALEEEQEAREELerQNRALRAELEALLSSKDDVGKSVHEL-ERACRVAEQAANDL 1569
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRR--ELRELEAEIASLERRKSNIPARLLALrDALAEALGLDEAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1570 RA-----QVTELEDE--------------------------LTAAEDAKLRLEVTVQALKTQHERDLQGRDEAG------ 1612
Cdd:COG4913 461 PFvgeliEVRPEEERwrgaiervlggfaltllvppehyaaaLRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDslagkl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1613 --------EERRRQLAKQLRDAEVERDEERKQRTLAV--------------------------------AARKKLEGELE 1652
Cdd:COG4913 541 dfkphpfrAWLEAELGRRFDYVCVDSPEELRRHPRAItragqvkgngtrhekddrrrirsryvlgfdnrAKLAALEAELA 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1653 ELKAQMASAGQGKEEAVKQLRKMQAQmKELWREVEETRtsreeifsqnrESEKRLKGLEAEVLRLQEELAASDRArrqaQ 1732
Cdd:COG4913 621 ELEEELAEAEERLEALEAELDALQER-REALQRLAEYS-----------WDEIDVASAEREIAELEAELERLDAS----S 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1733 QDRDEMADEVAngnlskaAILEEKRQLEGRLGQleeeleeeqsnselLNDRYRKLLLQVESLTTEL-SAERSFSAKAESG 1811
Cdd:COG4913 685 DDLAALEEQLE-------ELEAELEELEEELDE--------------LKGEIGRLEKELEQAEEELdELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1812 RQQLERQIQELRGRLGEEDAGARARHKMT--IAALESKLAQAEEQLEQETRErilsgkLVRRAEKRLKEVVLQVEEERRV 1889
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEerIDALRARLNRAEEELERAMRA------FNREWPAETADLDADLESLPEY 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1890 ADQLrDQLEKGNLRVKqlkrqleeaeeeasRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:COG4913 818 LALL-DRLEEDGLPEY--------------EERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
682-706 |
2.32e-04 |
|
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: 43.87 E-value: 2.32e-04
10 20
....*....|....*....|....*
gi 116284396 682 YKESLSRLMATLSNTNPSFVRCIVP 706
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1015-1127 |
2.73e-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: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1015 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRK-----------------------E 1071
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnkeyealqkeiesL 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1072 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDE 1127
Cdd:COG1579 102 KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
867-1179 |
3.18e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.63 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 867 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERA-RLAEQLRAEAELCAEAEETRGRLAARK 942
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 943 ---QELELVVSELEARVGEEEECSRQMQTEK--KRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE- 1016
Cdd:pfam02029 105 ennEEEENSSWEKEEKRDSRLGRYKEEETEIreKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKi 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1017 DQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQE----LEKLKRRLDGESSEL 1092
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeqkLEELRRRRQEKESEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1093 QEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARaqllkslreaqaalaeaqedlESERVARTKAEKQRrdLGEE 1172
Cdd:pfam02029 265 FEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQE---------------------EAERKLREEEEKRR--MKEE 321
|
....*..
gi 116284396 1173 LEALRGE 1179
Cdd:pfam02029 322 IERRRAE 328
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1636-1906 |
3.25e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1636 QRTLA-VAARKKLEGELEELKAQMAsagqgkeEAVKQLRKMQAQMKELWREVEETRTSREEIFSqNRESEKRLKGLEAEV 1714
Cdd:PRK11281 66 EQTLAlLDKIDRQKEETEQLKQQLA-------QAPAKLRQAQAELEALKDDNDEETRETLSTLS-LRQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1715 LRLQEELA-----------ASDRARRQ---AQQDRDEMADEVANGNLSKAAILEEKRQLegrlgqleeeleeEQSNSELL 1780
Cdd:PRK11281 138 QNAQNDLAeynsqlvslqtQPERAQAAlyaNSQRLQQIRNLLKGGKVGGKALRPSQRVL-------------LQAEQALL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1781 N--DRYRKLLLQVESLTTELSAERSFSAKAESgrQQLERQIQELRGRLGEEDagararhkmtiaaLESKLAQAEEQLEQE 1858
Cdd:PRK11281 205 NaqNDLQRKSLEGNTQLQDLLQKQRDYLTARI--QRLEHQLQLLQEAINSKR-------------LTLSEKTVQEAQSQD 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 116284396 1859 TRERILSGKLVRRaekrlkevvlQVEEERRVADQLRDQLEKGN------LRVKQ 1906
Cdd:PRK11281 270 EAARIQANPLVAQ----------ELEINLQLSQRLLKATEKLNtltqqnLRVKN 313
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
870-1095 |
4.13e-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: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 870 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAAR-------- 941
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvlsrsi 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 942 ---KQELELVVSELEARVGEEEECSRQmqteKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ 1018
Cdd:TIGR04523 478 nkiKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1019 N----------------SKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLK 1082
Cdd:TIGR04523 554 LkkenlekeideknkeiEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII 633
|
250
....*....|...
gi 116284396 1083 RRLDGESSELQEQ 1095
Cdd:TIGR04523 634 KNIKSKKNKLKQE 646
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1616-1761 |
4.26e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1616 RRQLAKQLRDAEVERDEERKQRTLAVAARKKlEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKelwREVEETRTSREE 1695
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANR-EAEEAELEQEREIETARIAEAEAELAKKKAEER---REAETARAEAEA 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1696 IFSQNRESEKRLKGLEAEVLRLQE--ELAASDRARRQAQQDRDEMADEVANgnlSKAAILEEKRQLEG 1761
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAEREReiELQEKEAEREEAELEADVRKPAEAE---KQAAEAEAEAEAEA 331
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
796-1091 |
4.93e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 796 RAGVLAQLEEERDLKVTDIIVSFQAAargylarRAFQKRQQQQSALRVMQRNCAAYLKLRHWQWWRLFTK-VKPLLQVTR 874
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKM-------KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEeKKKAEELKK 1654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 875 QDEVLQARAQELQKVQELQQQSAREvgelqgrVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEA 954
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEE-------AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 955 RVGEEEECSRQMQTEKKRLQQhiqeleahLEAEEGARQKLQLEKVTTEAKMKKF--EEDLLLLEDQNSKLSKERKLLEDR 1032
Cdd:PTZ00121 1728 NKIKAEEAKKEAEEDKKKAEE--------AKKDEEEKKKIAHLKKEEEKKAEEIrkEKEAVIEEELDEEDEKRRMEVDKK 1799
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1033 LAEFSSQAAEEEEKVKS----LNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSE 1091
Cdd:PTZ00121 1800 IKDIFDNFANIIEGGKEgnlvINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGE 1862
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1299-1488 |
5.64e-04 |
|
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: 44.37 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1299 ARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLE 1378
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1379 EEAAARERAGRELQT-----------AQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEKTETVDRLERGR 1447
Cdd:COG4942 101 AQKEELAELLRALYRlgrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 116284396 1448 RRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAA 1488
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1039-1246 |
5.86e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 45.31 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1039 QAAEEEEKVKSLNKLRLKY---EATIADMEDRLRKE-EKGRQELEKLKRRLDGE---SSELQEQM---VEQQQRAEELRA 1108
Cdd:PLN03188 1038 PESTDESPEKKLEQERLRWteaESKWISLAEELRTElDASRALAEKQKHELDTEkrcAEELKEAMqmaMEGHARMLEQYA 1117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1109 QLGRKEEELQAALARAED------EGGARAQLLKSLREAQAALAEAQEDLESERvartkaEKQRRDLGEELEALRGELED 1182
Cdd:PLN03188 1118 DLEEKHIQLLARHRRIQEgiddvkKAAARAGVRGAESKFINALAAEISALKVER------EKERRYLRDENKSLQAQLRD 1191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1183 TLDSTNAQQEL--RSKREQE--VTELKKTLEEETRIHEA--AVQELRQRHGQALGELAEQLEQARRGKGA 1246
Cdd:PLN03188 1192 TAEAVQAAGELlvRLKEAEEalTVAQKRAMDAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1618-1903 |
5.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1618 QLAKQLRDAEVERDEERKQRTlAVAARKKLEGELEELKAQMASAgqgkEEAVKQLRKmqaqmkelwreveetrtsREEIF 1697
Cdd:COG3206 152 AVANALAEAYLEQNLELRREE-ARKALEFLEEQLPELRKELEEA----EAALEEFRQ------------------KNGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1698 SqnreSEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANGNLSKAAILEekrqlegrlgqleeeleeeqsns 1777
Cdd:COG3206 209 D----LSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ----------------------- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1778 ellNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEEDAGARARHKMTIAALESKLAQAEEQLEQ 1857
Cdd:COG3206 262 ---SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 116284396 1858 eTRERILSgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLR 1903
Cdd:COG3206 339 -LEARLAE---LPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
992-1341 |
5.95e-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: 45.01 E-value: 5.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 992 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKE 1071
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1072 EKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEElqaalaraedeggaraqlLKSLREAQAALAEAQED 1151
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE------------------IKDLTNQDSVKELIIKN 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1152 LEServARTKAEKQRRDLGEELEALRGELEDTldstnaQQELRSKreqeVTELKKtLEEETRIHEAAVQELRQRHGQaLG 1231
Cdd:TIGR04523 459 LDN---TRESLETQLKVLSRSINKIKQNLEQK------QKELKSK----EKELKK-LNEEKKELEEKVKDLTKKISS-LK 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1232 ELAEQLEQarrgkgawEKTRlaLEAEVSELRAELSSLQTARQEGEQRRRRLELQ--LQEVQGRAGDGERARAEAAEKLQR 1309
Cdd:TIGR04523 524 EKIEKLES--------EKKE--KESKISDLEDELNKDDFELKKENLEKEIDEKNkeIEELKQTQKSLKKKQEEKQELIDQ 593
|
330 340 350
....*....|....*....|....*....|..
gi 116284396 1310 AQAELENVSGALNEAESKTIRLSKELSSTEAQ 1341
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
907-1309 |
6.46e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 907 VAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEE--CSRQMQTEKKRLQQHIQELEAhl 984
Cdd:pfam02029 7 AARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeaFLDRTAKREERRQKRLQEALE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 985 eaeegaRQKlQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLlEDRLAEfssqAAEEEEKVKSLNKLRLKYEATIADM 1064
Cdd:pfam02029 85 ------RQK-EFDPTIADEKESVAERKENNEEEENSSWEKEEKR-DSRLGR----YKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1065 EDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAA 1144
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1145 LAEAQEDLESERVARTKAEKQRRDLGE----ELEALRGEledtldstnaQQElrskREQEVTELKKTLEEETRIHEAavq 1220
Cdd:pfam02029 233 SQEREEEAEVFLEAEQKLEELRRRRQEkeseEFEKLRQK----------QQE----AELELEELKKKREERRKLLEE--- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1221 ELRQRhgqalgelaEQLEQARRGKGAWEKTRLALEAEvselraelsslqtarqegeqrrrrlelqlqevqgragdgeRAR 1300
Cdd:pfam02029 296 EEQRR---------KQEEAERKLREEEEKRRMKEEIE----------------------------------------RRR 326
|
....*....
gi 116284396 1301 AEAAEKLQR 1309
Cdd:pfam02029 327 AEAAEKRQK 335
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
884-1225 |
6.68e-04 |
|
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: 44.96 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 884 QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCAEAEETRgrLAARKQELELVVSELEARVGEEEECS 963
Cdd:pfam02463 670 ELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE--LLADRVQEAQDKINEELKLLKQKIDE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 964 RQMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLledrlaefssQAAEE 1043
Cdd:pfam02463 748 EEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE----------EAELL 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1044 EEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqmvEQQQRAEELRAQLGRKEEELQAALAR 1123
Cdd:pfam02463 818 EEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEEL---LQELLLKEEELEEQKLKDELESKEEK 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1124 AEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDstnaQQELRSKREQEVTE 1203
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE----EEEERNKRLLLAKE 970
|
330 340
....*....|....*....|..
gi 116284396 1204 LKKTLEEETRIHEAAVQELRQR 1225
Cdd:pfam02463 971 ELGKVNLMAIEEFEEKEERYNK 992
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
947-1400 |
6.83e-04 |
|
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: 44.71 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 947 LVVSELEARVGEEEECSRqmqTEKKRLQQHIQELEAHLEAEEgaRQKLQLEKVTTEAKMKKFE-EDLLLLEDQNSKLSKE 1025
Cdd:pfam05483 349 FVVTEFEATTCSLEELLR---TEQQRLEKNEDQLKIITMELQ--KKSSELEEMTKFKNNKEVElEELKKILAEDEKLLDE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1026 RKLLEDRLAEFSSQAAEE----EEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVE 1098
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieLTAHCDKLLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1099 QQQRAEELRAQLGRKEEELQAALARAEdeggaraQLLKSLREAQAALAEAQEDLESERvartKAEKQRRDlgeELEALRG 1178
Cdd:pfam05483 504 LTQEASDMTLELKKHQEDIINCKKQEE-------RMLKQIENLEEKEMNLRDELESVR----EEFIQKGD---EVKCKLD 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1179 ELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHgqalgelaeqleQARRGKGAWEKTRL-ALEAE 1257
Cdd:pfam05483 570 KSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEN------------KALKKKGSAENKQLnAYEIK 637
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1258 VSELRAELSSL-QTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAE--KLQ-----RAQAELENVSGALNEAESKTI 1329
Cdd:pfam05483 638 VNKLELELASAkQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEavKLQkeidkRCQHKIAEMVALMEKHKHQYD 717
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 1330 RLSKELSStEAQLHDAQEllQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSE 1400
Cdd:pfam05483 718 KIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1750-1955 |
7.71e-04 |
|
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: 43.98 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1750 AAILEEKRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGRLGEe 1829
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1830 dagARARHKMTIAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQLKR 1909
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 116284396 1910 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1552-1831 |
9.24e-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: 44.56 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1552 VHELERACRVAEQAANDLRAQVTELEDELTAAED----AKLRLEVTVQALKTQHERDLQ--------------------- 1606
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEevdsLKSQLADYQQALDVQQTRAIQyqqavqalekaralcglpdlt 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1607 ------------GRDEAGEERRRQLAKQLRDAEVERDEERKqrtlAVAARKKLEGE-------------LEELKAQMASA 1661
Cdd:COG3096 436 penaedylaafrAKEQQATEEVLELEQKLSVADAARRQFEK----AYELVCKIAGEversqawqtarelLRRYRSQQALA 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1662 GQGK---------EEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQ 1732
Cdd:COG3096 512 QRLQqlraqlaelEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLR 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1733 QDRDEMADEvANGNLSKAAILEekrQLEGRLGQLEEELEEEqsnsellnDRYRKLLLQVEsltTELSAERSFSAKAesgR 1812
Cdd:COG3096 592 ARIKELAAR-APAWLAAQDALE---RLREQSGEALADSQEV--------TAAMQQLLERE---REATVERDELAAR---K 653
|
330
....*....|....*....
gi 116284396 1813 QQLERQIQELRGRLGEEDA 1831
Cdd:COG3096 654 QALESQIERLSQPGGAEDP 672
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1026-1208 |
9.72e-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: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1026 RKLLEdrLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEqmveqqqRAEE 1105
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA-------RIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1106 LRAQLG--RKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDT 1183
Cdd:COG1579 78 YEEQLGnvRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170 180
....*....|....*....|....*
gi 116284396 1184 LDstnaqqELRSKREQEVTELKKTL 1208
Cdd:COG1579 158 LE------ELEAEREELAAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1059-1326 |
9.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1059 ATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE---LQAALARAEDEGGARAQLL 1135
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEidkLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1136 KSLREAQAALAEAQEDLE------------SERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTE 1203
Cdd:COG3883 89 GERARALYRSGGSVSYLDvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1204 LKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAweKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLE 1283
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA--AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 116284396 1284 LQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAES 1326
Cdd:COG3883 247 AGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGA 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1431-1955 |
1.10e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1431 QRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAavlraVEERERAEAEGREREARA 1510
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRK-----LEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1511 LSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAE---QAANDLRAQVTELEDELTAAEDAK 1587
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1588 LRLEVTVQALktqhERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASagqgKEE 1667
Cdd:PRK03918 355 EELEERHELY----EEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE----LKK 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1668 AVKQLRKMQAQMKELWREVEETRtsREEIFsqnRESEKRLKGLEAEVLRLQEELaasDRARRQAQQDRDEMADEVANGNL 1747
Cdd:PRK03918 427 AIEELKKAKGKCPVCGRELTEEH--RKELL---EEYTAELKRIEKELKEIEEKE---RKLRKELRELEKVLKKESELIKL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1748 SKaaILEEKRQLEGRL-GQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSFsakaESGRQQLERQIQELRGRL 1826
Cdd:PRK03918 499 KE--LAEQLKELEEKLkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL----KKKLAELEKKLDELEEEL 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1827 GEEDAGARARHKMTIAALESKLaqaeEQLEQETRERILsgklVRRAEKRLKEVVLQVEEERRVADQLRDQLEKGNLRVKQ 1906
Cdd:PRK03918 573 AELLKELEELGFESVEELEERL----KELEPFYNEYLE----LKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 116284396 1907 LKRQLEeaeeeasraQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:PRK03918 645 LRKELE---------ELEKKYSEEEYEELREEYLELSRELAGLRAELEE 684
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
902-1167 |
1.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 902 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSELEARVGEEEECSRQMQTEKKRLQQHIQELE 981
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 982 AHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERkllEDRLAEFSSQAAEEEEKVKSLNKLRLKyeatI 1061
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKELEKAKKALEKNEK----L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1062 ADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREA 1141
Cdd:COG1340 163 KELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
250 260
....*....|....*....|....*.
gi 116284396 1142 QAALAEAQEDLESERVARTKAEKQRR 1167
Cdd:COG1340 243 RKELKKLRKKQRALKREKEKEELEEK 268
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
902-1356 |
1.44e-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: 43.56 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 902 ELQGRVAQLEEERARLAEQLRAEAELCAEAEETRGRLAARKQELELVVSE----------LEARVGEEEECSRQMQTEKK 971
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 972 RLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSL 1050
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1051 NKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSE----LQEQMVEQQQRAEELRAQLGRKEEELQAALARAED 1126
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1127 EGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNaqqelrsKREQEVTELKK 1206
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN-------NKEVELEELKK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1207 TLEEEtrihEAAVQELRQrhgqaLGELAEQLEQARRGKGAWEKTRlalEAEVSELRAELSSLQTARQEGEQRRRRLELQL 1286
Cdd:pfam05483 413 ILAED----EKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1287 QEVQGR----AGDGERARAEAAEKLQRAQ---AELENVSGALNEAESKTIRLSKE---LSSTEAQLHDAQELLQEETRAK 1356
Cdd:pfam05483 481 EKEKLKnielTAHCDKLLLENKELTQEASdmtLELKKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQK 560
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1305-1853 |
1.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1305 EKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRvramEAEAAGLREQLEEEAAAR 1384
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESL----EGSKRKLEEKIRELEERI 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1385 ERAGRELQtaqaQLSEWRRRQEEeagaLEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQ 1464
Cdd:PRK03918 269 EELKKEIE----ELEEKVKELKE----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1465 RQLVSTLEKKQRKFDQLlaeEKAAVLRAVEERERAEAEGREREARALSLTRaleeeqeareelerqnraLRAELEALLSS 1544
Cdd:PRK03918 341 EELKKKLKELEKRLEEL---EERHELYEEAKAKKEELERLKKRLTGLTPEK------------------LEKELEELEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1545 KDDVGKSVHELERACRVAEQAANDLRAQVTELEDeltaaedAKLRLEVTVQALKTQHERDLQGRDEAG-----------E 1613
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAElkriekelkeiE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1614 ERRRQLAKQLRDAEVERDEER---KQRTLA---VAARKKLEG-ELEELKAQMASAGQGKEEAVKqLRKMQAQMKELWREV 1686
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESeliKLKELAeqlKELEEKLKKyNLEELEKKAEEYEKLKEKLIK-LKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1687 EETRTSREEIFSQNRESEKRLKGLEAEVL------------RLQE---------ELAASDRARRQAQQDRDEMADEVANG 1745
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEelgfesveeleeRLKElepfyneylELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1746 NLSKAAILEEKRQLEGRLGQLEEELEEeqsnsellnDRYRKLLLQVESLTTELSAERSFSAKAESGRQQLERQIQELRGR 1825
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKYSE---------EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580
....*....|....*....|....*...
gi 116284396 1826 LGEedagaRARHKMTIAALESKLAQAEE 1853
Cdd:PRK03918 703 LEE-----REKAKKELEKLEKALERVEE 725
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1042-1315 |
1.55e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.57 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1042 EEEEKVKSLNKLRLKYEAtiadmEDRLRKEEKGRQELEKLKRR---LDGESSELQEQMVEQQQRAEEL-RAQLGRKEEEL 1117
Cdd:pfam17380 288 QQQEKFEKMEQERLRQEK-----EEKAREVERRRKLEEAEKARqaeMDRQAAIYAEQERMAMERERELeRIRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1118 QAALARAEDEGGARAQLLKSLREAQAALAEA-QEDLESERVARTKAEKQRRDLGE---ELEALRGELEDTldstnAQQEL 1193
Cdd:pfam17380 363 ERIRQEEIAMEISRMRELERLQMERQQKNERvRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1194 RSKREQEVTELKKTLEEETRiHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRaelsslqTARQ 1273
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQE-RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK-------QAMI 509
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 116284396 1274 EGEQRRRRLELQLQEVQGRAGDGERARaeAAEKLQRAQAELE 1315
Cdd:pfam17380 510 EEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEME 549
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
966-1681 |
1.55e-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: 43.56 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 966 MQTEKKRLQQHIQELEAHLEAEEGARQKLQLEkvtTEAKMKKFEEDLllleDQNSKLSKERKLLEDRLAEFSSQAAEEEE 1045
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFE---NEKVSLKLEEEI----QENKDLIKENNATRHLCNLLKETCARSAE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1046 KVKSLNKLRLKYEATIADMEDRLRKEEKGRQELeklkrRLDGESS------ELQEQMVEQQQRAEELRAQLGRKEEELQA 1119
Cdd:pfam05483 170 KTKKYEYEREETRQVYMDLNNNIEKMILAFEEL-----RVQAENArlemhfKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1120 ALARAEDeggaRAQLLKSLREAQAALAEAQEDLESERVARTKAEKQrrdLGEELEALRGELEDTLDSTnaqqelrskreQ 1199
Cdd:pfam05483 245 LLIQITE----KENKMKDLTFLLEESRDKANQLEEKTKLQDENLKE---LIEKKDHLTKELEDIKMSL-----------Q 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1200 EVTELKKTLEEETRIHEAAVQELRQrhgqalgELAEQLEQArrgkgawEKTRLALEAEVSELRAELSSlqtarqegeqrr 1279
Cdd:pfam05483 307 RSMSTQKALEEDLQIATKTICQLTE-------EKEAQMEEL-------NKAKAAHSFVVTEFEATTCS------------ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1280 rrLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQ--ELLQEETRAK- 1356
Cdd:pfam05483 361 --LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKqfEKIAEELKGKe 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1357 LALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEARRRAAREAEALTQRLAEK 1436
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKH 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1437 TETVDRLERGRRRLQQELDDATmdlEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERERAEAEGREREARAL----- 1511
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKilenk 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1512 --SLTRALEEEQEAREELERQNRALR----AELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTEL----EDELT 1581
Cdd:pfam05483 596 cnNLKKQIENKNKNIEELHQENKALKkkgsAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKkiseEKLLE 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1582 AAEDAKLRLEvtvQALKTQHERDLQGRDEAG------EERRRQLAK--QLRDAEVERDEERKQRTlaVAARKKLEGELEE 1653
Cdd:pfam05483 676 EVEKAKAIAD---EAVKLQKEIDKRCQHKIAemvalmEKHKHQYDKiiEERDSELGLYKNKEQEQ--SSAKAALEIELSN 750
|
730 740
....*....|....*....|....*...
gi 116284396 1654 LKAQMASAGQGKEEAVKQLRKMQAQMKE 1681
Cdd:pfam05483 751 IKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1209-1763 |
1.66e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1209 EEETRIHEAAVQELRQRHGQA----LGELAEQLEQARRGKGAWE---------KTRLALEAEVSELRAELSSLqtARQEG 1275
Cdd:COG3899 663 EERRALHRRIARALEARGPEPleerLFELAHHLNRAGERDRAARlllraarraLARGAYAEALRYLERALELL--PPDPE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1276 EQRRRRLELQLQEVQGRAGDGERARaEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1355
Cdd:COG3899 741 EEYRLALLLELAEALYLAGRFEEAE-ALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALAL 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1356 KLALGSRV-----------------RAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEEA 1418
Cdd:COG3899 820 AERLGDRRlearalfnlgfilhwlgPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAA 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1419 RRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLRAVEERER 1498
Cdd:COG3899 900 AAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAA 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1499 AEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRAQVTELED 1578
Cdd:COG3899 980 AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAA 1059
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1579 ELTAAEDAKLRLEVTVQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQM 1658
Cdd:COG3899 1060 AALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLA 1139
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1659 ASAGQGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEM 1738
Cdd:COG3899 1140 AALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEA 1219
|
570 580
....*....|....*....|....*
gi 116284396 1739 ADEVANGNLSKAAILEEKRQLEGRL 1763
Cdd:COG3899 1220 AALLLLLLLAALALAAALLALRLLA 1244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1021-1369 |
1.71e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1021 KLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADME--DRLRKEEKGRQELEKLKRRLDGESSELQ--EQM 1096
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEelEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1097 VEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQllkslreaqAALAEAQEDLESERVARTKAEKQRRDLGEELEAL 1176
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATE---------EELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1177 RGELEDTLDSTNAQQELRSKREQEVT-----------------------------------------ELKKTLEEETRIH 1215
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1216 EAAVQELRQRHGQAlgELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQ--LQEVQGRA 1293
Cdd:COG4717 306 ELQALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1294 GDGERARAEAAEKLQRAQAELENVSGALNEAESKTI---------RLSKELSSTEAQLHDAQELLQEETRAKLALGSRVR 1364
Cdd:COG4717 384 EEELRAALEQAEEYQELKEELEELEEQLEELLGELEellealdeeELEEELEELEEELEELEEELEELREELAELEAELE 463
|
....*
gi 116284396 1365 AMEAE 1369
Cdd:COG4717 464 QLEED 468
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
804-1190 |
1.79e-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: 43.57 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 804 EEERDLKVTDIIVSfQAAARGYLARRAFQKRQQQQSALRVMQRNCAAyLKLrhwqwwrlftkvkpllQVTRQDEVLQARA 883
Cdd:pfam15921 507 EKERAIEATNAEIT-KLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKL----------------QMAEKDKVIEILR 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 884 QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaelcaeaeetrgRLAARKQELELVVSELEARVGEeeecs 963
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQ--------------EFKILKDKKDAKIRELEARVSD----- 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 964 rqMQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEE 1043
Cdd:pfam15921 630 --LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1044 EEKVKSLNKlrlkyeaTIADMEDRLRKEEKGRQELEKLKR-RLDGESSELQeQMVEQQQRAEELRAQLGRKEEELQAALA 1122
Cdd:pfam15921 708 LEQTRNTLK-------SMEGSDGHAMKVAMGMQKQITAKRgQIDALQSKIQ-FLEEAMTNANKEKHFLKEEKNKLSQELS 779
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1123 RAEDEGGARAQLLKSLREAQAALAEAQEDLES--ERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQ 1190
Cdd:pfam15921 780 TVATEKNKMAGELEVLRSQERRLKEKVANMEValDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1026-1266 |
1.86e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.14 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1026 RKLLeDRLAEFSSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEE---KGRQELEKLKRRlDGESSELQEQmVEQQQR 1102
Cdd:COG0497 144 RELL-DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDllrFQLEELEAAALQ-PGEEEELEEE-RRRLSN 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1103 AEELRAQLGrkeeelQAALARAEDEGGArAQLLKSLREAQAALAEAQEDLE--SERVARTKAEKQrrDLGEELEALRGEL 1180
Cdd:COG0497 221 AEKLREALQ------EALEALSGGEGGA-LDLLGQALRALERLAEYDPSLAelAERLESALIELE--EAASELRRYLDSL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1181 E---DTLDSTNA-QQELRS-KR-----EQEVTELKKTLEEE--------TRIH--EAAVQELRQrhgqALGELAEQLEQA 1240
Cdd:COG0497 292 EfdpERLEEVEErLALLRRlARkygvtVEELLAYAEELRAElaelensdERLEelEAELAEAEA----ELLEAAEKLSAA 367
|
250 260
....*....|....*....|....*.
gi 116284396 1241 RRgkgaweKTRLALEAEVSELRAELS 1266
Cdd:COG0497 368 RK------KAAKKLEKAVTAELADLG 387
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
873-1131 |
1.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 873 TRQDEVLQARAQELQ----KVQELQQQSAREVGELQGR----------------VAQLEEERARLAEQLRAEAELCAEAE 932
Cdd:COG4913 609 RAKLAALEAELAELEeelaEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 933 ETRGRLAARKQELELVVSELEARVGEEEECSRQmQTEKKRLQQHIQELEAHLEAEEGARQKLQLEKVTTEAKMKKFEEDL 1012
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKE-LEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1013 LL-LEDQNSKLSKERKLLEDRLaefssqaaeeeekVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgesse 1091
Cdd:COG4913 768 REnLEERIDALRARLNRAEEEL-------------ERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE-------- 826
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 116284396 1092 lqEQMVEQQQRAEELRAQL-GRKEEELQAALARAEDEGGAR 1131
Cdd:COG4913 827 --DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1161-1887 |
2.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1161 KAEKQRRDLGEELEALRGELEDTLdstnaqqelrsKREQEVTELKKTLEEETRIHEAAVQELRQRhgqaLGELAEQLEQA 1240
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFI-----------KRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1241 RRGKGAWEKTRlaleAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAaEKLQRAQAELENVSGA 1320
Cdd:PRK03918 227 EKEVKELEELK----EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1321 LNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKlalgSRVRAMEAEAAGLREQLEEEAAARERagreLQTAQAQLSE 1400
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKE----ERLEELKKKLKELEKRLEELEERHEL----YEEAKAKKEE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1401 WRRRQEEEAGaleageEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELddatmdlEQQRQLVSTLEKKQRKFD- 1479
Cdd:PRK03918 374 LERLKKRLTG------LTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI-------KELKKAIEELKKAKGKCPv 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1480 ---QLLAEEKAAVLRAVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGK-SVHEL 1555
Cdd:PRK03918 441 cgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKyNLEEL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1556 ERACRVAE---QAANDLRAQVTELEDELTAAEDAKLRLEVTVQALKTQherdlqgrdeagEERRRQLAKQLRD---AEVE 1629
Cdd:PRK03918 521 EKKAEEYEklkEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL------------EEELAELLKELEElgfESVE 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1630 RDEERKQRTLAVAAR----KKLEGELEELKAQMASAGQGKEEAVKQLRKMQAQMKELWREVEETrtsreeifsQNRESEK 1705
Cdd:PRK03918 589 ELEERLKELEPFYNEylelKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL---------EKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1706 RLKGLEAEVLRLQEELAASDRARRQAQQDRDEMadevangnlsKAAILEEKRQLEGRlgqleeeleeeqsnsellnDRYR 1785
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEI----------KKTLEKLKEELEER-------------------EKAK 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1786 KlllQVESLTTELSaersfsakaesgrqqlerQIQELRGRLgeedagARARHKMTIAALeSKLAQAEEQLEQETRERILS 1865
Cdd:PRK03918 711 K---ELEKLEKALE------------------RVEELREKV------KKYKALLKERAL-SKVGEIASEIFEELTEGKYS 762
|
730 740
....*....|....*....|..
gi 116284396 1866 GKLVRRAEKRLKEVVLQVEEER 1887
Cdd:PRK03918 763 GVRVKAEENKVKLFVVYQGKER 784
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1594-1953 |
2.39e-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: 42.80 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1594 VQALKTQHERDLQGRDEAGEERRRQLAKQLRDAEVERdeeRKQRTLAVAARkklEGELEELKAQMASAGQGKEEAVKQLR 1673
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVER---RRKLEEAEKAR---QAEMDRQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1674 KMQAQMKElwREVEETRtsREEIFSQnresEKRLKGLEaevlRLQEElaasdrarRQAQQDRDEMADEVANgnlsKAAIL 1753
Cdd:pfam17380 352 RIRQEERK--RELERIR--QEEIAME----ISRMRELE----RLQME--------RQQKNERVRQELEAAR----KVKIL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1754 EEKRQLEGRLGQLEEELEEEQSNsellNDRYRKLLLQVESLTTELSAERsfsakaesgRQQLERQIQELRGRLGEEDaga 1833
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQE----EARQREVRRLEEERAREMERVR---------LEEQERQQQVERLRQQEEE--- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1834 RARHKMTIAALESKLAQAEEQleqetRERILSGKLVRRAEKrlkevvlQVEEERRvadqlRDQLEKgnlrvKQLKRQLEE 1913
Cdd:pfam17380 472 RKRKKLELEKEKRDRKRAEEQ-----RRKILEKELEERKQA-------MIEEERK-----RKLLEK-----EMEERQKAI 529
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 116284396 1914 AEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1953
Cdd:pfam17380 530 YEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1533-1932 |
2.40e-03 |
|
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: 42.90 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1533 ALRAELEALLSSKDD-VGKSVHELERACRVAEQAANDLRAQVTELEDELTAAEDAKL--------RLEVTVQALKTQHER 1603
Cdd:pfam12128 283 ETSAELNQLLRTLDDqWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIetaaadqeQLPSWQSELENLEER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1604 -----DLQGRDEAGEERRRQLAKQLRDAEVERDEER---------KQRTLAVAARKKLEGEL-EELKAQMASAGQGK--- 1665
Cdd:pfam12128 363 lkaltGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKlakireardRQLAVAEDDLQALESELrEQLEAGKLEFNEEEyrl 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1666 EEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRlkglEAEVLRLQEELAASDRARRQAQqdrDEMADEVANG 1745
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAA----NAEVERLQSELRQARKRRDQAS---EALRQASRRL 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1746 NLSKAAILEEKRQLEGRLGQLEEELEEEQSnseLLNDRYRKLLLQVESLTTELSAERSFSAKAESGR------------- 1812
Cdd:pfam12128 516 EERQSALDELELQLFPQAGTLLHFLRKEAP---DWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNlygvkldlkridv 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1813 ---QQLERQIQELRGRLGEEDAGARARHkmtiAALESKLAQAEEQLEQETRERILSGKLVRRAEKRLKEVVLQVE-EERR 1888
Cdd:pfam12128 593 pewAASEEELRERLDKAEEALQSAREKQ----AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQsEKDK 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 116284396 1889 VADQLRDQLEKGNLRVKQLKRQLEEAEEEASRAQAGRRRLQREL 1932
Cdd:pfam12128 669 KNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1052-1169 |
3.08e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1052 KLRLKYEATIADMEDRLRKEEKGRQELEKLKRrldgesselqEQMVEQQQRAEELRAQLGRKEEELQAALARAEDEgGAR 1131
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKK----------EQDEASFERLAELRDELAELEEELEALKARWEAE-KEL 469
|
90 100 110
....*....|....*....|....*....|....*...
gi 116284396 1132 AQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDL 1169
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPL 507
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1198-1373 |
3.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1198 EQEVTELKKTLEEetriHEAAVQELRQRHGqaLGELAEQLEQarrgkgawektrlaLEAEVSELRAELSSLQTARQEGEQ 1277
Cdd:COG3206 181 EEQLPELRKELEE----AEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1278 RRRRLELQLQEVQGRAGD--GERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRA 1355
Cdd:COG3206 241 RLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
170
....*....|....*....
gi 116284396 1356 KL-ALGSRVRAMEAEAAGL 1373
Cdd:COG3206 321 ELeALQAREASLQAQLAQL 339
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1101-1605 |
3.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.54 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1101 QRAEELRAQLGRKEEELQAALARAEDEGGAR---------AQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGE 1171
Cdd:COG3899 729 ERALELLPPDPEEEYRLALLLELAEALYLAGrfeeaeallERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEE 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1172 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTR 1251
Cdd:COG3899 809 AYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAA 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1252 LALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRL 1331
Cdd:COG3899 889 AAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAA 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1332 SKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGA 1411
Cdd:COG3899 969 AAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAA 1048
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1412 LEAGEEARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVLR 1491
Cdd:COG3899 1049 LAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAA 1128
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1492 AVEERERAEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKSVHELERACRVAEQAANDLRA 1571
Cdd:COG3899 1129 ARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAA 1208
|
490 500 510
....*....|....*....|....*....|....
gi 116284396 1572 QVTELEDELTAAEDAKLRLEVTVQALKTQHERDL 1605
Cdd:COG3899 1209 LLALALLALEAAALLLLLLLAALALAAALLALRL 1242
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1027-1349 |
3.78e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.44 E-value: 3.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1027 KLLEDRLAEFSsqaaeeeEKVKSLnklrlkyEATIADMEDRLR-KEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEE 1105
Cdd:pfam00038 7 QELNDRLASYI-------DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1106 LRAQLGRKEEELQAALARAEDEGGARaqllkslREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGEledtld 1185
Cdd:pfam00038 73 LQLELDNLRLAAEDFRQKYEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKN------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1186 stnaqqelrskREQEVTELKKTLEEETRIHE---AAVQELrqrhGQALGELAEQLE-QARRGKG---AWEKTRLA-LEAE 1257
Cdd:pfam00038 140 -----------HEEEVRELQAQVSDTQVNVEmdaARKLDL----TSALAEIRAQYEeIAAKNREeaeEWYQSKLEeLQQA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1258 VSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEklqRAQAELENVSGALNEAESKTIRLSKELss 1337
Cdd:pfam00038 205 AARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQELISELEAELQETRQEM-- 279
|
330
....*....|..
gi 116284396 1338 tEAQLHDAQELL 1349
Cdd:pfam00038 280 -ARQLREYQELL 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1003-1365 |
4.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1003 AKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSS--QAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEK 1080
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREelEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1081 LKRRLDGESSELQEqmvEQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVART 1160
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1161 KAEKQRR-----------DLGEELEALRGELEDTLDS------------TNAQQELRSKREQEVTELKKT--LEEETRIH 1215
Cdd:COG4717 238 AAALEERlkearlllliaAALLALLGLGGSLLSLILTiagvlflvlgllALLFLLLAREKASLGKEAEELqaLPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1216 EAAVQELRQRHG----QALGELAEQLEQARRGKGAW-EKTRLALEAEVSELRAELSSL-------------QTARQEGEQ 1277
Cdd:COG4717 318 EEELEELLAALGlppdLSPEELLELLDRIEELQELLrEAEELEEELQLEELEQEIAALlaeagvedeeelrAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1278 RRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDA------QELLQE 1351
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLeedgelAELLQE 477
|
410
....*....|....
gi 116284396 1352 ETRAKLALGSRVRA 1365
Cdd:COG4717 478 LEELKAELRELAEE 491
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1098-1490 |
4.31e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 41.82 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1098 EQQQRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALR 1177
Cdd:COG5278 104 EQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1178 GELEDTLDSTNAQQELRSKREQEVTELKKTLEEETRIHEAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAE 1257
Cdd:COG5278 184 ALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1258 VSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSS 1337
Cdd:COG5278 264 AAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAA 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1338 TEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQLSEWRRRQEEEAGALEAGEE 1417
Cdd:COG5278 344 LALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALE 423
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1418 ARRRAAREAEALTQRLAEKTETVDRLERGRRRLQQELDDATMDLEQQRQLVSTLEKKQRKFDQLLAEEKAAVL 1490
Cdd:COG5278 424 LAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAA 496
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1041-1373 |
4.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1041 AEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEELQAA 1120
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1121 LARAEDEGGARAQLLKSLREAQAALAEAQEDLESERVARTKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1200
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1201 VTELKKTLEEETRIH-EAAVQELRQRHGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRR 1279
Cdd:COG4372 166 LAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1280 RRLELQLQEVQGRAGDGERARAEAAEKLQRAQAELENVSGALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLAL 1359
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 116284396 1360 GSRVRAMEAEAAGL 1373
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1096-1266 |
5.60e-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: 40.68 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1096 MVEQQQRAEEL------RAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQEDLESE-RVARTKAEKQRRD 1168
Cdd:COG1579 2 MPEDLRALLDLqeldseLDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEiEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1169 LGE-----ELEALRGELEdtldstnAQQELRSKREQEVTELKKTLEEetriHEAAVQELRQRHGQALGELAEQLEQARRG 1243
Cdd:COG1579 82 LGNvrnnkEYEALQKEIE-------SLKRRISDLEDEILELMERIEE----LEEELAELEAELAELEAELEEKKAELDEE 150
|
170 180
....*....|....*....|...
gi 116284396 1244 KGAWEKTRLALEAEVSELRAELS 1266
Cdd:COG1579 151 LAELEAELEELEAEREELAAKIP 173
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
990-1206 |
6.00e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 990 ARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERKLLEDRLAEFSSQAAEEEEKVKSLNKLRLKYE---------AT 1060
Cdd:PHA02562 214 NIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctQQ 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1061 IADMEDRLRK-EEKGRQ---ELEKLKRRLDgessELQEQMVE---QQQRAEELRAQLGRKEEELQAALARAEDeggARAQ 1133
Cdd:PHA02562 294 ISEGPDRITKiKDKLKElqhSLEKLDTAID----ELEEIMDEfneQSKKLLELKNKISTNKQSLITLVDKAKK---VKAA 366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1134 LlkslreaqaalaeaqedleservarTKAEKQRRDLGEELEALRGELEDtLDSTNAQQELRSKREQEVTELKK 1206
Cdd:PHA02562 367 I-------------------------EELQAEFVDNAEELAKLQDELDK-IVKTKSELVKEKYHRGIVTDLLK 413
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1621-1721 |
6.07e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.02 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1621 KQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLR-KMQAQMKELWREVEETRTSREeifsq 1699
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKeKMEEERENLLKEQERALESKL----- 265
|
90 100
....*....|....*....|...
gi 116284396 1700 nRESEKRLK-GLEAEVLRLQEEL 1721
Cdd:cd16269 266 -KEQEALLEeGFKEQAELLQEEI 287
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1800-1895 |
6.12e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1800 AERSFSAKAESGRQQLERQIQELRGR--LGEEDAGARARHKMTIAALESKLAQAEEQLEQ-------ETRERILsgKLVR 1870
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaaeTSQERKQ--KRKE 220
|
90 100
....*....|....*....|....*.
gi 116284396 1871 RAEKRLKEVVLQVEEERRVAD-QLRD 1895
Cdd:PRK11448 221 ITDQAAKRLELSEEETRILIDqQLRK 246
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1613-1758 |
6.18e-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: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1613 EERRRQLAKQLRDAEVERDEERKQRTLAVAARKKLEGELEELKAQMASAGQGKEEAVKQLRKMQA--QMKELWREVEETR 1690
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1691 TSREEIFSQNRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMADEVANgnlsKAAILEEKRQ 1758
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA----ELEELEAERE 166
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1015-1224 |
6.50e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1015 LEDQNSKLSKERKLLEDRLAEF---------SSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRL 1085
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFrqknglvdlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1086 --DGESSELQEQMVEQQQRAEELRAQLGRKEEELQAALARaedeggaRAQLLKSLREAQAALaeaqedLESERVARTKAE 1163
Cdd:COG3206 260 lqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ-------IAALRAQLQQEAQRI------LASLEAELEALQ 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116284396 1164 KQRRDLGEELEALRGELEDTldstnaqqelrSKREQEVTELKKTLEEETRIHEAAVQELRQ 1224
Cdd:COG3206 327 AREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVEVARELYESLLQRLEE 376
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1663-1955 |
7.73e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1663 QGKEEAVKQLRKMQAQMKELWREVEETRTSREEIFSQNRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQDRDEMADEV 1742
Cdd:COG5185 236 KGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENT--KEKIAEYTKSIDIKKATES 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1743 ANGNLSKAAILEE-KRQLEGRLGQLEEELEEEQSNSELLNDRYRKLLLQVESLTTELSAERSfSAKAESGRQQLERQIQE 1821
Cdd:COG5185 314 LEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKS-SEELDSFKDTIESTKES 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1822 LRGRLGEedagARARHKMTIAALESKLAQAEEQLEQETRErilsgklvrraekrLKEVVLQVEEERRVADQLRDQLEKGN 1901
Cdd:COG5185 393 LDEIPQN----QRGYAQEILATLEDTLKAADRQIEELQRQ--------------IEQATSSNEEVSKLLNELISELNKVM 454
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1902 LRVKQL--KRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1955
Cdd:COG5185 455 READEEsqSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1228-1362 |
7.99e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 40.72 E-value: 7.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1228 QALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQLQEVQGRAGDGERARAEAAEKL 1307
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 116284396 1308 QRAQAELEnvsgALNEAESKtirLSKELSSTEAQLhDAQELLQEETRAKLA-LGSR 1362
Cdd:PRK09039 133 ARALAQVE----LLNQQIAA---LRRQLAALEAAL-DASEKRDRESQAKIAdLGRR 180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1161-1397 |
8.11e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1161 KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEtrihEAAVQELRQRHGQALGELAEQLEQA 1240
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1241 RRGKGAWEKTRLALEAE-VSELRAELSSLQTARQEGEQRRRRLELQLQEVqgragdgERARAEAAEKLQRAQAELENVSG 1319
Cdd:COG3883 96 YRSGGSVSYLDVLLGSEsFSDFLDRLSALSKIADADADLLEELKADKAEL-------EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116284396 1320 ALNEAESKTIRLSKELSSTEAQLHDAQELLQEETRAKLALGSRVRAMEAEAAGLREQLEEEAAARERAGRELQTAQAQ 1397
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| DUF3498 |
pfam12004 |
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ... |
1042-1116 |
8.44e-03 |
|
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.
Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 40.90 E-value: 8.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116284396 1042 EEEEKVKSLNKLRL--KYEATIADMEDRLRKEEKgrqELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE 1116
Cdd:pfam12004 373 EESSGPESREELKQaeKYEQEISKLKERLRVSNR---KLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEE 446
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
865-1108 |
8.91e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 41.07 E-value: 8.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 865 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREVGElQGRVAQLEEERA--RLAEQLRAEAELcaeaeetrGRLAARK 942
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEKKLE-QERLRWTEAESKwiSLAEELRTELDA--------SRALAEK 1083
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 943 QELELvvsELEARVGEEEECSRQMQTE--KKRLQQ-------HIQELEAHLEAEEGARQklqLEKVTTEAKMKKFEEDLL 1013
Cdd:PLN03188 1084 QKHEL---DTEKRCAEELKEAMQMAMEghARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAESKFI 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1014 -LLEDQNSKL----SKERKLLEDRLAEFSSQAAEEEEKVKSLNKL--RLK-YEATIADMEDRLRKEE----KGRQELEKL 1081
Cdd:PLN03188 1158 nALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKeAEEALTVAQKRAMDAEqeaaEAYKQIDKL 1237
|
250 260
....*....|....*....|....*..
gi 116284396 1082 KRRLDGESSELQEQMVEQQQRAEELRA 1108
Cdd:PLN03188 1238 KRKHENEISTLNQLVAESRLPKEAIRP 1264
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1015-1351 |
9.19e-03 |
|
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: 41.19 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1015 LEDQNSKLSKERKLLEDRLAEFSSQAAEEEE-------KVKSLNKLRLKYEATIADM---------EDRLRKE-EKGRQE 1077
Cdd:TIGR00606 575 LEDWLHSKSKEINQTRDRLAKLNKELASLEQnknhinnELESKEEQLSSYEDKLFDVcgsqdeesdLERLKEEiEKSSKQ 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1078 LEKLKRRLDGESSELQEQMVEQQ------QRAEELRAQLGRKEEELQAALARAEDEGGARAQLLKSLREAQAALAEAQED 1151
Cdd:TIGR00606 655 RAMLAGATAVYSQFITQLTDENQsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1152 LESE--------RVARTKAEKQRRDLGEELEALRgELEDTLDSTNAQQELRSKREQEVTELKKTLEE----ETRIHEAA- 1218
Cdd:TIGR00606 735 RQSIidlkekeiPELRNKLQKVNRDIQRLKNDIE-EQETLLGTIMPEEESAKVCLTDVTIMERFQMElkdvERKIAQQAa 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1219 ----------VQELRQR---HGQALGELAEQLEQARRGKGAWEKTRLALEAEVSELRAELSSLQTARQEGEQRRRRLELQ 1285
Cdd:TIGR00606 814 klqgsdldrtVQQVNQEkqeKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVEL 893
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 116284396 1286 LQEVQGRAGDGERAR------AEAAEKLQRAQAELENVSGALNE-AESKTIRLSKELSSTEAQLHDAQELLQE 1351
Cdd:TIGR00606 894 STEVQSLIREIKDAKeqdsplETFLEKDQQEKEELISSKETSNKkAQDKVNDIKEKVKNIHGYMKDIENKIQD 966
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1037-1162 |
9.70e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116284396 1037 SSQAAEEEEKVKSLNKLRLKYEATIADMEDRLRKEEKGRQELEKLKRRLDGESSELQEQMVEQQQRAEELRAQLGRKEEE 1116
Cdd:COG2433 377 SIEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE 456
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 116284396 1117 LQAALaRAEDEGGARAQLLKSLREAQAALAEAQEDLEsERVARTKA 1162
Cdd:COG2433 457 ERREI-RKDREISRLDREIERLERELEEERERIEELK-RKLERLKE 500
|
|
| |
