|
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 ... |
115-784 |
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: 1337.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQERELFQETLESLRVLGLL 354
Cdd:cd14930 161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGFS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 355 PEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 434
Cdd:cd14930 241 HEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 435 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 514
Cdd:cd14930 321 ALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 515 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVLH 594
Cdd:cd14930 401 QREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLRDQADFSVLH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 595 YAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 674
Cdd:cd14930 481 YAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 675 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 754
Cdd:cd14930 561 SRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFM 640
|
650 660 670
....*....|....*....|....*....|
gi 564328072 755 DGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14930 641 DGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-784 |
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: 1293.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNIPGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQ-ERELFQETLESLRVLGL 353
Cdd:cd14920 161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQqDKDNFQETMEAMHIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14920 241 SHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd14920 321 FAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 514 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 593
Cdd:cd14920 401 YQREGIEWNFIDFGLDLQPCIDLIERPANPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPRQLKDKADFCII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 594 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 671
Cdd:cd14920 481 HYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDRIVGLDQVTGMTETAfgSAYKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14920 561 ESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 564328072 752 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14920 641 GFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
115-784 |
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: 1277.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKkGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPY-SHYRFLTNGPSSSPGQ-ERELFQETLESLRVL 351
Cdd:cd01377 161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVdDAEEFKLTDEAFDIL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 431
Cdd:cd01377 241 GFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQNKEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 432 ADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 511
Cdd:cd01377 321 VVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMFVLEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 512 EEYQREGIPWTFLDFGLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK-FQRPRNLRDQADF 590
Cdd:cd01377 400 EEYKKEGIEWTFIDFGLDLQPTIDLIEKP--NMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKnFKKPKPKKSEAHF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 591 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPRRGMFRTVGQLY 670
Cdd:cd01377 478 ILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEES---------GGGGGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 671 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 750
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 564328072 751 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
861-1941 |
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: 1276.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 861 TRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 940
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 941 EARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1021 LAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGR 1100
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1101 KEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1181 LRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSR 1260
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1261 QEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEE 1340
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1341 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQR 1420
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1421 LAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALS 1500
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1501 LTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1581 TVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQL 1660
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1661 KKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1740
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1741 LEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAG 1820
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1821 ARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLKRQLE 1900
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 564328072 1901 EAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRL 1941
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
115-784 |
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: 1173.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSIalshGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPG-QERELFQETLESLR 349
Cdd:cd14932 161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGqQDKELFAETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14932 241 IMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14932 321 EQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD 589
Cdd:cd14932 401 EQEEYQREGIEWSFIDFGLDLQPCIELIEKPNGPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPKKLKDDAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 590 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP-GGRPRRGMFRTVGQ 668
Cdd:cd14932 481 FCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDRIVGLDKVAGMGESLHgAFKTRKGMFRTVGQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 669 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14932 561 LYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 640
|
650 660 670
....*....|....*....|....*....|....*.
gi 564328072 749 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14932 641 IPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
115-784 |
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: 1130.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVP--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 265
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPavnpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 266 FDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPG-QERELFQET 344
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 345 LESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQ 424
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 425 KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 505 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPrNL 584
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFR 664
Cdd:cd14911 477 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14911 555 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 634
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 564328072 745 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14911 635 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
115-784 |
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: 1119.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQG---ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQE-RELFQETLESLRVLGL 353
Cdd:cd14919 158 ANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQdKDMFQETMEAMRIMGI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14919 238 PEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQTKEQAD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd14919 318 FAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFILEQEE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 514 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 593
Cdd:cd14919 398 YQREGIEWNFIDFGLDLQPCIDLIEKPAGPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDKADFCII 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 594 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPP--GGRPRRGMFRTVGQLYK 671
Cdd:cd14919 478 HYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDRIIGLDQVAGMSETALpgAFKTRKGMFRTVGQLYK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14919 558 EQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTPNSIPK 637
|
650 660 670
....*....|....*....|....*....|...
gi 564328072 752 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14919 638 GFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
115-784 |
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: 1100.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGKKDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQER-ELFQETLESLRVLGL 353
Cdd:cd14921 161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDdEMFQETLEAMSIMGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14921 241 SEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQAD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd14921 321 FAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 514 YQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVL 593
Cdd:cd14921 401 YQREGIEWNFIDFGLDLQPCIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPKQLKDKTEFSII 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 594 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGP--PGGRPRRGMFRTVGQLYK 671
Cdd:cd14921 481 HYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSlpSASKTKKGMFRTVGQLYK 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14921 561 EQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPK 640
|
650 660 670
....*....|....*....|....*....|...
gi 564328072 752 GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14921 641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
115-784 |
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: 1100.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPG----VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKKDQNslalSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQE-RELFQETLESLR 349
Cdd:cd15896 161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQdKDLFTETMEAFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd15896 241 IMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQTQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd15896 321 EQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFIL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD 589
Cdd:cd15896 401 EQEEYQREGIEWSFIDFGLDLQPCIDLIEKPASPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPKKLKDEAD 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 590 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQL 669
Cdd:cd15896 481 FCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDRIVGLDKVSGMSEMPGAFKTRKGMFRTVGQL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd15896 561 YKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNAI 640
|
650 660 670
....*....|....*....|....*....|....*
gi 564328072 750 PKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd15896 641 PKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
104-784 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1071.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 104 EDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQ 183
Cdd:pfam00063 2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 184 DREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:pfam00063 82 DKENQSILISGESGAGKTENTKKIMQYLASVSGS----GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNSSRFGKYIE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS-PG-QERELF 341
Cdd:pfam00063 158 IQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTiDGiDDSEEF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 342 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRD 421
Cdd:pfam00063 238 KITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 422 YVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:pfam00063 318 TVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVNEKLQQF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 502 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 581
Cdd:pfam00063 398 FNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEKK--PLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPHFQKP 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 582 RnLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVssLGDGPPGGRPRRG 661
Cdd:pfam00063 475 R-LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAAN--ESGKSTPKRTKKK 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 662 MFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:pfam00063 552 RFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRY 631
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 564328072 742 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:pfam00063 632 RILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
96-796 |
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: 994.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 96 NPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTE 175
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 176 GAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpGELERQLLQANPILEAFGNAKTVKNDNS 255
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEV------GSVEDQILESNPILEAFGNAKTLRNNNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 256 SRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS-P 334
Cdd:smart00242 155 SRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTvD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 335 GQE-RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNT-AAQKLCRLLGLGVTDFSRALL 412
Cdd:smart00242 235 GIDdAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEELEKALT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 413 TPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCIN 492
Cdd:smart00242 315 KRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVNSFEQLCIN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 493 YTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQ 572
Cdd:smart00242 394 YANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIE--KKPPGILSLLDEECRFPKGTDQTFLEKLNQHH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 573 GSHPKFQRPRNlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGdg 652
Cdd:smart00242 471 KKHPHFSKPKK-KGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGVS-----NAGSKK-- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 653 ppggrprrgMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:smart00242 543 ---------RFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 733 LFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERD 796
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
94-1171 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 895.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 94 RMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAV 173
Cdd:COG5022 59 RIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 174 TEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSpkgrkEPGVPGELERQLLQANPILEAFGNAKTVKND 253
Cdd:COG5022 139 AEEAYRNLLSEKENQTIIISGESGAGKTENAKRIMQYLASVTSS-----STVEISSIEKQILATNPILEAFGNAKTVRND 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 254 NSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS 333
Cdd:COG5022 214 NSSRFGKYIKIEFDENGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 334 PGQ--ERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRAL 411
Cdd:COG5022 294 IDGidDAKEFKITLDALKTIGIDEEEQDQIFKILAAILHIGNIEFKEDRN-GAAIFSDNSVLDKACYLLGIDPSLFVKWL 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 412 LTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGaSFLGILDIAGFEIFQLNSFEQLCI 491
Cdd:COG5022 373 VKRQIKTGGEWIVVPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCI 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 492 NYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpANPPGLLALLDEECWFPKATDKSFVEKVAQ- 570
Cdd:COG5022 452 NYTNEKLQQFFNQHMFKLEQEEYVKEGIEWSFIDY-FDNQPCIDLIEK-KNPLGILSLLDEECVMPHATDESFTSKLAQr 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 571 -EQGSHPKFQRPRnLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVgleqvssl 649
Cdd:COG5022 530 lNKNSNPKFKKSR-FRDNK-FVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEENIE-------- 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 650 gdgppggrpRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFP 729
Cdd:COG5022 600 ---------SKGRFPTLGSRFKESLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFP 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 730 NRILFQEFRQRYEILTPNA----IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVS 805
Cdd:COG5022 671 SRWTFDEFVQRYRILSPSKswtgEYTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATR 750
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 806 FQAAARGYLARRAFQRRQQQQSALRVMQRNCAAYLKLRNWQWWRLFIKVKPLLQVTRQDEVLQARAQELQKVQ--ELQQQ 883
Cdd:COG5022 751 IQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQktIKREK 830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 884 SAREvgelqgrvaQLEEERARLAEQLRAEAelcSEAEEtrarlaARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQ 963
Cdd:COG5022 831 KLRE---------TEEVEFSLKAEVLIQKF---GRSLK------AKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 964 HIQELethleaeegARQKLQLEKVTTEAKmKKFEEDLLL-LEDQNSKLSKERRLLEERlaEFSSQAAEEEEKVKSLNKLR 1042
Cdd:COG5022 893 SISSL---------KLVNLELESEIIELK-KSLSSDLIEnLEFKTELIARLKKLLNNI--DLEEGPSIEYVKLPELNKLH 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1043 V---KYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQK--QRAEELLIQLGRKEEELQSALVRAEEEGG 1117
Cdd:COG5022 961 EvesKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGalQESTKQLKELPVEVAELQSASKIISSEST 1040
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1118 ARAQlLKSLREAQAGLAEAQEDLEaervARAKAEKQRRDLGEELEALRGELEDT 1171
Cdd:COG5022 1041 ELSI-LKPLQKLKGLLLLENNQLQ----ARYKALKLRRENSLLDDKQLYQLEST 1089
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
115-784 |
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: 841.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSA-SSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS-----PGQE-RELFQETLES 347
Cdd:cd00124 160 GASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLNSSgcdriDGVDdAEEFQELLDA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 348 LRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNT--DQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd00124 240 LDVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDedSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ-GASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd00124 320 PLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFFNQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 505 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNL 584
Cdd:cd00124 400 HVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEGK--PLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleqvsslgdgppggrprrgmfr 664
Cdd:cd00124 477 AKLE-FGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ------------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 665 tvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd00124 519 -----FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 564328072 745 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd00124 594 APGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
115-784 |
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: 776.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 268
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFlatktgGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 269 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETL 345
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVsmNPYD-YHFCSQGVTTVDNmDDGEELMATD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 346 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14927 240 HAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRS-PRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd14927 320 GQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKlPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 505 TMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPR- 582
Cdd:cd14927 398 HMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPL---GILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPRp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 583 --NLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRR 660
Cdd:cd14927 475 dkKRKYEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLY---ENYVGSDSTEDPKSGVKEKRKKA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 661 GMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQR 740
Cdd:cd14927 552 ASFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQR 631
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 564328072 741 YEILTPNAIPK-GFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14927 632 YRILNPSAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
116-784 |
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: 761.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAATgdLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:cd14913 162 SADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLLIttNPYD-YPFISQGEILVASiDDAEELLATDSAIDI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14913 241 LGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQTV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 508
Cdd:cd14913 320 DQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 509 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRDQ 587
Cdd:cd14913 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKVVKGR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 588 AD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRT 665
Cdd:cd14913 475 AEahFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFAT------ADADSGKKKVAKKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14913 549 VSALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 564328072 746 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14913 629 ASAIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
115-784 |
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: 739.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL-EPYSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 352
Cdd:cd14909 161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNvDDGEEFSLTDQAFDILG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 432
Cdd:cd14909 241 FTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGRNVQQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 433 DFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14909 321 TNSIGALCKGVFDRLFKWLVKKCNETLDTQQKR-QHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMFVLEQE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 513 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLR---DQA 588
Cdd:cd14909 400 EYKREGIDWAFIDFGMDLLACIDLIEKPM---GILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPPKpgqQAA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 589 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleQVSSLGDGPPGGRPRRGMFRTVGQ 668
Cdd:cd14909 477 HFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHAG-----QSGGGEQAKGGRGKKGGGFATVSS 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 669 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14909 552 AYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPAG 631
|
650 660 670
....*....|....*....|....*....|....*.
gi 564328072 749 IpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14909 632 I-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
115-784 |
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: 707.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSpkGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGT--GKQSSDGKGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPY-SHYRFLTNGPSSSPGQER-ELFQETLESLRVLG 352
Cdd:cd14934 159 ADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLVPNpKEYHWVSQGVTVVDNMDDgEELQITDVAFDVLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 432
Cdd:cd14934 239 FSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQNMEQC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 433 DFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14934 319 NNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMFVLEQE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 513 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD---QA 588
Cdd:cd14934 398 EYKREGIEWVFIDFGLDLQACIDLLEKPM---GIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGGKGkgpEA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 589 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgppggRPRRGMFRTVGQ 668
Cdd:cd14934 475 HFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK-----------QKRGSSFMTVSN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 669 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14934 544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
|
650 660 670
....*....|....*....|....*....|....*.
gi 564328072 749 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14934 624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
116-784 |
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: 701.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSG-LIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGrkEPGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSG--ETQV----EEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS-PG-QERELFQETLESLRVLG 352
Cdd:cd01380 156 ANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPViDGvDDAAEFEETRKALTLLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQA 432
Cdd:cd01380 236 ISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 433 DFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 511
Cdd:cd01380 316 IVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 512 EEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPK--FQRPRnlRDQAD 589
Cdd:cd01380 396 EEYVKEEIEWSFIDF-YDNQPCIDLIE---GKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPR--FSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 590 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqvsslgdgppggrprrgmfRTVGQL 669
Cdd:cd01380 470 FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKNRK----------------------------------KTVGSQ 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd01380 516 FRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKE 595
|
650 660 670
....*....|....*....|....*....|....*
gi 564328072 750 PKGfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01380 596 WLR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
115-784 |
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: 694.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKKKLGA---LEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPG-QERELFQETLESLRVLGL 353
Cdd:cd14929 158 ADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESlDDAEELLATEQAMDILGF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd14929 238 LPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 434 FALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14929 318 YAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVLEQE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 513 EYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD--QAD 589
Cdd:cd14929 396 EYRKEGIDWVSIDFGLDLQACIDLIEKPM---GIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDKKkfEAH 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 590 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRrgmFRTVGQL 669
Cdd:cd14929 473 FELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLF---ENYISTDSAIQFGEKKRKKGAS---FQTVASL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd14929 547 HKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRTF 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 564328072 750 PKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14929 627 PKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
116-784 |
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: 694.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE--LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:cd14917 162 SADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItnNPYD-YAFISQGETTVASiDDAEELMATDNAFDV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14917 241 LGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTeEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 508
Cdd:cd14917 320 QQVIYATGALAKAVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 509 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLRD- 586
Cdd:cd14917 398 LEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPRNIKGk 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 587 -QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqVSSLGDGPPGGRPRRGMFRT 665
Cdd:cd14917 475 pEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAG------ADAPIEKGKGKAKKGSSFQT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14917 549 VSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILN 628
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 564328072 746 PNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14917 629 PAAIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
116-784 |
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: 676.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVAS-SPKGRKEPG--VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 272
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPnaNKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETLESLR 349
Cdd:cd14916 162 ASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtnNPYD-YAFVSQGEVSVASiDDSEELLATDSAFD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 350 VLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNTA-AQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 428
Cdd:cd14916 241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 429 KEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd14916 320 VQQVYYSIGALAKSVYEKMFNWMVTRINATLEtKQPRQ--YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 508 VLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNL-- 584
Cdd:cd14916 398 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPM---GIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPRNVkg 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRprrgmFR 664
Cdd:cd14916 475 KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSS-----FQ 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14916 550 TVSALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRIL 629
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 564328072 745 TPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14916 630 NPAAIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
117-784 |
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: 673.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 117 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGES 196
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 197 GAGKTENTKKVIQYLAHVA-SSPKGRKEPG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAvTGEKKKEESGkMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14918 163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSiDDQEELMATDSAIDIL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14918 242 GFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQTVQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 431 QADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14918 321 QVYNAVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 510 EQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLRDQA 588
Cdd:cd14918 399 EQEEYKKEGIEWTFIDFGMDLAACIELIEKPL---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSANFQKPKVVKGKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 589 D--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVegiVGLEQVSSlgdGPPGGRPRRGMFRTV 666
Cdd:cd14918 476 EahFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTY---ASAEADSG---AKKGAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14918 550 SALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 564328072 747 NAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14918 630 SAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
116-784 |
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: 667.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEitsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGP-SSSPGQERELFQETLESL 348
Cdd:cd14912 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLIttNPYD-YPFVSQGEiSVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 349 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 427
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLR 585
Cdd:cd14912 398 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyEQHLGKSANFQKPKVVK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 DQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEQVSSLGDGPPGGRPRRGMF 663
Cdd:cd14912 475 GKAEahFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF---SGAQTAEGASAGGGAKKGGKKKGSSF 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 664 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 743
Cdd:cd14912 552 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 631
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 744 LTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14912 632 LNASAIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
116-784 |
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: 663.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGRKEP----GVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEatsgKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETLESL 348
Cdd:cd14910 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLIttNPYD-YAFVSQGEITVPSiDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 349 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 427
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLR 585
Cdd:cd14910 398 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 D--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvEGIVGLEqvSSLGDGPPGGRPRRGMF 663
Cdd:cd14910 475 GkvEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLF---SGAAAAE--AEEGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 664 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 743
Cdd:cd14910 550 QTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 744 LTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14910 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-784 |
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: 660.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGRKE--PG-VPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 272
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEqqPGkMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLkADLLL---EPYShYRFLTNGPSSSPG-QERELFQETLESL 348
Cdd:cd14923 162 ASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPEL-IDLLListNPFD-FPFVSQGEVTVASiDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 349 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 427
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKV-AQEQGSHPKFQRPRNLR 585
Cdd:cd14923 397 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLyDQHLGKSNNFQKPKPAK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 DQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivglEQVSSLGDGPPGGRPRRGMF 663
Cdd:cd14923 474 GKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSNYAG----AEAGDSGGSKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 664 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 743
Cdd:cd14923 550 QTVSAVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRI 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 744 LTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14923 630 LNASAIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
116-784 |
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: 658.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE----LERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGKmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLL--EPYShYRFLTNGPSSSPG-QERELFQETLESL 348
Cdd:cd14915 162 LASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLIttNPYD-FAFVSQGEITVPSiDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 349 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmPDNT-AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 427
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALD-RSPRQgaSFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDtKQPRQ--YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQ-GSHPKFQRPRNLR 585
Cdd:cd14915 398 FVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPM---GIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPAK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 DQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSLGDGPPGGRPRRGMF 663
Cdd:cd14915 475 GKAEahFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSG-----GQTAEAEGGGGKKGGKKKGSSF 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 664 RTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEI 743
Cdd:cd14915 550 QTVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKV 629
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 744 LTPNAIPKG-FMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14915 630 LNASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
116-784 |
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: 636.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVasSPKGrkepgvPGELER---QLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYI 272
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAV--SGGS------ESEVERvkdMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLE-PYSHYRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:cd01378 154 VGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQrPEQYYYYSKSGCFDVDGiDDAADFKEVLNAMKV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVG---RDYVQKAQ 427
Cdd:cd01378 234 IGFTEEEQDSIFRILAAILHLGNIQFAEDEE-GNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGgggRSVYEVPL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFnhTMF 507
Cdd:cd01378 313 NVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIF--IEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 508 VL--EQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFVEKVAQEQGSHPKFQRPRNL 584
Cdd:cd01378 391 TLkaEQEEYVREGIEWTPIKY-FNNKIICDLIE--EKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RD--QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivGLEQVSSlgdgppggrprrGM 662
Cdd:cd01378 468 FElrRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPE-----GVDLDSK------------KR 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 663 FRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 742
Cdd:cd01378 531 PPTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 743 ILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01378 611 LLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
116-784 |
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: 632.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKgrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVTNNHS---------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGE--QLKADLLLEPYSHYRFLT-NGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14883 153 IIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHskELKEKLKLGEPEDYHYLNqSGCIRIDNiNDKKDFDHLRLAMNVL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIVLKK-ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14883 233 GIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 431 QADFALEALAKATYERLFRWLVLRLNRALDRsPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 510
Cdd:cd14883 313 EARDNRDAMAKALYSRTFAWLVNHINSCTNP-GQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHYVFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 511 QEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADF 590
Cdd:cd14883 392 QEEYEKEGINWSHIVFT-DNQECLDLIEKP--PLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRWKTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 591 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLY 670
Cdd:cd14883 469 GVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTYPD-LLALTGLSISLGGDTTSRGTSKGKPTVGDTF 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 671 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIP 750
Cdd:cd14883 548 KHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRARS 627
|
650 660 670
....*....|....*....|....*....|....
gi 564328072 751 KGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14883 628 ADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
116-784 |
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: 623.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRgkKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG---------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPS-SSPG-QERELFQETLESLRVLGL 353
Cdd:cd01383 151 KIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNClTIDGvDDAKKFHELKEALDTVGI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQAD 433
Cdd:cd01383 231 SKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 434 FALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEE 513
Cdd:cd01383 311 DARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 514 YQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRdqadFSVL 593
Cdd:cd01383 391 YELDGIDWTKVDF-EDNQECLDLIEK--KPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA----FTIR 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 594 HYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKES 673
Cdd:cd01383 464 HYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCSCQLPQLFAS------KMLDASRKALPLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 674 LSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIpKGF 753
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDV-SAS 616
|
650 660 670
....*....|....*....|....*....|.
gi 564328072 754 MDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01383 617 QDPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
115-784 |
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: 595.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVAsspkGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAIS----GQHS-----WIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPS-SSPGQ-ERELFQETLESLRVLG 352
Cdd:cd01381 152 AKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNClTCEGRdDAAEFADIRSAMKVLM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKK--ERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd01381 232 FTDEEIWDIFKLLAAILHLGNIKFEAtvVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 431 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS--FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 508
Cdd:cd01381 312 QALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFK 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 509 LEQEEYQREGIPWTFLDFgLDLQPCIDLI-ERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlRDQ 587
Cdd:cd01381 392 LEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMN---IMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS-DLN 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 588 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIvgleqvsslGDGPPGGRPrrgmfrTVG 667
Cdd:cd01381 467 TSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNEDISM---------GSETRKKSP------TLS 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 747
Cdd:cd01381 532 SQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPG 611
|
650 660 670
....*....|....*....|....*....|....*..
gi 564328072 748 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01381 612 IPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
115-784 |
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: 591.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRAVTEGRS-----VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRIS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPG--QERELFQETLESLRVL 351
Cdd:cd01384 156 GAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDgvDDAEEYRATRRAMDVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTpRIKVGRD-YVQKAQ 427
Cdd:cd01384 236 GISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSEFHLkaaAELLMCDEKALEDALCK-RVIVTPDgIITKPL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd01384 315 DPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVF 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 508 VLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQ 587
Cdd:cd01384 394 KMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEK--KPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK--LSR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 588 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSLGDGPPGGRPRRGM-FRTV 666
Cdd:cd01384 469 TDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPF----------------VAGLFPPLPREGTSSSSkFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 564328072 747 NAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 784
Cdd:cd01384 613 EV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
115-784 |
1.41e-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: 562.64 E-value: 1.41e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSGAG--------PIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPyshyrfLTNGPSSspgqerelFQETLESLRVLGL 353
Cdd:cd01382 153 GGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKDP------LLDDVGD--------FIRMDKAMKKIGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 354 LPEEITAMLRTVSAVLQFGNIVLKKERNTDQA-TMPDNTAAQKL---CRLLGLGVTDF-----SRALLTPRIKVGRDYVQ 424
Cdd:cd01382 219 SDEEKLDIFRVVAAVLHLGNIEFEENGSDSGGgCNVKPKSEQSLeyaAELLGLDQDELrvsltTRVMQTTRGGAKGTVIK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 425 KAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSprqgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 502
Cdd:cd01382 299 VPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIpfETS----SYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 503 NHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPR 582
Cdd:cd01382 375 NERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEAKLV--GILDLLDEESKLPKPSDQHFTSAVHQKHKNHFRLSIPR 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 583 --------NLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegIVGLEQVSSLGDGPP 654
Cdd:cd01382 452 ksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKF----------IRSLFESSTNNNKDS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 655 GGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 734
Cdd:cd01382 522 KQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSF 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 564328072 735 QEFRQRYEILTPNAIPKgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01382 602 HDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
115-784 |
1.18e-175 |
|
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: 549.76 E-value: 1.18e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQ----DREDQS 189
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 190 ILCTGESGAGKTENTKKVIQYLAHVAS-----SPKGRKEPGVPGE-----LERQLLQANPILEAFGNAKTVKNDNSSRFG 259
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSgfaqgASGEGEAASEAIEqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 260 KFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQE-R 338
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDdA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 339 ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATmpDNTAAQKL---CRLLGLGVTDFSRALLTPR 415
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTVLE--DATTLQSLklaAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 416 IKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTN 495
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTIS-SPDDKWGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 496 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIE-RPANPPGLLALLDEeCWFPKAT--DKSFV------- 565
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFITLDD-CWRFKGEeaNKKFVsqlhasf 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 566 ------EKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdveg 639
Cdd:cd14890 476 grksgsGGTRRGSSQHPHFVHPKFDADKQ-FGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRR------------ 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 640 ivGLEQVSslgdgppggrprrgmfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLE 719
Cdd:cd14890 543 --SIREVS------------------VGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 720 GIRICRQGFPNRILFQEFRQRYEILTPNAipkgfMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
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 ... |
115-784 |
5.84e-172 |
|
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: 538.98 E-value: 5.84e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG---------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQERELFQETLESLRVLGLL 354
Cdd:cd14872 152 ASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSGCIEVEGVDDVADFEEVVLAMEQLGFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 355 PEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCR---LLGLGVTDFSRALLTPRIKV-GRDYVQKAQTKE 430
Cdd:cd14872 232 DADINNVMSLIAAILKLGNIEFASGGGKSLVSGSTVANRDVLKEvatLLGVDAATLEEALTSRLMEIkGCDPTRIPLTPA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 431 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 510
Cdd:cd14872 312 QATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLE 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 511 QEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADF 590
Cdd:cd14872 392 EALYQSEGVKFEHIDF-IDNQPVLDLIEK--KQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRTSRTEF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 591 SVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGivgleqvsslgdgppggrPRRGMFRTVGQLY 670
Cdd:cd14872 469 IVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG------------------DQKTSKVTLGGQF 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 671 KESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtPNAIP 750
Cdd:cd14872 531 RKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VKTIA 609
|
650 660 670
....*....|....*....|....*....|....*
gi 564328072 751 KGFM-DGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14872 610 KRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
116-784 |
1.86e-167 |
|
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: 526.46 E-value: 1.86e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR--------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLK-ADLLLEPYSHYRFLTNGPSSSPGQE-----RELFQETLESLR 349
Cdd:cd01379 154 RISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIVnnsgnREKFEEIEQCFK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 350 VLGLLPEEITAMLRTVSAVLQFGNIVL----KKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd01379 234 VIGFTKEEVDSVYSILAAILHIGDIEFteveSNHQTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFN 503
Cdd:cd01379 314 NNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 504 HTMFVLEQEEYQREGIPWTFLDFGlDLQPCID-LIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPkFQRPR 582
Cdd:cd01379 394 QHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPM---GLLALLDEESRFPKATDQTLVEKFHNNIKSKY-YWRPK 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 583 nlRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgppggrprrgm 662
Cdd:cd01379 469 --SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ------------------------------ 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 663 frTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 742
Cdd:cd01379 517 --TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYY 594
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 743 ILTPNAIPKGFMDgKQACEKMIQALELDPnlYRVGQSKIFFR 784
Cdd:cd01379 595 FLAFKWNEEVVAN-RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
115-784 |
1.68e-164 |
|
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: 518.48 E-value: 1.68e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKK-RHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDDSD--------LLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQE--------RELFQETL 345
Cdd:cd14897 153 GAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNdseeleyyRQMFHDLT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 346 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14897 233 NIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:cd14897 313 WKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQY 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 502 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRP 581
Cdd:cd14897 393 FNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFFK--KPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVAS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 582 rnLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegivgleqvsslgdgppggrprrg 661
Cdd:cd14897 470 --PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFISDLFT-------------------------- 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 662 mfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:cd14897 522 ------SYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRY 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 564328072 742 EILTPNAiPKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 784
Cdd:cd14897 596 KEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
115-784 |
3.44e-164 |
|
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: 518.54 E-value: 3.44e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPkgrkepgvPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIVG 274
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVNQRR--------NNLVTEQILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-GGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSS-SPGQ-ERELFQETLESLRVLG 352
Cdd:cd01387 152 AITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCeIAGKsDADDFRRLLAAMQVLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAA--QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd01387 232 FSSEEQDSIFRILASVLHLGNVYFHKRQLRHgQEGVSVGSDAeiQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNrALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd01387 312 DQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 510 EQEEYQREGIPWTFLDFGlDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD 589
Cdd:cd01387 391 EQEEYIREQIDWTEIAFA-DNQPVINLISK--KPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPR--MPLPE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 590 FSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGiVGLEQVSSLGDGPPGGRPRRGmfRTVGQL 669
Cdd:cd01387 466 FTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSSHRA-QTDKAPPRLGKGRFVTMKPRT--PTVAAR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 670 YKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAI 749
Cdd:cd01387 543 FQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLVALKL 622
|
650 660 670
....*....|....*....|....*....|....*.
gi 564328072 750 PKGfMDGKQACEKMIQALELDP-NLYRVGQSKIFFR 784
Cdd:cd01387 623 PRP-APGDMCVSLLSRLCTVTPkDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
115-784 |
1.90e-162 |
|
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: 513.94 E-value: 1.90e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAG--------GLNDSTIKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLggAGEQLKADLLLEPYSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14903 153 GAKCRTYLLEKTRVISHERPERNYHIFYQLL--ASPDVEERLFLDSANECAYTgANKTIKIEGmSDRKHFARTKEALSLI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATM--PDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 429
Cdd:cd14903 231 GVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNRALDRSPRQgASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVL 509
Cdd:cd14903 311 DQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFKT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 510 EQEEYQREGIPWTFLDFgLDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKVAqeqGSHPKFQR----PRNLR 585
Cdd:cd14903 390 VQIEYEEEGIRWAHIDF-ADNQDVLAVIE---DRLGIISLLNDEVMRPKGNEESFVSKLS---SIHKDEQDviefPRTSR 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 DQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMfRT 665
Cdd:cd14903 463 TQ--FTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEKVESPAAASTSLARGARRRRGGALTT-TT 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14903 540 VGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 564328072 746 PNAiPKGFMDGKQACEKMIQALELD-PNLYRVGQSKIFFR 784
Cdd:cd14903 620 PEG-RNTDVPVAERCEALMKKLKLEsPEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
115-782 |
2.64e-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: 510.49 E-value: 2.64e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMY------RGKKRHEVPPHIYAVTEGAYRSMLQDRE-- 186
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 187 --DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRI 264
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENVRDRVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 265 NFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLtngpSSSPGQER------ 338
Cdd:cd14901 161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL----NSSQCYDRrdgvdd 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 339 -ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI-VLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRI 416
Cdd:cd14901 237 sVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLcFVKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 417 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS-FLGILDIAGFEIFQLNSFEQLCINYTN 495
Cdd:cd14901 317 RAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFAN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 496 EKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSH 575
Cdd:cd14901 397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYP-NNDACVAMFE--ARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKH 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 576 PKFQRPRNLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdvegivgleqVSSlgdgppg 655
Cdd:cd14901 474 ASFSVSKLQQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAF----------------LSS------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 656 grprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQ 735
Cdd:cd14901 531 ---------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHD 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 564328072 736 EFRQRYEILTPNAIPKGFMDGKQACEKMIQA------LELDPNLYrVGQSKIF 782
Cdd:cd14901 602 AFVHTYSCLAPDGASDTWKVNELAERLMSQLqhselnIEHLPPFQ-VGKTKVF 653
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
115-784 |
6.26e-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: 508.07 E-value: 6.26e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLahVASSPKGRKEpGVpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd01385 81 ESGSGKTESTNFLLHHL--TALSQKGYGS-GV----EQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFL--TNGPSSSPGQERELFQETLESLRVLG 352
Cdd:cd01385 154 AVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnqSDCYTLEGEDEKYEFERLKQAMEMVG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKER-NTDQATMPDNTAAQKL-CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd01385 234 FLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPEVLDIiSELLRVKEETLLEALTTKKTVTVGETLILPYKLP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 431 QADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd01385 314 EAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnLRD 586
Cdd:cd01385 393 FKLEQEEYKKEGISWHNIEY-TDNTGCLQLISK--KPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ-VME 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 587 QAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQVSSL----------------- 649
Cdd:cd01385 469 PA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAF-------VRELIGIDPVAVFrwavlrafframaafre 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 650 -GDGPPGGRPRRGMFR------------------TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLD 710
Cdd:cd01385 541 aGRRRAQRTAGHSLTLhdrttksllhlhkkkkppSVSAQFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLR 620
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 711 QLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd01385 621 QLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
115-784 |
8.19e-158 |
|
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: 500.86 E-value: 8.19e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFL-TNGPSSSPG-QERELFQETLESLRVL 351
Cdd:cd14873 161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLnQSGCVEDKTiSDQESFREVITAMEVM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIvlkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQ 431
Cdd:cd14873 241 QFSKEEVREVSRLLAGILHLGNI---EFITAGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNVQQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 432 ADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQ 511
Cdd:cd14873 318 AVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKHIFSLEQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 512 EEYQREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQadFS 591
Cdd:cd14873 396 LEYSREGLVWEDIDW-IDNGECLDLIEKKL---GLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNN--FG 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 592 VLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWkdvegivglEQVSSLGDGPPGGRPRRGMFRTVGQLYK 671
Cdd:cd14873 470 VKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---------EHVSSRNNQDTLKCGSKHRRPTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 672 ESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPK 751
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
650 660 670
....*....|....*....|....*....|...
gi 564328072 752 GFMDGKqaCEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14873 621 EDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
115-746 |
1.13e-157 |
|
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: 501.14 E-value: 1.13e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRgKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI----- 268
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRS-----LVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKlkskr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 269 ----AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQL----------------------LGGAGEQLKADLLL-EPYS 321
Cdd:cd14888 155 msgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLcaaareakntglsyeendeklaKGADAKPISIDMSSfEPHL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 322 HYRFLT-NGPSSSPG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL--- 396
Cdd:cd14888 235 KFRYLTkSSCHELPDvDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTDDLekv 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 397 CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIA 476
Cdd:cd14888 315 ASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCGVLDIF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 477 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWF 556
Cdd:cd14888 395 GFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLQ--EKPLGIFCMLDEECFV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 557 PKATDKSFVEKVAQEQGSHPKFQRPRNlrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKd 636
Cdd:cd14888 472 PGGKDQGLCNKLCQKHKGHKRFDVVKT--DPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNLFS- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 637 vegivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 716
Cdd:cd14888 549 -----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGG 617
|
650 660 670
....*....|....*....|....*....|
gi 564328072 717 VLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14888 618 VLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
115-784 |
1.65e-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: 1.65e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEV---PPHIYAVTEGAYRSMLQDR----ED 187
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDVPGFDSQRKEEATAsspPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 188 QSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS-PGQEREL-F 341
Cdd:cd14892 161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEvDGVDDATeF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 342 QETLESLRVLGLLPEEITAMLRTVSAVLQFGNivLKKERNTDQATMP----DNTAAQKLCRLLGLGVTDFSRALLTPRIK 417
Cdd:cd14892 241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGN--VRFEENADDEDVFaqsaDGVNVAKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 418 VGRDYV-QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQ---------GASFLGILDIAGFEIFQLNSFE 487
Cdd:cd14892 319 TARGSVlEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 488 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPanPPGLLALLDEECWFP-KATDKSFVE 566
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKK--PLGLLPLLEEQMLLKrKTTDKQLLT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 567 KVAQEQ-GSHPKFQRPRNLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDrltaeiwkdvegivgleq 645
Cdd:cd14892 476 IYHQTHlDKHPHYAKPRFECDE--FVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLRSSSK------------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 646 vsslgdgppggrprrgmFRTvgqlykeSLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICR 725
Cdd:cd14892 536 -----------------FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRR 591
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 726 QGFPNRILFQEFRQRYEILTPN-AIPKGFMDGKQACEKM-----IQALELDPNLYRVGQSKIFFR 784
Cdd:cd14892 592 EGFPIRRQFEEFYEKFWPLARNkAGVAASPDACDATTARkkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
115-784 |
4.30e-149 |
|
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: 477.60 E-value: 4.30e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH--------EVPPHIYAVTEGAYRSMLQDR 185
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 186 EDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE-----------LERQLLQANPILEAFGNAKTVKNDN 254
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSsiratskstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 255 SSRFGKFIRINFDI-AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPYSHYRFLTNGPSS 332
Cdd:cd14907 161 SSRFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLgLKNQLSGDRYDYLKKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 333 SPGQER----ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAA-QKLCRLLGLGVTD 406
Cdd:cd14907 241 CYEVDTindeKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDdSTLDDNSPCCVKNKETlQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 407 FSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL------DRSPRQGASF-LGILDIAGFE 479
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekDQQLFQNKYLsIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 480 IFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTF--LDFgLDLQPCIDLIERPanPPGLLALLDEECWFP 557
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKP--PIGIFNLLDDSCKLA 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 558 KATDKSFVEKVAQEQGSHPKFQRPRNLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDV 637
Cdd:cd14907 478 TGTDEKLLNKIKKQHKNNSKLIFPNKINKDT-FTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 638 EGivgleqvsSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGV 717
Cdd:cd14907 557 DG--------SQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGV 628
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 718 LEGIRICRQGFPNRILFQEFRQRYEILTPNaipkgfmdgkqacekmiqaleldpnlYRVGQSKIFFR 784
Cdd:cd14907 629 LESIRVRKQGYPYRKSYEDFYKQYSLLKKN--------------------------VLFGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
117-784 |
7.34e-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: 7.34e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 117 VLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSML----QDREDQSILC 192
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 193 TGESGAGKTENTKKVIQYLAHVAsspKGRKEpgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYI 272
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC---RGNSQ------LEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRFR-NGHV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 273 VGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPySHYRFLTN--GPSSSPGQERELFQETLESLR 349
Cdd:cd14889 153 KGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGiSAEDRENYGLLDP-GKYRYLNNgaGCKREVQYWKKKYDEVCNAMD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 350 VLGLLPEEITAMLRTVSAVLQFGNIVLK-KERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 428
Cdd:cd14889 232 MVGFTEQEEVDMFTILAGILSLGNITFEmDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 429 KEQADFALEALAKATYERLFRWLVLRLNRALdrSPRQGASF----LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:cd14889 312 KQQAEDARDSIAKVAYGRVFGWIVSKINQLL--APKDDSSVelreIGILDIFGFENFAVNRFEQACINLANEQLQYFFNH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 505 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNl 584
Cdd:cd14889 390 HIFLMEQKEYKKEGIDWKEITY-KDNKPILDLFL--NKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRS- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 rDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFR 664
Cdd:cd14889 466 -KSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPLLSVLFTATRSRTGTLMPRAKLPQAGSDNFNSTRKQ 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14889 545 SVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKIL 624
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 564328072 745 --TPNaIPKgfmdGKQACEKMIQALELDPnlYRVGQSKIFFR 784
Cdd:cd14889 625 lcEPA-LPG----TKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
116-744 |
2.15e-136 |
|
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: 440.51 E-value: 2.15e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMY-----------RGKKRHEVPPHIYAVTEGAYRSM-- 181
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 182 --LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSP-KGRKEPGVPGE-LERQLLQANPILEAFGNAKTVKNDNSSR 257
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNlAASVSMGKSTSgIAAKVLQTNILLESFGNARTLRNDNSSR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 258 FGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKAdlllepyshyrfltngpssspgqe 337
Cdd:cd14900 162 FGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 338 RELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD-QATMPDNTAAQKL------CRLLGLGVTDFSRA 410
Cdd:cd14900 218 RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDATKLEKA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 411 LLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL---DRSPRQGAS-FLGILDIAGFEIFQLNSF 486
Cdd:cd14900 298 LSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNAFLkmdDSSKSHGGLhFIGILDIFGFEVFPKNSF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVE 566
Cdd:cd14900 378 EQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIS--QRPTGILSLIDEECVMPKGSDTTLAS 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 567 KVAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKANEWLMKNMDplndnvaaLLHQstdrltaeiwkdvegivglEQV 646
Cdd:cd14900 455 KLYRACGSHPRFSASRIQRARGLFTIVHYAGHVEYSTDGFLEKNKD--------VLHQ-------------------EAV 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 647 SslgdgppggrprrgMFRTVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQ 726
Cdd:cd14900 508 D--------------LFVYGLQ-FKEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVARA 572
|
650
....*....|....*...
gi 564328072 727 GFPNRILFQEFRQRYEIL 744
Cdd:cd14900 573 GFPIRLLHDEFVARYFSL 590
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
115-784 |
2.02e-135 |
|
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: 438.61 E-value: 2.02e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAHVASspkGRKEPGVPgelerQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAG---GRKDKTIA-----KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSS--PG-QERELFQETLESLRV 350
Cdd:cd14904 153 GAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMqiPGlDDAKLFASTQKSLSL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEEITAMLRTVSAVLQFGNIVLkKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKE 430
Cdd:cd14904 233 IGLDNDAQRTLFKILSGVLHLGEVMF-DKSDENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 431 QADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLE 510
Cdd:cd14904 312 EAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 511 QEEYQREGIPWTFLDFGlDLQPCIDLIErpaNPPGLLALLDEECWFPKATDKSFVEKV---AQEQGSHPKFQRPRNLRDQ 587
Cdd:cd14904 392 EEEYIREGLQWDHIEYQ-DNQGIVEVID---GKMGIIALMNDHLRQPRGTEEALVNKIrtnHQTKKDNESIDFPKVKRTQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 588 adFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgLEQVSSLGDGPPGGRPRrgmfRTVG 667
Cdd:cd14904 468 --FIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSGKGTKAP----KSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPN 747
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 564328072 748 AIPKGfmDGKQACEKMIQAL-ELDPNLYRVGQSKIFFR 784
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIgRKSPLEYQIGKSLIYFK 653
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
115-784 |
6.06e-132 |
|
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: 428.69 E-value: 6.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERyySGLI----YTYSGLFCVVINPYKQLPiytEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDRE---D 187
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 188 QSILCTGESGAGKTENTKKVIQYLAH------------VASSPKGRKEPGVpgELERQLLQANPILEAFGNAKTVKNDNS 255
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTravggkkasgqdIEQSSKKRKLSVT--SLDERLMDTNPILESFGNAKTLRNHNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 256 SRFGKFIRINFDIAGY-IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLT-NGPSSS 333
Cdd:cd14891 154 SRFGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 334 PG-QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKK----ERNTDQATMPDNTAAQKLCRLLGLGVTDFS 408
Cdd:cd14891 234 DNiDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 409 RALLTPRIkVGRDYVQKAQ-TKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRqGASFLGILDIAGFEIFQL-NSF 486
Cdd:cd14891 314 KVITQREI-VTRGETFTIKrNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-PLPYIGVLDIFGFESFETkNDF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIpwtflDFGLDLQP----CIDLIErpANPPGLLALLDEECWFPKATDK 562
Cdd:cd14891 392 EQLLINYANEALQATFNQQVFIAEQELYKSEGI-----DVGVITWPdnreCLDLIA--SKPNGILPLLDNEARNPNPSDA 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 563 SFVEKVAQEQGSHPKFQRP--RNLRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQStdrltaeiwkdvegi 640
Cdd:cd14891 465 KLNETLHKTHKRHPCFPRPhpKDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS--------------- 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 641 vgleqvsslgdgppggrprrgmfrtvgQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEG 720
Cdd:cd14891 528 ---------------------------AKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQT 580
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 721 IRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQA-CEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14891 581 CEVLKVGLPTRVTYAELVDVYKPVLPPSVTRLFAENDRTlTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
115-784 |
2.43e-128 |
|
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: 418.41 E-value: 2.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKepgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIVG 274
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDR--------LRQPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-HGVIVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSS--SPGQERELFQETLESLRVLG 352
Cdd:cd14896 152 ASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACrlQGKEDAQDFEGLLKALQGLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNTDQ--ATMPDNTAAQKLCRLLGLGvTDFSRALLTPRIKV-GRDYVQKAQTK 429
Cdd:cd14896 232 LCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVP-PERLEGAVTHRVTEtPYGRVSRPLPV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 430 EQADFALEALAKATYERLFRWLVLRLNRALdRSPRQGASF--LGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMF 507
Cdd:cd14896 311 EGAIDARDALAKTLYSRLFTWLLKRINAWL-APPGEAESDatIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 508 VLEQEEYQREGIPWTFLDfGLDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrDQ 587
Cdd:cd14896 390 AQEEEECQRELLPWVPIP-QPPRESCLDLLV--DQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL--PL 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 588 ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrprrgmfrTVG 667
Cdd:cd14896 465 PVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAEPQYGLGQGKP----------------TLA 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 668 QLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTpN 747
Cdd:cd14896 529 SRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-S 607
|
650 660 670
....*....|....*....|....*....|....*..
gi 564328072 748 AIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14896 608 ERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
115-746 |
5.18e-128 |
|
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: 420.07 E-value: 5.18e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYR--------GKKRHEVPPHIYAVTEGAYRSMLQ-D 184
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 185 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPG-ELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSDAvEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFL-TNGPSSSPGQER---- 338
Cdd:cd14902 161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnSYGPSFARKRAVadky 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 339 -ELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTP 414
Cdd:cd14902 241 aQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRFHLakcAELMGVDVDKLETLLSSR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 415 RIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--------RSPRQGASFLGILDIAGFEIFQLNSF 486
Cdd:cd14902 321 EIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLNRNGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE 566
Cdd:cd14902 401 EQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDDKSN--GLFSLLDQECLMPKGSNQALST 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 567 KVAQEQGShpkfqrprnlRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkdVEGIVGLEQV 646
Cdd:cd14902 478 KFYRYHGG----------LGQ--FVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEV-------VVAIGADENR 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 647 SSLG-DGPPGGRPRRGMFRT--VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRI 723
Cdd:cd14902 539 DSPGaDNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRI 618
|
650 660
....*....|....*....|...
gi 564328072 724 CRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14902 619 ARHGYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
115-784 |
3.66e-126 |
|
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: 413.54 E-value: 3.66e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR--GKKRHE-------VPPHIYAVTEGAYRSMLQD- 184
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 185 REDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---LERQLLQANPILEAFGNAKTVKNDNSSRFGKF 261
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGNGEEGAPNEGEELGklsIMDRVLQSNPILEAFGNARTLRNDNSSRFGKF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 262 IRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQ----------LKADLLLEPYSHYRFLTNGPS 331
Cdd:cd14908 161 IELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEehekyefhdgITGGLQLPNEFHYTGQGGAPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 332 SSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQK----LCRLLGLGVTDF 407
Cdd:cd14908 241 LREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEE-DGAAEIAEEGNEKclarVAKLLGVDVDKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 408 SRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGA-SFLGILDIAGFEIFQLNSF 486
Cdd:cd14908 320 LRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFAHNSF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 487 EQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFP-KATDKSFV 565
Cdd:cd14908 400 EQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQ--AKKKGILTMLDDECRLGiRGSDANYA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 566 EKV--------AQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKANEWLM-KNMDPLNdnvaallhqstdrLTAEIwkd 636
Cdd:cd14908 477 SRLyetylpekNQTHSENTRFEATSIQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIP-------------LTADS--- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 637 vegivgleqvsslgdgppggrprrgMFRTvGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 716
Cdd:cd14908 541 -------------------------LFES-GQQFKAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 717 VLEGIRICRQGFPNRILFQEFRQRYEILTPnAIPKGFM-------DGKQACEKMI----------QALELDPNL----YR 775
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLP-LIPEVVLswsmerlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQ 673
|
....*....
gi 564328072 776 VGQSKIFFR 784
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
113-795 |
8.55e-125 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 414.43 E-value: 8.55e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 113 NEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHE-VPPHIYAVTEGAYRSMLQDREDQSIL 191
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 192 CTGESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA---SSKSGNMD----LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGG 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 272 IVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPG-QERELFQETLESLRV 350
Cdd:PTZ00014 261 IRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGiDDVKDFEEVMESFDS 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEEITAMLRTVSAVLQFGNI-VLKKERN--TDQAT-MPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:PTZ00014 341 MGLSESQIEDIFSILSGVLLLGNVeIEGKEEGglTDAAAiSDESLEVfNEACELLFLDYESLKKELTVKVTYAGNQKIEG 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNH 504
Cdd:PTZ00014 421 PWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPGGfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVD 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 505 TMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNL 584
Cdd:PTZ00014 499 IVFERESKLYKDEGISTEELEY-TSNESVIDLLCGKGK--SVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVD 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RDQaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE---GIVGLEQVsslgdgppggrprrg 661
Cdd:PTZ00014 576 SNK-NFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEvekGKLAKGQL--------------- 639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 662 mfrtVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:PTZ00014 640 ----IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQF 715
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 742 EILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR---AGVLAQLEEER 795
Cdd:PTZ00014 716 KYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREK 772
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
115-780 |
2.45e-123 |
|
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: 406.67 E-value: 2.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHIYAVTEGAYRSMLQDREDQSILC 192
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 193 TGESGAGKTENTKKVIQYLAHVASS--PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSnqQQNNNNNNNNNSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 271 YIV-GANIETYLLEKSR-AIRQAKDECSFHIFYQLLGGAGEQLKADLLLEP-YSHYRFL-------------TNGPSSSP 334
Cdd:cd14906 161 GKIdGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLdarddvissfksqSSNKNSNH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 335 GQEREL---FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQAT--MPDNTAA-QKLCRLLGLGVTDFS 408
Cdd:cd14906 241 NNKTESiesFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAyqKDKVTASlESVSKLLGYIESVFK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 409 RALLTPRIKV-GRDYVQ-KAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR----------SPRQGASFLGILDIA 476
Cdd:cd14906 321 QALLNRNLKAgGRGSVYcRPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVLDIF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 477 GFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWF 556
Cdd:cd14906 401 GFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSD--GILSLLDDECIM 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 557 PKATDKSFVEKVAQEQGSHPKFQRpRNLrDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLtaeiwkd 636
Cdd:cd14906 478 PKGSEQSLLEKYNKQYHNTNQYYQ-RTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFL------- 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 637 vegIVGLEQVSSLGDGPPGGRPRRGMfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNG 716
Cdd:cd14906 549 ---KKSLFQQQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 717 VLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSK 780
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
115-782 |
4.32e-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: 398.21 E-value: 4.32e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRH-EVPPHIYAVTEGAYRSMLQDREDQSILCT 193
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA---SAKSGNMD----LRIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVASEGGIR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPG-QERELFQETLESLRVLG 352
Cdd:cd14876 154 YGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGiDDVADFEEVLESLKSMG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGN--IVLKKERNTDQATMPDNTAAQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQ 427
Cdd:cd14876 234 LTEEQIDTVFSIVSGVLLLGNvkITGKTEQGVDDAAAISNESLEVFkeaCSLLFLDPEALKRELTVKVTKAGGQEIEGRW 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 428 TKEQADFALEALAKATYERLFRWLVLRLNRALDrsPRQG-ASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14876 314 TKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRD 586
Cdd:cd14876 392 FERESKLYKDEGIPTAELEY-TSNAEVIDVLCGKGK--SVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKVDSN 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 587 QaDFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLgdgppggrprrgmfrtV 666
Cdd:cd14876 469 I-NFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKGKIAKGSL----------------I 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 667 GQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTP 746
Cdd:cd14876 532 GSQFLKQLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDL 611
|
650 660 670
....*....|....*....|....*....|....*.
gi 564328072 747 NAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIF 782
Cdd:cd14876 612 GIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
115-784 |
2.19e-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: 391.67 E-value: 2.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVpgelerqlLQA-NPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIV 273
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVLSVEK--------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPY--SHYRFLTngPSSSPGQEREL---FQETLESL 348
Cdd:cd01386 153 SASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLaeSNSFGIV--PLQKPEDKQKAaaaFSKLQAAM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 349 RVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRAL------------LTPRI 416
Cdd:cd01386 231 KTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIfkhhlsggpqqsTTSSG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 417 KVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLgILDIAGFeifQLN---------SFE 487
Cdd:cd01386 311 QESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSSIT-IVDTPGF---QNPahsgsqrgaTFE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 488 QLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERP---ANPP---------GLLALLDEECW 555
Cdd:cd01386 387 DLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQApqqALVRsdlrdedrrGLLWLLDEEAL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 556 FPKATDKSFVEKV--AQEQGSHPKFQRPRNLRDQA-DFSVLHYAGK--VDYKANEWLMK-NMDPLNDNVAALLHQSTDRL 629
Cdd:cd01386 467 YPGSSDDTFLERLfsHYGDKEGGKGHSLLRRSEGPlQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQESQKET 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 630 TAEIWKDVegivgleqvsslgdgppggrprrgmfrtVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEkrAGKLEPR--- 706
Cdd:cd01386 547 AAVKRKSP----------------------------CLQI-KFQVDALIDTLRRTGLHFVHCLLPQHN--AGKDERStss 595
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 707 -----------LVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGF-----MDGKQACEKMIQALELD 770
Cdd:cd01386 596 paagdelldvpLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELDLE 675
|
730
....*....|....
gi 564328072 771 PNLYRVGQSKIFFR 784
Cdd:cd01386 676 KSSYRIGLSQVFFR 689
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
116-745 |
4.69e-118 |
|
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: 391.24 E-value: 4.69e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPiyteaivEMYRGKKRHE-------VPPHIYAVTEGAYRSMLQ----- 183
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIP-------GLYDLHKYREempgwtaLPPHVFSIAEGAYRSLRRrlhep 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 184 --DREDQSILCTGESGAGKTENTKKVIQYLA----HVASSPKGRKEPGVPGElerQLLQANPILEAFGNAKTVKNDNSSR 257
Cdd:cd14895 75 gaSKKNQTILVSGESGAGKTETTKFIMNYLAesskHTTATSSSKRRRAISGS---ELLSANPILESFGNARTLRNDNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 258 FGKFIRINF-----DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYS--HYRFLTNG- 329
Cdd:cd14895 152 FGKFVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSaqEFQYISGGq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 330 --PSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---------------QATMPDNTA 392
Cdd:cd14895 232 cyQRNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 393 AQKL---CRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDR-----SPR 464
Cdd:cd14895 312 QQHLdivSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalNPN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 465 QGAS-----FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIEr 539
Cdd:cd14895 392 KAANkdttpCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLE- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 540 pANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlRDQAD--FSVLHYAGKVDYKANEWLMKNMDPLNDN 617
Cdd:cd14895 470 -QRPSGIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASR--TDQADvaFQIHHYAGAVRYQAEGFCEKNKDQPNAE 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 618 VAALLHQSTDRLTAEIWKDVEGIVglEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHE 697
Cdd:cd14895 547 LFSVLGKTSDAHLRELFEFFKASE--SAELSLGQPKLRRRSSVLSSVGIGSQFKQQLASLLDVVQQTQTHYIRCIKPNDE 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 564328072 698 KRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14895 625 SASDQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLV 672
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
115-746 |
1.15e-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: 371.49 E-value: 1.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKR-HEVPPHIYAVTEGAYRSMLQDRE--DQSI 190
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 191 LCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAG 270
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLtngPSSSPGQERELFQETLESLRV 350
Cdd:cd14880 161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWL---PNPERNLEEDCFEVTREAMLH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA---AQKLCRLLGLGVTDFSRALLTPRIKVGRDYV--QK 425
Cdd:cd14880 238 LGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQQQvfKK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 505
Cdd:cd14880 318 PCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQQHFVAH 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 506 MFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKS-FVEKVAQEQGSHPKFQRPRnL 584
Cdd:cd14880 398 YLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIE--GSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGHNK-L 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSlgdgppggrPRRGMFR 664
Cdd:cd14880 474 SREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANPEEKTQEEPSG---------QSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14880 545 TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKLL 624
|
..
gi 564328072 745 TP 746
Cdd:cd14880 625 RR 626
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
115-784 |
1.04e-109 |
|
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276851 Cd Length: 650 Bit Score: 365.36 E-value: 1.04e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRH-----EVPPHIYAVTEGAYRSMLQDREDQ 188
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 189 SILCTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDI 268
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHSTSST--------DVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 269 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPS-SSPG-QERELFQETLE 346
Cdd:cd14886 153 DGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCyDAPGiDDQKEFAPVRS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 347 SLRVLgLLPEEITAMLRTVSAVLQFGNIVLKKERN--TDQATMPDNTAA-QKLCRLLGLGVTDFSRALLTPRIKVGRDYV 423
Cdd:cd14886 233 QLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDmgVINAAKISNDEDfGKMCELLGIESSKAAQAIITKVVVINNETI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 424 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL--DRSPRQgasFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:cd14886 312 ISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEIIqfDADARP---WIGILDIYGFEFFERNTYEQLLINYANERLQQY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 502 FNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIERPANppGLLALLDEECWFPKATDKSFVE----KVAQE-----Q 572
Cdd:cd14886 389 FINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNL--SIFSFLEEQCLIQTGSSEKFTSscksKIKNNsfipgK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 573 GShpkfqrprnlrdQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdg 652
Cdd:cd14886 466 GS------------QCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIPNEDGNMK------- 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 653 ppggrprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRI 732
Cdd:cd14886 527 ----------GKFLGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYND 596
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 733 LFQEFRQRYEILT--PNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14886 597 TFEEFFHRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
115-784 |
2.10e-104 |
|
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: 350.65 E-value: 2.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYS-GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRG-KKRHEVPPHIYAVTEGAYRSM-LQDREDQSIL 191
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLAlPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 192 CTGESGAGKTENTKKVIQYL---AHVASSPKGRKEpgVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD- 267
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLgqlSYMHSSNTSQRS--IADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYFDp 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 268 IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADL-LLEPYSHYR-------FLTNGPSSSPGQERE 339
Cdd:cd14875 159 TSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKclnggntFVRRGVDGKTLDDAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 340 LFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNtDQATMPDNTAAQKLCRLLGLGVTDFSRALLtprIKVG 419
Cdd:cd14875 239 EFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQN-DKAQIADETPFLTACRLLQLDPAKLRECFL---VKSK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 420 RDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDrsPR---QGASFLGILDIAGFEIFQLNSFEQLCINYTNE 496
Cdd:cd14875 315 TSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASIT--PQgdcSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 497 KLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLIErpANPPGLLALLDEECWFPKATDKSFVEKVAQE-QGSH 575
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFD--QKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKS 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 576 PKFQRPRN-LRDQadFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQvsslgdgpp 654
Cdd:cd14875 470 PYFVLPKStIPNQ--FGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEKGLARRKQ--------- 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 655 ggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILF 734
Cdd:cd14875 539 ----------TVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPI 608
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 735 QEFRQRYEILTPNAIPKGFMDGK--QACEKMIQALE-----LDPNlYRVGQSKIFFR 784
Cdd:cd14875 609 EQFCRYFYLIMPRSTASLFKQEKysEAAKDFLAYYQrlygwAKPN-YAVGKTKVFLR 664
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
115-741 |
2.15e-99 |
|
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: 337.84 E-value: 2.15e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVP------------PHIYAVTEGAYRSM 181
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGY--AYDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 182 LQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPGE---------LERQLLQANPILEAFGNAKTVKN 252
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTGNNNLTNSESISppaspsrttIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 253 DNSSRFGKFIRINF-DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-----AGEQLKADLLLEPYSHYRFL 326
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncvSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 327 TNGPSSSPG---QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL-----KKERNT--DQATMPDNTAA--- 393
Cdd:cd14899 239 NQSLCSKRRdgvKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFeqiphKGDDTVfaDEARVMSSTTGafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 394 --QKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSP-------- 463
Cdd:cd14899 319 hfTKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQAsapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 464 ------RQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGlDLQPCIDLI 537
Cdd:cd14899 399 sdvddeEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 538 ERpaNPPGLLALLDEECWFPKATDKSFVEKVAQE---QGSHPKFQRPRNLRDQADFSVLHYAGKVDYKANEWLMKNMDPL 614
Cdd:cd14899 478 EH--RPIGIFSLTDQECVFPQGTDRALVAKYYLEfekKNSHPHFRSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 615 NDNVAALLHQSTDRLTAEIW--KDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCI 692
Cdd:cd14899 556 CESAAQLLAGSSNPLIQALAagSNDEDANGDSELDGFGGRTRRRAKSAIAAVSVGTQFKIQLNELLSTVRATTPRYVRCI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 564328072 693 VPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRY 741
Cdd:cd14899 636 KPNDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
116-748 |
1.22e-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: 328.01 E-value: 1.22e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQlpIYTEAIVEMYRGKKRHeVPPHIYAVTEGAYRSMLQdREDQSILCTGE 195
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLV-HGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLA-HVASSPKgrkepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiaGYIVG 274
Cdd:cd14898 78 SGSGKTENAKLVIKYLVeRTASTTS----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--GKITG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADlllepYSHYRFLTnGPSSSPGQERELFQETLESLRVLGLL 354
Cdd:cd14898 146 AKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKND-----FIDTSSTA-GNKESIVQLSEKYKMTCSAMKSLGIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 355 peEITAMLRTVSAVLQFGNIVLKKERNTdqaTMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADF 434
Cdd:cd14898 220 --NFKSIEDCLLGILYLGSIQFVNDGIL---KLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQART 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 435 ALEALAKATYERLFRWLVLRLNRALDRSprqGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEY 514
Cdd:cd14898 295 IRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 515 QREGIPWTFLDFgLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAqeqgshpKFQRpRNLRDQAD--FSV 592
Cdd:cd14898 372 KEEGIEWPDVEF-FDNNQCIRDFEKPC---GLMDLISEESFNAWGNVKNLLVKIK-------KYLN-GFINTKARdkIKV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 593 LHYAGKVDYKANEWLMKNmdplndnvaallhqsTDRLTAEIWKDvEGIVGLEQVSSLgdgppggrprrgmfrtvGQLYKE 672
Cdd:cd14898 440 SHYAGDVEYDLRDFLDKN---------------REKGQLLIFKN-LLINDEGSKEDL-----------------VKYFKD 486
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 673 SLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 748
Cdd:cd14898 487 SMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGITL 562
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
115-784 |
2.17e-96 |
|
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: 329.30 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYS--------GLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDRE 186
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 187 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 266
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG----LEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 267 DIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGgaGEQLKADLLLEPYSHYRFLTNgpssspgqerelFQETLE 346
Cdd:cd14887 157 TGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCN--AAVAAATQKSSAGEGDPESTD------------LRRITA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 347 SLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTA--------AQKLCRLL-------GLGVTDFSRAL 411
Cdd:cd14887 223 AMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTSvsvgceetAADRSHSSevkclssGLKVTEASRKH 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 412 LT--------PRIKVGRDYV------------QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPR------- 464
Cdd:cd14887 303 LKtvarllglPPGVEGEEMLrlalvsrsvretRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKpsesdsd 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 465 ------QGASFLGILDIAGFEIFQ---LNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGI---------PWTF-LD 525
Cdd:cd14887 383 edtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVfqnqdcsafPFSFpLA 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 526 FGLDLQP--CIDLIERP--------ANPPGL---------LALLDEECWFPKATDKSFVEKVAQ--EQGSHPKFQRPRNL 584
Cdd:cd14887 463 STLTSSPssTSPFSPTPsfrsssafATSPSLpsslsslssSLSSSPPVWEGRDNSDLFYEKLNKniINSAKYKNITPALS 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 585 RDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLhQSTDRLTAEIwkdvegivgleqvssLGDGPPGGRPRRGMFR 664
Cdd:cd14887 543 RENLEFTVSHFACDVTYDARDFCRANREATSDELERLF-LACSTYTRLV---------------GSKKNSGVRAISSRRS 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 665 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 744
Cdd:cd14887 607 TLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETK 686
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 564328072 745 TPNAIpKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 784
Cdd:cd14887 687 LPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
112-783 |
8.62e-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: 313.33 E-value: 8.62e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 112 LNEASVLHNLRERYYSGLIYTY---SGLfcVVINPYKQLPIYTEAIVEMYR-------GKKRHEVPPHIYAVTEGAYRSM 181
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 182 LQDREDQSILCTGESGAGKTENTKKVIQYLAHV-ASSPKGRKepgvpgeLERQLLQANPILEAFGNAKTVKNDNSSRFGK 260
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLsSHSKKGTK-------LSSQISAAEFVLDSFGNAKTLTNPNASRFGR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 261 FIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNG-----PSSSPG 335
Cdd:cd14879 152 YTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYgchplPLGPGS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 336 QERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNI--VLKKERNTDqATMPDNTAA-QKLCRLLGLGVTDFsRALL 412
Cdd:cd14879 232 DDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLefTYDHEGGEE-SAVVKNTDVlDIVAAFLGVSPEDL-ETSL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 413 TPRIK-VGRD----YVQKAQTKEQADfaleALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEifQL---- 483
Cdd:cd14879 310 TYKTKlVRKElctvFLDPEGAAAQRD----ELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQ--NRsstg 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 484 -NSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERPanPPGLLALLDEEC-WFPKATD 561
Cdd:cd14879 384 gNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSY-FDNSDCVRLLRGK--PGGLLGILDDQTrRMPKKTD 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 562 KSFVEKVAQEQGSHPKFQRPRNLRDQAD---FSVLHYAGKVDYKANEWLMKNMDPLndnvaallhqSTDRLTaeiwkdve 638
Cdd:cd14879 461 EQMLEALRKRFGNHSSFIAVGNFATRSGsasFTVNHYAGEVTYSVEGFLERNGDVL----------SPDFVN-------- 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 639 givgleqvsslgdgppggrprrgMFRTVGQLyKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVL 718
Cdd:cd14879 523 -----------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLP 578
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 719 EGIRICRQGFPNRILFQEFRQRYEILTPnaipkgFMDGKQACEKMIQALELDPNLYRVGQSKIFF 783
Cdd:cd14879 579 ELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
115-784 |
5.55e-90 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 308.28 E-value: 5.55e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR---GKKRHEVPPHIYAVTEGAYRSMLQDREDQSIL 191
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLsssGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 192 CTGESGAGKTENTKKVIQYLAHVASSPKGrkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF-DIAG 270
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRT--------TFDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQFcERKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 271 YIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNG-PSSSPGQERELFQETL---- 345
Cdd:cd14878 153 HLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTmREDVSTAERSLNREKLavlk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 346 ESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14878 233 QALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMIIR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAS---FLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLF 502
Cdd:cd14878 313 RHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQDEQKSMqtlDIGILDIFGFEEFQKNEFEQLCVNMTNEKMHHYI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 503 NHTMFVLEQEEYQREGIPW----------TFLDFGLDlqpcidlierpaNPPGLLALLDEEC---W-----FPKATdKSF 564
Cdd:cd14878 393 NEVLFLQEQTECVQEGVTMetayspgnqtGVLDFFFQ------------KPSGFLSLLDEESqmiWsvepnLPKKL-QSL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 565 VEKVAQEQGSHPKFQRPRN--LRDQ-ADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKdvegiv 641
Cdd:cd14878 460 LESSNTNAVYSPMKDGNGNvaLKDQgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQ------ 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 642 gleqvSSLGdgppggrprrgmfrTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGI 721
Cdd:cd14878 534 -----SKLV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMV 594
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 722 RICRQGFPNRILFQEFRQRYEILTPNAI-PKGFMDGKQACEKMIQALELDPnlYRVGQSKIFFR 784
Cdd:cd14878 595 KIFRYGYPVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
115-784 |
3.61e-86 |
|
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276897 Cd Length: 637 Bit Score: 296.54 E-value: 3.61e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLpiytEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVI----DVDINEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAhvasspKGRKEPGvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14937 77 ESGSGKTEASKLVIKYYL------SGVKEDN---EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNG----PSSSPGQERELFQETLESLRV 350
Cdd:cd14937 148 SSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKnvviPEIDDAKDFGNLMISFDKMNM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 351 LGLLPEeitaMLRTVSAVLQFGNIV---LKKERNTDQATMPDNT--AAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14937 228 HDMKDD----LFLTLSGLLLLGNVEyqeIEKGGKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKIEI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSpRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 505
Cdd:cd14937 304 PLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNN-KELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYLYI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 506 MFVLEQEEYQREGIPWTFLDFGLDlQPCIDLIERPANppgLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRnlR 585
Cdd:cd14937 383 VYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTS---IISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTK--K 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 D-QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgivgleqVS-SLGdgppggRPRRGMF 663
Cdd:cd14937 457 DiNKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVE-------VSeSLG------RKNLITF 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 664 RtvgqlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRIcRQGFPNRILFQEFRQRYEI 743
Cdd:cd14937 524 K-----YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEY 597
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 564328072 744 LTPNAIPKGFMDGKQACEKMIQAlELDPNLYRVGQSKIFFR 784
Cdd:cd14937 598 LDYSTSKDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
115-736 |
1.57e-78 |
|
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276850 [Multi-domain] Cd Length: 685 Bit Score: 275.63 E-value: 1.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYRGKKRHE-------VPPHIYAVTEGAYRSMLQDRE 186
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 187 DQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRkepgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 266
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMT-------ERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 267 D---------IAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGG-AGEQLKADLLLEPYSHYRFL---------- 326
Cdd:cd14884 154 EeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGlSDEDLARRNLVRNCGVYGLLnpdeshqkrs 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 327 ----------TNGPSSSPGQEREL-FQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKkerntdqatmpdntAAqk 395
Cdd:cd14884 234 vkgtlrlgsdSLDPSEEEKAKDEKnFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK--------------AA-- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 396 lCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRAL-----------DRSPR 464
Cdd:cd14884 298 -AECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVlkckekdesdnEDIYS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 465 QGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFlDFGLDLQPCIDLIERpanpp 544
Cdd:cd14884 377 INEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCS-DVAPSYSDTLIFIAK----- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 545 gLLALLDE-----ECWFPKATDKSFV-----EKVAQEQGSH------PKFQRPRNLRDQAD---FSVLHYAGKVDYKANE 605
Cdd:cd14884 451 -IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVsygfvlNHDADGTAKKQNIKkniFFIRHYAGLVTYRINN 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 606 WLMKNMDPLNDNVAALLHQSTDRLTAEiwkdvegivgleqvsslgdgpPGGRPRRGMFRTVGQLYKESLSRLMATLSNTN 685
Cdd:cd14884 530 WIDKNSDKIETSIETLISCSSNRFLRE---------------------ANNGGNKGNFLSVSKKYIKELDNLFTQLQSTD 588
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 564328072 686 PSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 736
Cdd:cd14884 589 MYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
116-783 |
5.04e-73 |
|
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: 257.73 E-value: 5.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYkqlpiyteaiveMYRGKKRHEVPPHIYA-------VTEGAYRSMLQDREDQ 188
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPY------------RDVGNPLTLTSTRSSPlapqllkVVQEAVRQQSETGYPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 189 SILCTGESGAGKTENTKKVIQYLAHVASSpkgrkepGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDi 268
Cdd:cd14881 70 AIILSGTSGSGKTYASMLLLRQLFDVAGG-------GPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVT- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 269 AGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYS--HYRFLTNGPSSSPGQEREL-FQETL 345
Cdd:cd14881 142 DGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGYSpaNLRYLSHGDTRQNEAEDAArFQAWK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 346 ESLRVLGLlpeEITAMLRTVSAVLQFGNIVLKkERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQK 425
Cdd:cd14881 222 ACLGILGI---PFLDVVRVLAAVLLLGNVQFI-DGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLVKS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 426 AQTKEQADFALEALAKATYERLFRWLVLRLNRALdrspRQGAS--------FLGILDIAGFEIFQLNSFEQLCINYTNEK 497
Cdd:cd14881 298 VCDANMSNMTRDALAKALYCRTVATIVRRANSLK----RLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCAET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 498 LQQLFNHTMFVLEQEEYQREGIPwTFLDFG-LDLQPCIDLIErpANPPGLLALLDEECwFPKATDKSFVEKVAQEQGSHP 576
Cdd:cd14881 374 MQHFYNTHIFKSSIESCRDEGIQ-CEVEVDyVDNVPCIDLIS--SLRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 577 KFQRPRNLRDQAdFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQstdrltaeiwkdvegivgleQVSSLGdgppgg 656
Cdd:cd14881 450 RLFEAKPQDDRM-FGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK--------------------QNCNFG------ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 657 rprrgmFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 736
Cdd:cd14881 503 ------FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKA 576
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 737 FRQRYEILTPNAIPKGFMDGKQACEKMIQ--ALELDPNL-------YRVGQSKIFF 783
Cdd:cd14881 577 FNARYRLLAPFRLLRRVEEKALEDCALILqfLEAQPPSKlssvstsWALGKRHIFL 632
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
116-744 |
9.22e-70 |
|
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: 248.50 E-value: 9.22e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGE 195
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 196 SGAGKTENTKKVIQYLAHVASspkgrkepGVPGELERqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGA 275
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGD--------GNRGATGR-VESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 276 NIETYLLEKSRAIRQAKDECSFHIFYQLLGG--AGEQLKaDLLLEPYSHYRFLTNGPSSSPGQER----------ELFQE 343
Cdd:cd14882 153 IFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFieAQNRLK-EYNLKAGRNYRYLRIPPEVPPSKLKyrrddpegnvERYKE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 344 TLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKerNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYV 423
Cdd:cd14882 232 FEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 424 QKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQL 501
Cdd:cd14882 310 RRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSfpRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 502 FNHTMFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIErpANPPGLLALLDEECwfPKATDKSFV-EKVAQEQGSHPKfqr 580
Cdd:cd14882 390 YNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDQLM--TKPDGLFYIIDDAS--RSCQDQNYImDRIKEKHSQFVK--- 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 581 prnLRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDvegivglEQVSSLgdgppggrprr 660
Cdd:cd14882 462 ---KHSAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTN-------SQVRNM----------- 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 661 gmfRTVGQLYKESLSRLMATLS-NTNPS---FVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQE 736
Cdd:cd14882 521 ---RTLAATFRATSLELLKMLSiGANSGgthFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
....*...
gi 564328072 737 FRQRYEIL 744
Cdd:cd14882 598 FLRRYQFL 605
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
116-784 |
1.36e-66 |
|
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: 239.99 E-value: 1.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLP-IYTEAIVEMYrgKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNY--NQRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVG 274
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL---TTDLSRSK-----YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 275 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQ--ERELFQETLESLRVLG 352
Cdd:cd14905 152 AKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGSISVESidDNRVFDRLKMSFVFFD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 353 LLPEEITAMLRTVSAVLQFGNIVLKKERNtdQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAqtkeqa 432
Cdd:cd14905 232 FPSEKIDLIFKTLSFIIILGNVTFFQKNG--KTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVNEAVENR------ 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 433 dfalEALAKATYERLFRWLVLRLNRALdrSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQE 512
Cdd:cd14905 304 ----DSLARSLYSALFHWIIDFLNSKL--KPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 513 EYQREGIPW-TFLDFGlDLQPCIDLIERPANppgllaLLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlrdqaDFS 591
Cdd:cd14905 378 EYQTERIPWmTPISFK-DNEESVEMMEKIIN------LLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPN-----KFG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 592 VLHYAGKVDYKANEWLMKNMDPLNDNvAALLHQSTdrLTAEIWKDvEGIVGLEQVSSlgdgppggrPRRGMFRTVGQLYK 671
Cdd:cd14905 446 IEHYFGQFYYDVRGFIIKNRDEILQR-TNVLHKNS--ITKYLFSR-DGVFNINATVA---------ELNQMFDAKNTAKK 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 672 ESLS--RLMATLSNTNPS-----------------------------------------------FVRCIVPNHEKRAGK 702
Cdd:cd14905 513 SPLSivKVLLSCGSNNPNnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfhFIRCIKPNSKKTHLT 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 703 LEPRLVLDQLRCNGVLEGIRICRQGFP----NRILFqefrQRYEILTPNAipKGFMD-GKQACEKMIQALELDPNLYRVG 777
Cdd:cd14905 593 FDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFF----DRFSFFFQNQ--RNFQNlFEKLKENDINIDSILPPPIQVG 666
|
....*..
gi 564328072 778 QSKIFFR 784
Cdd:cd14905 667 NTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
115-749 |
1.36e-65 |
|
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: 235.92 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 115 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYrgkkrhevppHIYAVTEGAYRSMLQDRED-QSILCT 193
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 194 GESGAGKTENTKKVIQYLAhvaSSPKGRKEpgvpgelERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDiAGYIV 273
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT---SQPKSKVT-------TKHSSAIESVFKSFGCAKTLKNDEATRFGCSIDLLYK-RNVLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 274 GANIE-TYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNGPSSSPGQER-ELFQETLESLRVL 351
Cdd:cd14874 140 GLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDvNHFKHLEDALHVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 352 GLLPEEITAMLRTVSAVLQFGNIVLKKERNTD---QATMPDNTAAQKLCRLLgLGVtDFSR--ALLTPRIKVGrdyvqKA 426
Cdd:cd14874 220 GFSDDHCISIYKIISTILHIGNIYFRTKRNPNveqDVVEIGNMSEVKWVAFL-LEV-DFDQlvNFLLPKSEDG-----TT 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 427 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGAsfLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 506
Cdd:cd14874 293 IDLNAALDNRDSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHS 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 507 FVLEQEEYQREGIPWTF-LDFGLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNlR 585
Cdd:cd14874 371 FHDQLVDYAKDGISVDYkVPNSIENGKTVELLFK--KPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARN-K 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 586 DQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSslgdgppggrprrgmfrt 665
Cdd:cd14874 448 ERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSSNTSDMIVS------------------ 509
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 666 VGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILT 745
Cdd:cd14874 510 QAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLL 589
|
....
gi 564328072 746 PNAI 749
Cdd:cd14874 590 PGDI 593
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
118-742 |
1.34e-62 |
|
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: 229.86 E-value: 1.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 118 LHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKR----------HEVPPHIYAVTEGAYRSMLQDRED 187
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 188 QSILCTGESGAGKTENTKKVIQYLAHVASS----PKGRKEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 263
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDEteprPDSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMIS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 264 INFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAG------EQLKADLLLEPYSHYRFLTNGPSSSPGQE 337
Cdd:cd14893 164 VEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdptlrDSLEMNKCVNEFVMLKQADPLATNFALDA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 338 RElFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVL------KKERNTDQATMPDNTAAqklCRLLGLGVTDFSRAL 411
Cdd:cd14893 244 RD-YRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpegGKSVGGANSTTVSDAQS---CALKDPAQILLAAKL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 412 LTPRIKVGRDYVQKAQ----------------TKEQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQG----A 467
Cdd:cd14893 320 LEVEPVVLDNYFRTRQffskdgnktvsslkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRYEKSNivinS 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 468 SFLGILDIAGFEIF--QLNSFEQLCINYTNEKLQQLF-NHTMFV----LEQEEYQREG--IPWTFLDFGLDLQPCIDLIE 538
Cdd:cd14893 400 QGVHVLDMVGFENLtpSQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSEQEKCLQLFE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 539 RPanPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQAD------------FSVLHYAGKVDYKANEW 606
Cdd:cd14893 480 DK--PFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTNeylapskdwrllFIVQHHCGKVTYNGKGL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 607 LMKNMDPLNDNVAALLHQSTDrltaeiwkDVEGIVGLEQVSSL-----GDGPPGGRPRRGMFRTVGQLYKESLS------ 675
Cdd:cd14893 558 SSKNMLSISSTCAAIMQSSKN--------AVLHAVGAAQMAAAssekaAKQTEERGSTSSKFRKSASSARESKNitdsaa 629
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 676 --------RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYE 742
Cdd:cd14893 630 tdvynqadALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
137-271 |
1.64e-58 |
|
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: 199.49 E-value: 1.64e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 137 FCVVINPYKQLPIYTEAIV-EMYRGKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVA 215
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIiVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564328072 216 SS--PKGRKEPGVP-----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGY 271
Cdd:cd01363 81 FNgiNKGETEGWVYlteitVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
116-782 |
1.12e-52 |
|
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: 199.29 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 116 SVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYR-GKKRHEVPPHIYAVTEGAYRSMLQDREDQSILCTG 194
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 195 ESGAGKTENTKKVIQYLAHVA----SSPKGRKEPG-----------VPGELERQLLQANPILEAFGNAKTVKNDNSSRFG 259
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVkgsrRLPTNLNDQEednihneentdYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 260 KFIRINFDiAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPYSHYRFLTNgpSSSPGQERE 339
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNN--EKGFEKFSD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 340 LFQETLESLRVLGLL---PEEITAMLRTVSAVLQFGNI----------VLKKER----------------NTDQATMPDN 390
Cdd:cd14938 239 YSGKILELLKSLNYIfddDKEIDFIFSVLSALLLLGNTeivkafrkksLLMGKNqcgqninyetilseleNSEDIGLDEN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 391 TAAQKL-CRLLGLGVTDFSRALLTPRIkVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALD--RSPRQGA 467
Cdd:cd14938 319 VKNLLLaCKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTqlQNININT 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 468 SFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANpPGLL 547
Cdd:cd14938 398 NYINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPTE-GSLF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 548 ALLDEECwFPKATDKS-FVEKVAQEQGSHPKFQRPRN-LRDQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQS 625
Cdd:cd14938 477 SLLENVS-TKTIFDKSnLHSSIIRKFSRNSKYIKKDDiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 626 TDRLTAEIWK----DVEGIVGLEQ-----VSSLGDGPPGGRPRRGMFRTvgqLYKESLSRLMATLSNTNPSFVRCIVPNH 696
Cdd:cd14938 556 ENEYMRQFCMfynyDNSGNIVEEKrrysiQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMKPNE 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 697 EKRA-GKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIltPNAipkgfmDGKQACEKMIQALELDPNLYR 775
Cdd:cd14938 633 SKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDI--KNE------DLKEKVEALIKSYQISNYEWM 704
|
....*..
gi 564328072 776 VGQSKIF 782
Cdd:cd14938 705 IGNNMIF 711
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
888-1462 |
2.36e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.21 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 888 VGELQGRVAQLEE--ERARLAEQLRAEAELCsEAEETRARLAARKQELELVVTELEARVGEEEECS---RQLQSEKKRLQ 962
Cdd:COG1196 195 LGELERQLEPLERqaEKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAELEELEAELEELEaelAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 963 QHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLR 1042
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1043 VKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQL 1122
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1123 LKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEART 1202
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1203 HEVAMQELRQRHSQALVELTEQLEQA------RRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQE 1276
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYEAAleaalaAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1277 vqgrSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEA 1356
Cdd:COG1196 594 ----RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1357 EAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARR 1436
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
570 580
....*....|....*....|....*.
gi 564328072 1437 RLQQELDDATVDLGQQKQLLSTLEKK 1462
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1147-1743 |
6.64e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1147 RAKAEKQ----RRDLgEELEALRGELEDTLDSTnaqqelrsKREQEVTELKKTLEEEARTHEVAMQELRQRHSQA-LVEL 1221
Cdd:COG1196 174 KEEAERKleatEENL-ERLEDILGELERQLEPL--------ERQAEKAERYRELKEELKELEAELLLLKLRELEAeLEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1222 TEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVE 1301
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1302 LESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQT 1381
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1382 TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEK 1461
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1462 KQRKfdqllAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLsskddVGKNVH 1541
Cdd:COG1196 485 ELAE-----AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL-----QNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1542 ELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEE 1621
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1622 RKQRALAMAARKKLELELEELKAQT-SAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEmfTLSRESEKRLKGLEA 1700
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGgSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE--ALLAEEEEERELAEA 712
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 564328072 1701 EVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEE 1743
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1032-1676 |
3.56e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.28 E-value: 3.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1032 EEKVKSLNKLRvkyeatiaDMEDRLKK-----EEKGRQeLEKLKRrldgesselqeqmmeQKQRAEE-LLIQLGRKEEEL 1105
Cdd:COG1196 172 ERKEEAERKLE--------ATEENLERledilGELERQ-LEPLER---------------QAEKAERyRELKEELKELEA 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1106 QSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKR 1185
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1186 EQEVTELKKTLEEEARTHEVAMQELrQRHSQALVELTEQLEQArrgksvwEKTRLSLEAEVSELKTELSSLQTSRQEGEQ 1265
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEEL-EELEEELEELEEELEEA-------EEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1266 KRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKL 1345
Cdd:COG1196 380 ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1346 ALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLsewRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKT 1425
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE---ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1426 EAVERLERARRRLQQELDDATVDlgqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRAL 1505
Cdd:COG1196 537 EAALEAALAAALQNIVVEDDEVA----AAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1506 EEEQEAREELERQNRALRAELEALLSSKDDVGKnVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEvtvqAL 1585
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR-LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELA----ER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1586 KAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQA 1665
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELER 767
|
650
....*....|.
gi 564328072 1666 QMKELWREVEE 1676
Cdd:COG1196 768 ELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
920-1565 |
2.80e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.20 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 920 EETRARLAarkqELELVVTELEARVGEEEEcsrqlQSEKKRLQQHIQELETHLEAEEGARQKLQLEkvtteAKMKKFEED 999
Cdd:COG1196 182 EATEENLE----RLEDILGELERQLEPLER-----QAEKAERYRELKEELKELEAELLLLKLRELE-----AELEELEAE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1000 LLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSE 1079
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1080 LQEQMMEQKQRAEELLIQLGRKEEELQSAlvraeeeggaraqllkslreaqaglAEAQEDLEAERVARAKAEKQRRDLGE 1159
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELEEA-------------------------EAELAEAEEALLEAEAELAEAEEELE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1160 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTR 1239
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1240 LSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRL 1319
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1320 SKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLRE--QMEEEVVARERAGRELQTTQAQLSEWRRRQEEEA 1397
Cdd:COG1196 543 ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAalAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1398 AVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQqelddatvdlGQQKQLLSTLEKKQRKFDQLLAEEKAAV 1477
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG----------GSRRELLAALLEAEAELEELAERLAEEE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1478 LRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDL 1557
Cdd:COG1196 693 LELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
....*...
gi 564328072 1558 RTQVTELE 1565
Cdd:COG1196 773 EREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1423 |
1.14e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 119.27 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 867 LQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAElcsEAEETRARLAARKQELElvvtelearvge 946
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL---ELEEAQAEEYELLAELA------------ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 947 eeecsrQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSS 1026
Cdd:COG1196 299 ------RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1027 QAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQeqmmEQKQRAEELLIQLGRKEEELQ 1106
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE----EALAELEEEEEEEEEALEEAA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1107 SALVRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTN-AQQELRSKR 1185
Cdd:COG1196 449 EEEAELEEE---EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLlAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1186 EQEVTELKKTLEEEARTHE-VAMQELRQRHSQALVELTEQLEQARRGKsvweKTRLSLEAEVSELKTELSSLQTSRQEG- 1263
Cdd:COG1196 526 VAVLIGVEAAYEAALEAALaAALQNIVVEDDEVAAAAIEYLKAAKAGR----ATFLPLDKIRARAALAAALARGAIGAAv 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1264 ----------EQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDT 1333
Cdd:COG1196 602 dlvasdlreaDARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1334 QELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAARE 1413
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
570
....*....|
gi 564328072 1414 AETLAQRLAE 1423
Cdd:COG1196 762 LEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
862-1608 |
1.37e-26 |
|
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: 119.39 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 862 RQDEVLQARAQELQKVQELQQQ-SAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 940
Cdd:TIGR02168 200 RQLKSLERQAEKAERYKELKAElRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 941 EARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1021 LAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELliqlgr 1100
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA------ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1101 KEEELQSALVRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:TIGR02168 434 ELKELQAELEELEEE---LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1181 LRSKREQE------VTELKKTLEEEARTHEVAMQELRQ----RHSQALVELTEQLEQARRGKSVW--------------- 1235
Cdd:TIGR02168 511 LLKNQSGLsgilgvLSELISVDEGYEAAIEAALGGRLQavvvENLNAAKKAIAFLKQNELGRVTFlpldsikgteiqgnd 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1236 ------EKTRLSLEAEVSELKTELSSL----------QTSRQEGEQKRRRLESQLQ------EVQGRSSDSERARAEAAE 1293
Cdd:TIGR02168 591 reilknIEGFLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRivtldgDLVRPGGVITGGSAKTNS 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1294 KLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARE 1373
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1374 RAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQK 1453
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1454 QLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTraleeeqEAREELERQNRALRAELEALLSSK 1533
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL-------NERASLEEALALLRSELEELSEEL 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1534 DDVGKNVHELERARRVAEQAASDLRTQVTELEDEL-----TAAEDAKLRLEVtVQALKAQHERDLQGRDDAGEERRRQLA 1608
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIdnlqeRLSEEYSLTLEE-AEALENKIEDDEEEARRRLKRLENKIK 982
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
234-725 |
5.91e-25 |
|
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: 113.68 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 234 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDIAGY---IVGANIETYLLEKSRAIRQA------KDECSFHIFYQ 302
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 303 LLGGAG-----EQLKADLLLEPY--SHYRFLTNGPSSSPG---------QERELFQETLESLRVLGLLPEEITAMLRTVS 366
Cdd:cd14894 329 MVAGVNafpfmRLLAKELHLDGIdcSALTYLGRSDHKLAGfvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 367 AVLQFGNIVLKKERNTDQATMPDN---TAAQKLCRLLGLG-VTDFSRALLTPRIKV--GRDYVQKAQTKEQADFALEALA 440
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELGsVEKLERMLMTKSVSLqsTSETFEVTLEKGQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 441 KATYERLFRWLVLRLNRAL----------------DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQqlfnh 504
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEATkmsalstdgnkhqmdsNASAPEAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLY----- 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 505 tmfvleQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKAT----------DKSFVEKVAQEQGS 574
Cdd:cd14894 564 ------AREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRNIYDRNSS 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 575 HPKfQRPRNLRDQA----------DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GIVG 642
Cdd:cd14894 638 RLP-EPPRVLSNAKrhtpvllnvlPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESSqlGWSP 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 643 LEQVSSLGDGPPGGRPRRGMfrtVGQlYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIR 722
Cdd:cd14894 717 NTNRSMLGSAESRLSGTKSF---VGQ-FRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQME 792
|
...
gi 564328072 723 ICR 725
Cdd:cd14894 793 ICR 795
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1285-1876 |
1.52e-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: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1285 ERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQ 1364
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1365 MEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDD 1444
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1445 ATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRA 1524
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1525 ELEALLSSKDDVGKnvhELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERR 1604
Cdd:COG1196 464 LLAELLEEAALLEA---ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAAL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1605 RQLAKQLRDAEVERDEER--------KQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEE 1676
Cdd:COG1196 541 EAALAAALQNIVVEDDEVaaaaieylKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGD 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1677 TRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEE 1756
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1757 ELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSfsakAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKL 1836
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAERE----ELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 564328072 1837 AQ-------AEEQL-EQESRERILSGKL--VRRAEKRLKEVVLQVDEERR 1876
Cdd:COG1196 777 EAlgpvnllAIEEYeELEERYDFLSEQRedLEEARETLEEAIEEIDRETR 826
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1144-1943 |
1.60e-24 |
|
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: 112.46 E-value: 1.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1144 RVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQ-------QELRSKREQ--------EVTELKKTLEEeARTHEVAMQ 1208
Cdd:TIGR02168 175 KETERKLERTRENL-DRLEDILNELERQLKSLERQaekaeryKELKAELRElelallvlRLEELREELEE-LQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1209 ELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR 1288
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1289 AEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEE 1368
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1369 VVARERAGRELQTTQAQLSEwrrrqeeeaAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVD 1448
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEE---------AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1449 LGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRA---------VEDRERVEAE-GREREA----RALSLTRALEEEQEAREE 1514
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgilgvLSELISVDEGyEAAIEAalggRLQAVVVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1515 LERQNRALRAELEALLSSKDDVGKNVHELERAR-RVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDL 1593
Cdd:TIGR02168 564 FLKQNELGRVTFLPLDSIKGTEIQGNDREILKNiEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1594 QGR----DD---------AGEERRRQLAKQLRDAEVERDEERKQR-----ALAMAARKKLELELEELKAQTSAAGQGKEE 1655
Cdd:TIGR02168 644 GYRivtlDGdlvrpggviTGGSAKTNSSILERRREIEELEEKIEEleekiAELEKALAELRKELEELEEELEQLRKELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1656 AVKQLKKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNl 1735
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1736 skaatlEEKRQLEGRLgqleeeleeeqnnsELLKDHYRKLVLQVETLTTELSAersfsakAESGRQQLERQIQELRARLg 1815
Cdd:TIGR02168 803 ------EALDELRAEL--------------TLLNEEAANLRERLESLERRIAA-------TERRLEDLEEQIEELSEDI- 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1816 EEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQL 1895
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 564328072 1896 KRQLEEAeeeasrAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:TIGR02168 935 EVRIDNL------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
862-1399 |
5.78e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 111.00 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 862 RQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaelcsEAEETRARLAARKQELELVVTELE 941
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK-------KAEEKKKADEAKKAEEKKKADEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 942 ARVGEE---EECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1018
Cdd:PTZ00121 1309 KKAEEAkkaDEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1019 E-RLAEFSSQAAEEEEkvKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQmMEQKQRAEELL-- 1095
Cdd:PTZ00121 1389 EkKKADEAKKKAEEDK--KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK-AEEAKKAEEAKkk 1465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1096 IQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDST 1175
Cdd:PTZ00121 1466 AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1176 NAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQrhsqalVELTEQLEQARrgksvWEKTRLSLEAEVSELKTELSS 1255
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK------AEEAKKAEEAR-----IEEVMKLYEEEKKMKAEEAKK 1614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1256 LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARaeAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQE 1335
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK--KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564328072 1336 LLQEETRAKLALgSRVRALEAE----AAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAV 1399
Cdd:PTZ00121 1693 ALKKEAEEAKKA-EELKKKEAEekkkAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
870-1525 |
2.03e-23 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 109.46 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 870 RAQELQKVQELQQ-QSAREVGELQGRVAQLEEERARLAEQLRaEAELCSEAEETRARLAARKQElELVVTELEARVGEEE 948
Cdd:PTZ00121 1171 KAEDAKKAEAARKaEEVRKAEELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAE-EAKKDAEEAKKAEEE 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 949 ECSRQLQSEKKRLQQHIQELETHLEAEEgARQKLQLEKvtteAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQA 1028
Cdd:PTZ00121 1249 RNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKK----AEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKK 1323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1029 AEEEEKvkSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRldGESSELQEQmmEQKQRAEELliqlGRKEEELQSA 1108
Cdd:PTZ00121 1324 AEEAKK--KADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK--AEAAEKKKE--EAKKKADAA----KKKAEEKKKA 1393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1109 --LVRAEEEGGARAQLLKSLREAQAGLAEAQEdlEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKRE 1186
Cdd:PTZ00121 1394 deAKKKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1187 QEvtELKKTLEEEARTHEVamqelrQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSElktELSSLQTSRQEGEQK 1266
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEA------KKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD---EAKKAEEAKKADEAK 1540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1267 R---RRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRA 1343
Cdd:PTZ00121 1541 KaeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI 1620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1344 KLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAE 1423
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE 1700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1424 --KTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRKFDQLLAEEkaavlravEDRERVEAEGREREARALS 1500
Cdd:PTZ00121 1701 akKAEELKKKEAEEKKKAEELKKAeEENKIKAEEAKKEAEEDKKKAEEAKKDE--------EEKKKIAHLKKEEEKKAEE 1772
|
650 660
....*....|....*....|....*
gi 564328072 1501 LTRALEEEQEAREELERQNRALRAE 1525
Cdd:PTZ00121 1773 IRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
948-1732 |
6.88e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.06 E-value: 6.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 948 EECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQ 1027
Cdd:TIGR02168 196 NELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1028 AAEEEEKVKSLNKLRVKYEATIADMEDRLkkeekgrQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQS 1107
Cdd:TIGR02168 276 VSELEEEIEELQKELYALANEISRLEQQK-------QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1108 ALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQ 1187
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL-------EDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1188 EVTELKKTLEEEArthevamqelRQRHSQALVELTEQLEQarrgksvwektrlsLEAEVSELKTELSSLQTSRQEGEQKR 1267
Cdd:TIGR02168 422 EIEELLKKLEEAE----------LKELQAELEELEEELEE--------------LQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1268 RRLESQLQEVQGRssdseraraeaAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELlqeETRAKLAL 1347
Cdd:TIGR02168 478 DAAERELAQLQAR-----------LDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGY---EAAIEAAL 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1348 GSRVRALEAEaaGLREQMEE-EVVARERAGRelqTTQAQLSEWRrrqeeeAAVLEAGEEARRRAAREAETLAQRL---AE 1423
Cdd:TIGR02168 544 GGRLQAVVVE--NLNAAKKAiAFLKQNELGR---VTFLPLDSIK------GTEIQGNDREILKNIEGFLGVAKDLvkfDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1424 KTEAVERLERARRRLQQELDDATVDLGQ--QKQLLSTLE-----------KKQRKFDQLLAEEKAAVLRAVEDRERVEAE 1490
Cdd:TIGR02168 613 KLRKALSYLLGGVLVVDDLDNALELAKKlrPGYRIVTLDgdlvrpggvitGGSAKTNSSILERRREIEELEEKIEELEEK 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1491 GREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTA 1570
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1571 AEDAKLRLEVTVQALKAQHERDLQG-----------RDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELEL 1639
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEElkalrealdelRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1640 EELKAQTS--AAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARR 1717
Cdd:TIGR02168 853 DIESLAAEieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE 932
|
810
....*....|....*
gi 564328072 1718 QAQQDRDEMAEEVAS 1732
Cdd:TIGR02168 933 GLEVRIDNLQERLSE 947
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1496 |
7.24e-23 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.06 E-value: 7.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVT 938
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 939 ELEARVgeeeecsRQLQSEKKRLQQHIQELETHLEAEEGARQKLQ-----LEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1013
Cdd:TIGR02168 383 TLRSKV-------AQLELQIASLNNEIERLEARLERLEDRRERLQqeieeLLKKLEEAELKELQAELEELEEELEELQEE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 RRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIA---DMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQR 1090
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDsleRLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGY 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1091 AEELLIQLGrkeEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQE----DLEAERVARAKAEKQRRDLGEELEALRG 1166
Cdd:TIGR02168 536 EAAIEAALG---GRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSikgtEIQGNDREILKNIEGFLGVAKDLVKFDP 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1167 ELE-------------DTLDSTNAQQEL----------------------------------RSKREQEVTELKKTLEEE 1199
Cdd:TIGR02168 613 KLRkalsyllggvlvvDDLDNALELAKKlrpgyrivtldgdlvrpggvitggsaktnssileRRREIEELEEKIEELEEK 692
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1200 ARTHEVAMQELRQRHSqalvELTEQLEQARRGKsvwektrLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQG 1279
Cdd:TIGR02168 693 IAELEKALAELRKELE----ELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1280 RSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAA 1359
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1360 GLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQ 1439
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR 921
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1440 QELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVED-----RERVEAEGREREA 1496
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDdeeeaRRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
859-1388 |
4.06e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 104.84 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQA----RAQELQKVQELQQQS--AREVGELQGRVaqleEERARLAEQLRAEAELCSEAEET-RARLAARKQ 931
Cdd:PTZ00121 1282 ELKKAEEKKKAdeakKAEEKKKADEAKKKAeeAKKADEAKKKA----EEAKKKADAAKKKAEEAKKAAEAaKAEAEAAAD 1357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 932 ELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLS 1011
Cdd:PTZ00121 1358 EAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEAKKKAEEKKKADE 1435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1012 KERRLLEERLAEFSSQAAEEEEKVKSLNKlrvKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRA 1091
Cdd:PTZ00121 1436 AKKKAEEAKKADEAKKKAEEAKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1092 EELliqlgRKEEELQSALVRAEEEGGARAQLLKSLREAQAG--LAEAQEDLEAERVARA----KAEKQRRDLGEELEALR 1165
Cdd:PTZ00121 1513 DEA-----KKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAdeLKKAEELKKAEEKKKAeeakKAEEDKNMALRKAEEAK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1166 GELEDTLDSTNAQQELRSKREQEvtELKKTLEEEARTHEV-AMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEA 1244
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAE--EAKKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1245 EVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEA-----AEKLQRAQVELESVSTALSEAESKAIRL 1319
Cdd:PTZ00121 1666 EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAeekkkAEELKKAEEENKIKAEEAKKEAEEDKKK 1745
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1320 SKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEaaGLREQMEEEVVARERAGRELQTTQAQLSE 1388
Cdd:PTZ00121 1746 AEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE--ELDEEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
877-1395 |
4.00e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 100.91 E-value: 4.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 877 VQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVGEEEECSRQLQS 956
Cdd:PRK03918 191 IEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELE----SLEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 957 EKKRLQQHIQELETHlEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSsqaaEEEEKVK 1036
Cdd:PRK03918 267 RIEELKKEIEELEEK-VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE----EKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1037 SLNKLRVKYEATIADMEDRLKKEEKGRQ---ELEKLKRRLDGESSELQEQMMEQKQRAEElliQLGRKEEELQSALVRAE 1113
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKRLTGLTPEKLEKELEELEKAKE---EIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1114 EEGGARAQLLKSLREAQAGL----AEAQEDLEAERVARAKAE-----KQRRDLGEELEALRGELEDTLDSTNAQQELRsk 1184
Cdd:PRK03918 419 KEIKELKKAIEELKKAKGKCpvcgRELTEEHRKELLEEYTAElkrieKELKEIEEKERKLRKELRELEKVLKKESELI-- 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1185 REQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRG-------KSVWEKTRLSLEAEVSELKTELSSLQ 1257
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSlkkelekLEELKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1258 TS-RQEGEQKRRRLESQLQEVqgRSSDSERARAEAAEK-LQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQE 1335
Cdd:PRK03918 577 KElEELGFESVEELEERLKEL--EPFYNEYLELKDAEKeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1336 LLQEETRAKLAlgSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEE 1395
Cdd:PRK03918 655 KYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
948-1743 |
2.04e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.45 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 948 EECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE----RRLLEERLAE 1023
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKaedaRKAEEARKAE 1173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1024 FSSQA-----AEEEEKVKSLNKlrvkyeatiadMEDRLKKEEKGRQELEklkRRLDGESSELQEQMMEQKQRAEElliqL 1098
Cdd:PTZ00121 1174 DAKKAeaarkAEEVRKAEELRK-----------AEDARKAEAARKAEEE---RKAEEARKAEDAKKAEAVKKAEE----A 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1099 GRKEEELQsalvRAEEEggaraqllkSLREAQAGLAEAQEDLEAERVARAKAEKQRRdlgeelealRGELEDTLDSTNAQ 1178
Cdd:PTZ00121 1236 KKDAEEAK----KAEEE---------RNNEEIRKFEEARMAHFARRQAAIKAEEARK---------ADELKKAEEKKKAD 1293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1179 QELRSKREQEVTELKKTLEEEARTHEVAMQ-ELRQRHSQALVELTEQLEQARRGKSVWEKTRLSlEAEVSELKTELSSLQ 1257
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKaEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD-EAEAAEEKAEAAEKK 1372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1258 TSrqEGEQKRRRLESQLQEVqgRSSDSERARAE----AAEKLQRAQVELESVSTALSEAESKaiRLSKELSSAESQLHDT 1333
Cdd:PTZ00121 1373 KE--EAKKKADAAKKKAEEK--KKADEAKKKAEedkkKADELKKAAAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1334 QELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEaavleageearrraarE 1413
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAK----------------K 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1414 AETLAQRLAEKTEAVERLERARRRLQQELDDAtvdlgqqkqllstleKKQRKFDQLlaeEKAAVLRAVEDRERVEAEGRE 1493
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKA---------------EEKKKADEL---KKAEELKKAEEKKKAEEAKKA 1572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1494 REARALSLTRALEeeqeareelerqnralraeleallsskddvgknVHELERARrvAEQAASDLRTQVTELEDELTAAED 1573
Cdd:PTZ00121 1573 EEDKNMALRKAEE---------------------------------AKKAEEAR--IEEVMKLYEEEKKMKAEEAKKAEE 1617
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1574 AKLRLEvtvQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVE---RDEERKQRALAMAARKKLELELEELKAQTSAAG 1650
Cdd:PTZ00121 1618 AKIKAE---ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1651 QGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSRESEKRlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1730
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
810
....*....|...
gi 564328072 1731 ASGNLSKAATLEE 1743
Cdd:PTZ00121 1771 EEIRKEKEAVIEE 1783
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
855-1736 |
2.29e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.45 E-value: 2.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 855 KPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaEAELCSEAEETRARLAARKQE-- 932
Cdd:PTZ00121 1073 KPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDAR-KAEEARKAEDARKAEEARKAEda 1151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 933 --LELVVTELEARVGEEEECSRQL-QSEKKRLQQHIQELETHLEAEEGAR--QKLQLEKVTTEAKMKKFEEDlllledqn 1007
Cdd:PTZ00121 1152 krVEIARKAEDARKAEEARKAEDAkKAEAARKAEEVRKAEELRKAEDARKaeAARKAEEERKAEEARKAEDA-------- 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1008 SKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQE----LEKLKRRLDGESSELQEQ 1083
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkkAEEKKKADEAKKAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1084 MMEQKQRAEElliqlGRKEEELQSalvRAEEeggaraqllkSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEA 1163
Cdd:PTZ00121 1304 ADEAKKKAEE-----AKKADEAKK---KAEE----------AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1164 LRGELEDTLDSTNAQQELRSKREQ--EVTELKKTLEEE-ARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRL 1240
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAEEDkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1241 SLEAEvsELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQ---RAQVELESVSTALSEAESKai 1317
Cdd:PTZ00121 1446 ADEAK--KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKAdeaKKAAEAKKKADEAKKAEEA-- 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1318 RLSKELSSAESQLHDTQELLQEETRAKLALGsrvRALEAEAAGLREQMEEEVVARERagRELQTTQAQLSewrrRQEEEA 1397
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELK---KAEELKKAEEKKKAEEAKKAEED--KNMALRKAEEA----KKAEEA 1592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1398 AVLEAGEEARRRAAREAETLAQRLAEKTEAverlerarrrlqQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAV 1477
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKIKA------------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1478 LRAVEDRERVEAEGREREAralslTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDL 1557
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1558 RtqvTELEDELTAAEDAKLRLEvtvQALKAQHERdlQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA--LAMAARKKL 1635
Cdd:PTZ00121 1736 K---KEAEEDKKKAEEAKKDEE---EKKKIAHLK--KEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVdkKIKDIFDNF 1807
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1636 ELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRA 1715
Cdd:PTZ00121 1808 ANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEA 1887
|
890 900
....*....|....*....|.
gi 564328072 1716 RRQAQQDRDEMAEEVASGNLS 1736
Cdd:PTZ00121 1888 DEIEKIDKDDIEREIPNNNMA 1908
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
858-1485 |
8.07e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 97.06 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 858 LQVTRQDEVLQAraqELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVV 937
Cdd:TIGR02169 290 LRVKEKIGELEA---EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 938 TELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLL 1017
Cdd:TIGR02169 367 EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1018 EERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAE---EL 1094
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhGT 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1095 LIQLGRKEEELQSALvraEEEGGARAQLLKSLREAQAglAEAQEDLEAERVARA------KAEKQRRDLGEELEAlrGEL 1168
Cdd:TIGR02169 527 VAQLGSVGERYATAI---EVAAGNRLNNVVVEDDAVA--KEAIELLKRRKAGRAtflplnKMRDERRDLSILSED--GVI 599
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1169 EDTLD-----------------STNAQQELRSKREQEVTELKKTLEEEARTHEVAM---QELRQRHSQALVELTEQLEQA 1228
Cdd:TIGR02169 600 GFAVDlvefdpkyepafkyvfgDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMtggSRAPRGGILFSRSEPAELQRL 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1229 RRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTA 1308
Cdd:TIGR02169 680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSE 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1309 LSEAESKAIRLSKELSSAESQL-----HDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQ 1383
Cdd:TIGR02169 760 LKELEARIEELEEDLHKLEEALndleaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1384 AQLSEWRRRQEEEAAVLEAGEEARRRaareaetLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQ 1463
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQI 912
|
650 660
....*....|....*....|..
gi 564328072 1464 RKFDQLLAEEKAAvLRAVEDRE 1485
Cdd:TIGR02169 913 EKKRKRLSELKAK-LEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
866-1249 |
2.66e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.51 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 866 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaELCSEAEETRARLAARKQELElvvtELEARVG 945
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QLRKELEELSRQISALRKDLA----RLEAEVE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 946 EEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1025
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1026 SQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKeekgrqeleklkrrLDGESSELQEQMMEQKQRAEELLIQLGRKEEEL 1105
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDIES--------------LAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1106 QSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEEL-EALRGELEDTLDSTNAQQELRSK 1184
Cdd:TIGR02168 890 ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEEYSLTLEEAEALENKIEDDEEE 969
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1185 REQEVTELKKTLEEEARTHEVAMQELRQRhSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSEL 1249
Cdd:TIGR02168 970 ARRRLKRLENKIKELGPVNLAAIEEYEEL-KERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
887-1396 |
7.89e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.57 E-value: 7.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 887 EVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELElvvtELEARVgeeEECSRQLQSEKKRLQQHIQ 966
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE----DLRETI---AETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 967 ELETHLEAEEGARQKLQLEKVTTEAkmkkfeedlllLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYE 1046
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDADAEA-----------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1047 ATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSL 1126
Cdd:PRK02224 356 ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1127 REAQAGLAEAQEDLEA----------ERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQ--------------QELR 1182
Cdd:PRK02224 436 RTARERVEEAEALLEAgkcpecgqpvEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERleraedlveaedriERLE 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1183 SKREqEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRL---SLEAEVSELKTELSSLQT- 1258
Cdd:PRK02224 516 ERRE-DLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREevaELNSKLAELKERIESLERi 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1259 ---------SRQEGEQKRRRLEsQLQEVQGRSSD-----SERAR-----------AEAAEKLQRAQVELESVSTALSEAE 1313
Cdd:PRK02224 595 rtllaaiadAEDEIERLREKRE-ALAELNDERRErlaekRERKReleaefdeariEEAREDKERAEEYLEQVEEKLDELR 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1314 SKAIRLSKELSSAESQLHDTQELLQEETraklALGSRVRALEAeaagLREQMEeevvareragrELQTTQAQL-SEWRRR 1392
Cdd:PRK02224 674 EERDDLQAEIGAVENELEELEELRERRE----ALENRVEALEA----LYDEAE-----------ELESMYGDLrAELRQR 734
|
....
gi 564328072 1393 QEEE 1396
Cdd:PRK02224 735 NVET 738
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1183-1957 |
2.41e-17 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 89.43 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1183 SKREQEVTELKKTLEEEARTHEVAMQElrqrhsQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQE 1262
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAE------EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKA 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1263 GEQKRRRLESQLQEVQgrssdseraRAEAAEKLQRAQvELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETR 1342
Cdd:PTZ00121 1149 EDAKRVEIARKAEDAR---------KAEEARKAEDAK-KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEAR 1218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1343 aklalgsrvRALEAEAAGLREQMEEEVVARERAGRELQTTQAQlsEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLA 1422
Cdd:PTZ00121 1219 ---------KAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE--EIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1423 EKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLL--AEEK---AAVLRAVEDRERVEAEGREREAR 1497
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKkkAEEAkkaAEAAKAEAEAAADEAEAAEEKAE 1367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1498 ALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDlrtqvtelEDELTAAEDAKLR 1577
Cdd:PTZ00121 1368 AAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK--------AEEKKKADEAKKK 1439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1578 LEVTVQA----LKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRAlamaarkkleLELEELKAQTSAAGQGK 1653
Cdd:PTZ00121 1440 AEEAKKAdeakKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA----------EEAKKKADEAKKAAEAK 1509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1654 EEAVKQLKKMQAQMKELWREVEETRSSREemftLSRESEKRlkglEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASG 1733
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADE----AKKAEEKK----KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1734 NLSKAATLEEKRQLEGrlgQLEEELEEEQNNSELLKDHYRKLvlQVETLTTElSAERSFSAKAESGRQQLERQIQELRAR 1813
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEV---MKLYEEEKKMKAEEAKKAEEAKI--KAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1814 lgEEDAGARARQKMLIAALESKlaQAEEQLEQESRERILSGKLVRRAE--KRLKEVVLQVDEERRVADQLRDQLEKSNLR 1891
Cdd:PTZ00121 1656 --EEENKIKAAEEAKKAEEDKK--KAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEEENKIK 1731
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1892 LKQLKR----------QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVF 1957
Cdd:PTZ00121 1732 AEEAKKeaeedkkkaeEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNF 1807
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
941-1876 |
3.88e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.49 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 941 EARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKvtTEAKMKKFEEDLLLLEDQNSKLSKERRLLEER 1020
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA--KKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1021 LAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQmmeqkqraeelLIQLGR 1100
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE-----------LLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1101 KEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE 1180
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1181 LRSKREQEVTELKKTLEEEArthevamQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSR 1260
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEA-------QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1261 QEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAqvelesvSTALSEAESKAIRLSKELSSAESQLHDTQELLQEe 1340
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER-------SQKESKARSGLKVLLALIKDGVGGRIISAHGRLG- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1341 tRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQR 1420
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1421 LAEKTEAVERLERARRRLQQELDDATVDLGqqKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALS 1500
Cdd:pfam02463 612 TLEADEDDKRAKVVEGILKDTELTKLKESA--KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1501 LTRALEEEQEAREELErqnraLRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam02463 690 AKEEILRRQLEIKKKE-----QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1581 TVQALKAQHERDlqgrddagEERRRQLAKQLRDAEVERDEERKQRALAMAarkkleleleelkaqtsaagqgKEEAVKQL 1660
Cdd:pfam02463 765 EKSELSLKEKEL--------AEEREKTEKLKVEEEKEEKLKAQEEELRAL----------------------EEELKEEA 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1661 KKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAAT 1740
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEK 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1741 LEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAErsfsAKAESGRQQLERQIQELRARLGEEdag 1820
Cdd:pfam02463 895 EKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLE----EADEKEKEENNKEEEEERNKRLLL--- 967
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1821 ararQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERR 1876
Cdd:pfam02463 968 ----AKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1208 |
4.96e-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: 87.82 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 862 RQDEVLQARAQELQKVQELQqqsaREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELE 941
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDAS----RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 942 ARVGEEEECSRQLqsEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1021
Cdd:TIGR02169 772 EDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1022 AEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRK 1101
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1102 EEELqsalvraeeeggarAQLLKSLREaqaGLAEAQEDLEAERVarakaEKQRRDLGEELEALRG-------ELEDTLDS 1174
Cdd:TIGR02169 930 EEEL--------------SEIEDPKGE---DEEIPEEELSLEDV-----QAELQRVEEEIRALEPvnmlaiqEYEEVLKR 987
|
330 340 350
....*....|....*....|....*....|....*
gi 564328072 1175 TNAQQELRSKREQEVTELKKTLEE-EARTHEVAMQ 1208
Cdd:TIGR02169 988 LDELKEKRAKLEEERKAILERIEEyEKKKREVFME 1022
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
857-1380 |
7.45e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.04 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELV 936
Cdd:PRK03918 216 LPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 937 VtELEARVGEEEECSRQLQSEKKRLQQHIQELE---THLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1013
Cdd:PRK03918 296 I-KLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 RRlLEERLAEFSSQAAEE-----EEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRL--------DGESSEL 1080
Cdd:PRK03918 375 ER-LKKRLTGLTPEKLEKeleelEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgreltEEHRKEL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1081 QEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKsLREAQAGLAEAQEDLEAERVARAKAE-KQRRDLGE 1159
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIK-LKELAEQLKELEEKLKKYNLEELEKKaEEYEKLKE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1160 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHevamQELRQRHSQALVELTEQLEQARRGKSVWEKTR 1239
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELL----KELEELGFESVEELEERLKELEPFYNEYLELK 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1240 lSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEaaEKLQRAQVELESVSTALSEAESKAIRL 1319
Cdd:PRK03918 609 -DAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEEL 685
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1320 SKELSSAESQLHDTQELLQEETRAKLALGSRVRALEaEAAGLREQMEE-EVVARERAGRELQ 1380
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKyKALLKERALSKVG 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
942-1722 |
1.08e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 87.05 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 942 ARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKvtteAKMKKFEEDLLLLED-QNSKLSKERRLLEER 1020
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRER----EKAERYQALLKEKREyEGYELLKEKEALERQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1021 LAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKgrqeleKLKRRLDGESSELQEQMMEQKQRAEelliQLGR 1100
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNK------KIKDLGEEEQLRVKEKIGELEAEIA----SLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1101 KEEELQSALVRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDtLDSTNAqqE 1180
Cdd:TIGR02169 309 SIAEKERELEDAEER---LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE-VDKEFA--E 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1181 LRSKREQEVTELKKTLEE--EARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQT 1258
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREinELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1259 SRQEGEQKRRRLESQLQEVQGRSSDSERaraEAAEKLQRAQvelesvstALSEAESKAIRLSKELSSAESQLHDT-QELL 1337
Cdd:TIGR02169 463 DLSKYEQELYDLKEEYDRVEKELSKLQR---ELAEAEAQAR--------ASEERVRGGRAVEEVLKASIQGVHGTvAQLG 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1338 QEETRAKLALGSrvraleaeAAGLREQ---MEEEVVA--------RERAGR-------ELQTTQAQLS------------ 1387
Cdd:TIGR02169 532 SVGERYATAIEV--------AAGNRLNnvvVEDDAVAkeaiellkRRKAGRatflplnKMRDERRDLSilsedgvigfav 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1388 --------------------------EWRRRQE-------------EEAAVLEAGEEARRRAAREAETLAQRLAEKTEAV 1428
Cdd:TIGR02169 604 dlvefdpkyepafkyvfgdtlvvediEAARRLMgkyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERL 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1429 ERLERARRRLQQELDDATVDLGQQKQLLSTLEKK----QRKFDQLLAEEKAAVLRAVEDRERVEAEGREREaralsltra 1504
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQELSDASRKigeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE--------- 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1505 leeeqeareelerqnrALRAELEALLSSKDDVGKNVHELERArrVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQA 1584
Cdd:TIGR02169 755 ----------------NVKSELKELEARIEELEEDLHKLEEA--LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1585 LKAQHERDLQGRDDAgEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQ 1664
Cdd:TIGR02169 817 IEQKLNRLTLEKEYL-EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 564328072 1665 AQMKELWREVEETRSSREEMftlsresEKRLKGLEAEVLRLQEELAASDRARRQAQQD 1722
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKK-------RKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
859-1174 |
5.69e-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: 84.34 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVT 938
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 939 ELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE 1018
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1019 ERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQL 1098
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1099 GRKEEELQSALVRAEEEGGAR-AQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDS 1174
Cdd:TIGR02168 939 DNLQERLSEEYSLTLEEAEALeNKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEA 1015
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1071-1850 |
8.55e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 84.04 E-value: 8.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1071 RRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARakA 1150
Cdd:PTZ00121 1070 EGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEA-----------RKAEEAKKKAEDARKAEEARK--A 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1151 EKQRRdlgeELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEV-AMQELRQrhsqalVELTEQLEQAR 1229
Cdd:PTZ00121 1137 EDARK----AEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVrKAEELRK------AEDARKAEAAR 1206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1230 RgksvWEKTRLSLEAEVSElktelsslqtSRQEGEQKRRRLESQLQEVQGRSSDSERaRAEAAEKLQRAQVELESVSTAL 1309
Cdd:PTZ00121 1207 K----AEEERKAEEARKAE----------DAKKAEAVKKAEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAA 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1310 SEAESKaiRLSKELSSAEsQLHDTQELLQEETRAKlALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEW 1389
Cdd:PTZ00121 1272 IKAEEA--RKADELKKAE-EKKKADEAKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEA 1347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1390 RRRQEEEAAvleageearrraareaeTLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQL 1469
Cdd:PTZ00121 1348 AKAEAEAAA-----------------DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1470 LAEEKA------AVLRAVEDRERVEAEGREREAR-ALSLTRALEEEQEAREELERQNRALRAEleaLLSSKDDVGKNVHE 1542
Cdd:PTZ00121 1411 KKAAAAkkkadeAKKKAEEKKKADEAKKKAEEAKkADEAKKKAEEAKKAEEAKKKAEEAKKAD---EAKKKAEEAKKADE 1487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1543 LERARRVAEQAASDLRTQVTELE--DELTAAEDAKLRLEvtvqALKAQHERDLQGRDDAGEERRrqlAKQLRDAEVERDE 1620
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKkaDEAKKAEEAKKADE----AKKAEEAKKADEAKKAEEKKK---ADELKKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1621 ERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMK-ELWREVEETRSSREEMFTLSRESEK--RLKG 1697
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKveQLKK 1640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1698 LEAEVLRLQEEL--AASDRARRQAQQDRDEMAEEVASGNLSKAAtlEEKRQLEGRLgqleEELEEEQNNSELLKDHYRKL 1775
Cdd:PTZ00121 1641 KEAEEKKKAEELkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAE--EDEKKAAEAL----KKEAEEAKKAEELKKKEAEE 1714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564328072 1776 VLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALE---SKLAQAEEQLEQESRER 1850
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEirkEKEAVIEEELDEEDEKR 1792
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1518-1930 |
1.24e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1518 QNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERdLQGRD 1597
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR-LEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1598 DAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEET 1677
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1678 RSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEE 1757
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1758 LEEEQNNSELLKDHYRKLVLQVETLT----TELSAERSFSAKAESGRQQLERQIQELRARLGEEDAG------------A 1821
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAarllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaayeaaleaaL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1822 RARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLKRQLEE 1901
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
410 420
....*....|....*....|....*....
gi 564328072 1902 AEEEASRAQAGRRRLQRELEDVTESAESM 1930
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEG 653
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1087-1626 |
1.71e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.78 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1087 QKQRAEELLIQLGRKEEELQSAlvraeeeGGARAQLLKSLREAQaglaEAQEDLEAErvaraKAEKQRRDLGEELEALRG 1166
Cdd:PRK02224 150 DRQDMIDDLLQLGKLEEYRERA-------SDARLGVERVLSDQR----GSLDQLKAQ-----IEEKEEKDLHERLNGLES 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1167 ELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEvamqelrqrhsqALVELTEQLEQARRGKSVWEKTRLSLEAEV 1246
Cdd:PRK02224 214 ELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE------------ELETLEAEIEDLRETIAETEREREELAEEV 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1247 SELKTELSSLQTSRQE-------GEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRL 1319
Cdd:PRK02224 282 RDLRERLEELEEERDDllaeaglDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEEL 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1320 SKELSSAESQLHDTQELLQEETRAKLALGSRVRALEA----------EAAGLREQMEEEvvaRERAGRELQTTQAQLSEW 1389
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREE---RDELREREAELEATLRTA 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1390 RRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQL------LSTLEKKQ 1463
Cdd:PRK02224 439 RERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLveaedrIERLEERR 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1464 RKFDQLLAEEKAAVLRAVEDRERVEAEGREREARAlsltraleeeqeareelerqnRALRAELEALLSSKDDVGKNVHEL 1543
Cdd:PRK02224 519 EDLEELIAERRETIEEKRERAEELRERAAELEAEA---------------------EEKREAAAEAEEEAEEAREEVAEL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1544 ERARrvaeQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGE--ERRRQLAKQLRDAEVERDEE 1621
Cdd:PRK02224 578 NSKL----AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEkrERKRELEAEFDEARIEEARE 653
|
....*
gi 564328072 1622 RKQRA 1626
Cdd:PRK02224 654 DKERA 658
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
873-1708 |
4.26e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 81.65 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 873 ELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQlRAEAE----LCSEAEETRAR-LAARKQELELVVTELEARVGEE 947
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-REKAEryqaLLKEKREYEGYeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 948 EECSRQLQSEKKRLQQHIQELETHLEA----------EEGARQKLQLEKVttEAKMKKFEEDLLLLEDQNSKLSKERRLL 1017
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEElnkkikdlgeEEQLRVKEKIGEL--EAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1018 EERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQ 1097
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1098 LGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTldstna 1177
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV------ 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1178 qQELRSKREQEVTELKKTLE--EEARTHEVAMQELRQRHSQALVELTEQLeqarrgKSVWEKTRLSLE-AEVSELKTELS 1254
Cdd:TIGR02169 482 -EKELSKLQRELAEAEAQARasEERVRGGRAVEEVLKASIQGVHGTVAQL------GSVGERYATAIEvAAGNRLNNVVV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1255 SLQTSRQEGEQ--KRRRLESQ----LQEVQGRSSDSERARAEAA----------EKLQRAQVELESVSTALSE--AESKA 1316
Cdd:TIGR02169 555 EDDAVAKEAIEllKRRKAGRAtflpLNKMRDERRDLSILSEDGVigfavdlvefDPKYEPAFKYVFGDTLVVEdiEAARR 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1317 IRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEE 1396
Cdd:TIGR02169 635 LMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1397 AAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAA 1476
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1477 VLRAveDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASD 1556
Cdd:TIGR02169 795 EIQA--ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1557 LRTQVTELEDELTAAEDAKLRLEVTVQALkaqherdlqgrddagEERRRQLAKQLRDAEvERDEERKQRALAMAARKKLE 1636
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLREL---------------ERKIEELEAQIEKKR-KRLSELKAKLEALEEELSEI 936
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1637 LELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELwrevEETRSSREEMFtlsRESEKRLKGLEAEVLRLQEE 1708
Cdd:TIGR02169 937 EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL----EPVNMLAIQEY---EEVLKRLDELKEKRAKLEEE 1001
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
863-1492 |
2.79e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 863 QDEVLQARAQE--LQKVQELQQQSAREVGELqgRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTEL 940
Cdd:COG4913 241 HEALEDAREQIelLEPIRELAERYAAARERL--AELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 941 EARVGEEEECSRQLQS----EKKRLQQHIQELETHLEAEEGARQKLQLekvtteakmkkfeedllLLEDQNSKLSKERRL 1016
Cdd:COG4913 319 DALREELDELEAQIRGnggdRLEQLEREIERLERELEERERRRARLEA-----------------LLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1017 LEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQ-KQRAEEL- 1094
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlGLDEAELp 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1095 ----LIQLGRKEEELQSALVRAEeeGGARAQLLkslreaqaglaeaqedLEAERVARAKAEKQRRDLGEEL--EALRGEL 1168
Cdd:COG4913 462 fvgeLIEVRPEEERWRGAIERVL--GGFALTLL----------------VPPEHYAAALRWVNRLHLRGRLvyERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1169 EDTLDSTNAQQELRSKREQEVTELKKTLEeearthevamQELRQRHSQALVELTEQLEQARRG----------KSVWEK- 1237
Cdd:COG4913 524 PDPERPRLDPDSLAGKLDFKPHPFRAWLE----------AELGRRFDYVCVDSPEELRRHPRAitragqvkgnGTRHEKd 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1238 ----------------TRL-SLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRS--SDSERARAEAAEKLQRA 1298
Cdd:COG4913 594 drrrirsryvlgfdnrAKLaALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeySWDEIDVASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1299 QVELESVSTAlseaeskairlSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRE 1378
Cdd:COG4913 674 EAELERLDAS-----------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1379 LQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEK-TEAVERLERARRRLQQELDDATVDLGQQKQLLS 1457
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLD 822
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 564328072 1458 TLE-----KKQRKFDQLLAE----EKAAVLRAVEdRERVEAEGR 1492
Cdd:COG4913 823 RLEedglpEYEERFKELLNEnsieFVADLLSKLR-RAIREIKER 865
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1062-1872 |
2.86e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 79.01 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1062 GRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKslREAQAglaeaQEDLE 1141
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRR--RESQS-----QEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1142 aervarakaeKQRRDLGEELEALRGELEDTLDSTNAQQElrskreqevtELKKTLeeeaRTHEVAMQELRQrhsqALVEL 1221
Cdd:pfam15921 145 ----------NQLQNTVHELEAAKCLKEDMLEDSNTQIE----------QLRKMM----LSHEGVLQEIRS----ILVDF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1222 TEQleqarRGKSVWEKTRLSlEAEVSELKTELSSLQtsrqegeqkrRRLESQLQEVQGR----SSDSERARAEAAEK--- 1294
Cdd:pfam15921 197 EEA-----SGKKIYEHDSMS-TMHFRSLGSAISKIL----------RELDTEISYLKGRifpvEDQLEALKSESQNKiel 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1295 -LQRAQVELESVstaLSEAESKAIRLSKELSSAESQLHDTQ---ELLQEETRAKLALGSR-VRALEAEAAGLR------- 1362
Cdd:pfam15921 261 lLQQHQDRIEQL---ISEHEVEITGLTEKASSARSQANSIQsqlEIIQEQARNQNSMYMRqLSDLESTVSQLRselreak 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1363 -------EQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAverLERAR 1435
Cdd:pfam15921 338 rmyedkiEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTG---NSITI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1436 RRLQQELDDATVDLGQQKQLLSTLEKK-QRKFDQllaeEKAAVLRAVEDRERVEAegrerearalsltraleeeqearee 1514
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAMKSEcQGQMER----QMAAIQGKNESLEKVSS------------------------- 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1515 lerqnraLRAELEallSSKDDVGKNVHELERARRV---AEQAASDLRTQVTELED--ELTAAEDAKLRLEVTVQALKAQH 1589
Cdd:pfam15921 466 -------LTAQLE---STKEMLRKVVEELTAKKMTlesSERTVSDLTASLQEKERaiEATNAEITKLRSRVDLKLQELQH 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1590 erdLQGRDDageerrrqlakQLRDAEVERDEERKQRAlamAARKKLELELEELKAQTSAAGQGKEEAvkqlKKMQAQMKE 1669
Cdd:pfam15921 536 ---LKNEGD-----------HLRNVQTECEALKLQMA---EKDKVIEILRQQIENMTQLVGQHGRTA----GAMQVEKAQ 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1670 LWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEEL-----AASDRAR--RQAQQDRDEMAEEVASGNlSKAATLE 1742
Cdd:pfam15921 595 LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklvnAGSERLRavKDIKQERDQLLNEVKTSR-NELNSLS 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1743 EKRQLEGRlgqleeeleEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQ-------LERQIQELRARLG 1815
Cdd:pfam15921 674 EDYEVLKR---------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkvamgMQKQITAKRGQID 744
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1816 ---------EEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVD 1872
Cdd:pfam15921 745 alqskiqflEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
859-1472 |
4.50e-14 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 78.09 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARaqelQKVQELQQQSAREVGELQGRVAQLEEER---------ARLAEQLRAEAELCSEAEETRARLAAR 929
Cdd:TIGR00618 244 YLTQKREAQEEQ----LKKQQLLKQLRARIEELRAQEAVLEETQerinrarkaAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 930 KQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIqelETHLEAEEGARQKLQLEKVTTEAK-MKKFEEDLLLLEDQ-- 1006
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEI---HIRDAHEVATSIREISCQQHTLTQhIHTLQQQKTTLTQKlq 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1007 --NSKLSKERRL--------------------------LEERLAEFSSQAAEEE-----EKVKSLNKLRVKYEATI---A 1050
Cdd:TIGR00618 397 slCKELDILQREqatidtrtsafrdlqgqlahakkqqeLQQRYAELCAAAITCTaqcekLEKIHLQESAQSLKEREqqlQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1051 DMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIqLGRKEEELQSALVRAEEEGGARAQLLKSLREAQ 1130
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTYAQLETSEEDVYHQLTSER 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1131 AGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQEL 1210
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQ 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1211 RQRHSQALVELT-----------EQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQg 1279
Cdd:TIGR00618 636 QCSQELALKLTAlhalqltltqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIE- 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1280 rssDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHdtqELLQEETRAKLALGSRVRALEAEAA 1359
Cdd:TIGR00618 715 ---EYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAH---FNNNEEVTAALQTGAELSHLAAEIQ 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1360 GLREQMEEEVvareragRELQTTQAQLSEWRRRQEEEAAVleageeARRRAAREAETLAQRLAEKTeaverlerarrRLQ 1439
Cdd:TIGR00618 789 FFNRLREEDT-------HLLKTLEAEIGQEIPSDEDILNL------QCETLVQEEEQFLSRLEEKS-----------ATL 844
|
650 660 670
....*....|....*....|....*....|...
gi 564328072 1440 QELDDATVDLGQQKQLLSTLEKKQRKFDQLLAE 1472
Cdd:TIGR00618 845 GEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
859-1381 |
4.99e-14 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 78.19 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQ---LRAEA-ELCSEAEETRARLAARKQELE 934
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEledLRAELeEVDKEFAETRDELKDYREKLE 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 935 LVVTELEARVGEEeecsRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKER 1014
Cdd:TIGR02169 396 KLKREINELKREL----DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1015 RLLEERLAEFS---SQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKG----------------------------- 1062
Cdd:TIGR02169 472 YDLKEEYDRVEkelSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGvhgtvaqlgsvgeryataievaagnrlnn 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1063 ---------RQELEKLKRRLDGESSELQEQMMEQKQR------------------------------------------- 1090
Cdd:TIGR02169 552 vvveddavaKEAIELLKRRKAGRATFLPLNKMRDERRdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvediea 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1091 AEELLIQ----------------------------LGRKEEELQSALVRAEEEG--GARAQLLKSLREAQAGLAEAQEDL 1140
Cdd:TIGR02169 632 ARRLMGKyrmvtlegelfeksgamtggsraprggiLFSRSEPAELQRLRERLEGlkRELSSLQSELRRIENRLDELSQEL 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1141 EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEE-EARTHEV--AMQELRQRHSQA 1217
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEElEEDLHKLeeALNDLEARLSHS 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1218 LV-ELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQ 1296
Cdd:TIGR02169 792 RIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE 871
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1297 RAQVELESVSTALSEAESKAIRLSKELSSAESQLH------DTQELLQEETRAKL-ALGSRVRALEAEAAGLREQMEEEV 1369
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEeleaqiEKKRKRLSELKAKLeALEEELSEIEDPKGEDEEIPEEEL 951
|
650
....*....|....*...
gi 564328072 1370 VA------RERAGRELQT 1381
Cdd:TIGR02169 952 SLedvqaeLQRVEEEIRA 969
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1220-1943 |
1.10e-13 |
|
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: 77.03 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1220 ELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEqKRRRLESQLQEVQG-----RSSDSERARAEAAEK 1294
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellkEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1295 LQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARE 1373
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGeLEAEIASLERSIAEKERELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1374 RAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQK 1453
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1454 QLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSK 1533
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1534 DDVGKNVHELERARRVAEQAASDLRTQVTELEDEL-----TAAEDAKLRlEVTVQALKAQHERDLQG---RDDAGEERRR 1605
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgTVAQLGSVG-ERYATAIEVAAGNRLNNvvvEDDAVAKEAI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1606 QLAKQLRDAEVE-------RDEERKQRALAMAARKKLELELEELKAQTSAA----------GQGKEEAVKQLKKmqAQMK 1668
Cdd:TIGR02169 565 ELLKRRKAGRATflplnkmRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvVEDIEAARRLMGK--YRMV 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1669 ELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASgnlSKAATLEEKRQLE 1748
Cdd:TIGR02169 643 TLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDE---LSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1749 GRLGQLEEELEEEQNNSELLKDHYRKLvlqvETLTTELSAERSFSAKAESGRQQLERQIQELRARLGE---EDAGARARQ 1825
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEEDL----SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDleaRLSHSRIPE 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1826 --------KMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLKR 1897
Cdd:TIGR02169 796 iqaelsklEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 564328072 1898 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
855-1303 |
1.15e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 76.64 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 855 KPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLeEERARLAEQLRAeaeLCSEAEETRARLAAR-KQEL 933
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKA---KKEELERLKKRLTGLtPEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 934 ELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKvtteakmkkfeedLLLLEDQNSKLSKE 1013
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG-------------RELTEEHRKELLEE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 RRLleeRLAEFSSQAAEEEEKVKSLNKLRVKYEATIADmEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEE 1093
Cdd:PRK03918 457 YTA---ELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1094 LLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaervarAKAEKQRRDLGEELEALRGELEDTLD 1173
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELE------ELGFESVEELEERLKELEPFYNEYLE 606
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1174 STNAQQELRS---KREQEVTELKKTLEEEARThEVAMQELRQRHSQALVELTEQLEQARRGKsvwektRLSLEAEVSELK 1250
Cdd:PRK03918 607 LKDAEKELEReekELKKLEEELDKAFEELAET-EKRLEELRKELEELEKKYSEEEYEELREE------YLELSRELAGLR 679
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 564328072 1251 TELSSLQTSRQEGEQKRRRLESQLQEVqgrssdsERARAEaAEKLQRAQVELE 1303
Cdd:PRK03918 680 AELEELEKRREEIKKTLEKLKEELEER-------EKAKKE-LEKLEKALERVE 724
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
887-1268 |
2.57e-13 |
|
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: 75.87 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 887 EVGELQGRVAQLEEERARLAEQLRaeaELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQ 966
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELR---RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 967 ELEthleaeegarqklqlekvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEfsSQAAEEEEKVKSLNKLRVKYE 1046
Cdd:TIGR02169 752 EIE------------------NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1047 ATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSL 1126
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1127 REAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQElrskrEQEVTELKKTLEEEARTHEVA 1206
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-----IPEEELSLEDVQAELQRVEEE 966
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1207 MQELRQRHSQALVELTEQleqarrgksvwEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRR 1268
Cdd:TIGR02169 967 IRALEPVNMLAIQEYEEV-----------LKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
924-1396 |
3.39e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.08 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 924 ARLAAR--KQELELVVTELEARVGEEEEcsRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1001
Cdd:PRK02224 174 ARLGVErvLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1002 LLEDqnskLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQ 1081
Cdd:PRK02224 252 ELET----LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1082 EQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEEL 1161
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1162 EALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAM-----QELRQR-HSQALVELTEQLEqarrgksvw 1235
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEGSpHVETIEEDRERVE--------- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1236 ektrlSLEAEVSELKTELSSLQtSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESK 1315
Cdd:PRK02224 479 -----ELEAELEDLEEEVEEVE-ERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1316 AIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAeaaglreqMEEEVVARERAGRELQTTQAQLSEWRRRQEE 1395
Cdd:PRK02224 553 AEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER--------IRTLLAAIADAEDEIERLREKREALAELNDE 624
|
.
gi 564328072 1396 E 1396
Cdd:PRK02224 625 R 625
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
872-1388 |
3.65e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 75.14 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 872 QELQKVQELQQQSAREVGELQGRVAQL------------------EEERAR---LAEQLRAEAELCSEAEETRARLAark 930
Cdd:pfam05483 219 EDHEKIQHLEEEYKKEINDKEKQVSLLliqitekenkmkdltfllEESRDKanqLEEKTKLQDENLKELIEKKDHLT--- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 931 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKL 1010
Cdd:pfam05483 296 KELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1011 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYE--ATIADMEDRLKKEEKgrqELEKLKRRLDGESSELQEQMMEQK 1088
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelKKILAEDEKLLDEKK---QFEKIAEELKGKEQELIFLLQARE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1089 QRAEELLIQL----------GRKEEELQSALVRAEEEGGA-----------RAQLLKSLREAQAGLAEAQEDLEAERVAR 1147
Cdd:pfam05483 450 KEIHDLEIQLtaiktseehyLKEVEDLKTELEKEKLKNIEltahcdkllleNKELTQEASDMTLELKKHQEDIINCKKQE 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1148 AKAEKQRRDLGE-------ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQR--HSQAL 1218
Cdd:pfam05483 530 ERMLKQIENLEEkemnlrdELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQieNKNKN 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1219 VELTEQLEQARRGKSVWEKTRLSL-EAEVSELKTELSS--------LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARA 1289
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAyEIKVNKLELELASakqkfeeiIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVK 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1290 EAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSaESQLHDTQEllQEETRAKLALGSRVRALEAEAAGLREQMEEEV 1369
Cdd:pfam05483 690 LQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDS-ELGLYKNKE--QEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
570
....*....|....*....
gi 564328072 1370 VARERAGRELQTTQAQLSE 1388
Cdd:pfam05483 767 EEKEKLKMEAKENTAILKD 785
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1049-1817 |
3.99e-13 |
|
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: 75.10 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1049 IADMEDRLKKEEKGRQELEKLKRRLD------GESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEggaraqL 1122
Cdd:TIGR02169 162 IAGVAEFDRKKEKALEELEEVEENIErldliiDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA------L 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1123 LKSLREAQAGLAEAQEDLEaervaraKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE-VTELKKTLEEEAR 1201
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1202 THEVAMQELRQ---RHSQALVELT---EQLEQARRGKSVWEKTRLSLEAEVSELKTELSSL-----------QTSRQEGE 1264
Cdd:TIGR02169 309 SIAEKERELEDaeeRLAKLEAEIDkllAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraeleevdkefAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1265 QKRRRLE--------------SQLQEVQGRSSDSERARAEAA---EKLQRAQVELESVSTALSEAESKAIRLSKELSSAE 1327
Cdd:TIGR02169 389 DYREKLEklkreinelkreldRLQEELQRLSEELADLNAAIAgieAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1328 SQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEAR 1407
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNR 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1408 rraareaetlAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRK-----------FDQLLAEEKAA 1476
Cdd:TIGR02169 549 ----------LNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlveFDPKYEPAFKY 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1477 VLRAVEDRERVEAEGRER-EARALSL--------------TRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVH 1541
Cdd:TIGR02169 619 VFGDTLVVEDIEAARRLMgKYRMVTLegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1542 ELERARRVAEQAASDLRTQVTELEDELTAAEDAklrlEVTVQALKAQHERDLQGRDDAGEERRRQLakqlrdAEVERDEE 1621
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQE----EEKLKERLEELEEDLSSLEQEIENVKSEL------KELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1622 RKQRALAmaarkkleleleelKAQTSAAGQGKEEAVKQLKKMQAQMkelwREVEETRSSREEMFtlsRESEKRLKGLEAE 1701
Cdd:TIGR02169 769 ELEEDLH--------------KLEEALNDLEARLSHSRIPEIQAEL----SKLEEEVSRIEARL---REIEQKLNRLTLE 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1702 VLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVET 1781
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
810 820 830
....*....|....*....|....*....|....*.
gi 564328072 1782 LTTELSAERSFSAKAESGRQQLERQIQELRARLGEE 1817
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
895-1929 |
8.08e-13 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 74.09 E-value: 8.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 895 VAQLEEERARLAEQLRAEAELCSEAEEtraRLAARKQELELVVTELEARVGEE--------EECSRQLQSEKKRL-QQHI 965
Cdd:NF041483 246 AAESDQARRQAAELSRAAEQRMQEAEE---ALREARAEAEKVVAEAKEAAAKQlasaesanEQRTRTAKEEIARLvGEAT 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 966 QELE-THLEAEEG-ARQKLQLEKVTTEAKMKKfeeDLLLLEDQNSKLSKERRLLEERLAEFSSQA-------AEEEEKVK 1036
Cdd:NF041483 323 KEAEaLKAEAEQAlADARAEAEKLVAEAAEKA---RTVAAEDTAAQLAKAARTAEEVLTKASEDAkattraaAEEAERIR 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1037 SLNKL---RVKYEAtiADMEDRLKKEEKGRQELEKLKrrldgeSSELQEQMMEQKQRAEELliqlgRKEEELQSALVRAE 1113
Cdd:NF041483 400 REAEAeadRLRGEA--ADQAEQLKGAAKDDTKEYRAK------TVELQEEARRLRGEAEQL-----RAEAVAEGERIRGE 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1114 EEGGARAQLLKSLREAQAGLAEAQEDL-EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQE-LRSKREQEVTE 1191
Cdd:NF041483 467 ARREAVQQIEEAARTAEELLTKAKADAdELRSTATAESERVRTEAIERATTLRRQAEETLERTRAEAErLRAEAEEQAEE 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1192 LKKTLEEEARthevamqELRqrhsqalvELTEQLEQARRGKSVWEKTRLSLEAEvSELKTELSSLQTSRQEGEQKRRRle 1271
Cdd:NF041483 547 VRAAAERAAR-------ELR--------EETERAIAARQAEAAEELTRLHTEAE-ERLTAAEEALADARAEAERIRRE-- 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1272 sqlqevqgRSSDSERARAEAAEKLQRAQVELES------------VSTALSEAESKAIRLSKELSSAESQLHDTQELLQE 1339
Cdd:NF041483 609 --------AAEETERLRTEAAERIRTLQAQAEQeaerlrteaaadASAARAEGENVAVRLRSEAAAEAERLKSEAQESAD 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1340 ETRAKLALGSRVRALEAeAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLeagEEARRRAAREAETLAQ 1419
Cdd:NF041483 681 RVRAEAAAAAERVGTEA-AEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEEL---LASARKRVEEAQAEAQ 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1420 RLAEKTEA-VERLERARRRLQQELDDATVDLGQQKQ-----LLSTLE--------KKQRKFDQLLAEEKAAVLRAVEDRE 1485
Cdd:NF041483 757 RLVEEADRrATELVSAAEQTAQQVRDSVAGLQEQAEeeiagLRSAAEhaaertrtEAQEEADRVRSDAYAERERASEDAN 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1486 RVEAEGREREARALSLtraleeeqeareelerqnralraeleallsSKDDVGKNVHELERARRVAEQAASDLRtqvTELE 1565
Cdd:NF041483 837 RLRREAQEETEAAKAL------------------------------AERTVSEAIAEAERLRSDASEYAQRVR---TEAS 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1566 DELTAAEDAKLRLEVtvqalkaqherdlQGRDDAgeERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQ 1645
Cdd:NF041483 884 DTLASAEQDAARTRA-------------DAREDA--NRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEA 948
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1646 TSAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSR-ESEKRLKGLEAEVLRLQEELAAS-----DRARRQA 1719
Cdd:NF041483 949 ERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRtEAERVKAEAAAEAERLRTEAREEadrtlDEARKDA 1028
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1720 QQDRDEMAEEV---ASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYR----------KLVLQVETLTTEL 1786
Cdd:NF041483 1029 NKRRSEAAEQAdtlITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAARKEAERivaeatvegnSLVEKARTDADEL 1108
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1787 --SAERSFSA---KAESGRQQLERQIQELRARLGEEDA----GARARQKMLIAALESKLAQAEEQLEQ--------ESRE 1849
Cdd:NF041483 1109 lvGARRDATAireRAEELRDRITGEIEELHERARRESAeqmkSAGERCDALVKAAEEQLAEAEAKAKElvsdanseASKV 1188
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1850 RILSgklVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRL-KQLKRQLEEAEEEASRAQAGRRRLQreleDVTESAE 1928
Cdd:NF041483 1189 RIAA---VKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTvEEGKRELDVLVRRREDINAEISRVQ----DVLEALE 1261
|
.
gi 564328072 1929 S 1929
Cdd:NF041483 1262 S 1262
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
788-1276 |
9.96e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 9.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 788 LAQLEEERdlkvtdiivsfqaaargylarrafqrrqqqqsalrvmqrncaaylklrnwqwwrlfikvkpLLQVTRQDEVL 867
Cdd:COG1196 360 LAEAEEAL-------------------------------------------------------------LEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 868 QARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEE 947
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 948 EECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQ 1027
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1028 AAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQE---LEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEE 1104
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1105 LQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDtldstnAQQELRSK 1184
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE------LAERLAEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1185 REQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELsslqtSRQEGE 1264
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPP-----DLEELE 766
|
490
....*....|..
gi 564328072 1265 QKRRRLESQLQE 1276
Cdd:COG1196 767 RELERLEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1288-1943 |
1.34e-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: 73.55 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1288 RAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAEsqlhDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQME 1366
Cdd:TIGR02168 174 RKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAE----RYKELKAELRELELALlVLRLEELREELEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1367 EEVVARERAGRELQTTQAQLSEWRRRQEEeaavleageearrraareaetlaqrlaekteaverlerarrrLQQELDDAT 1446
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSE------------------------------------------LEEEIEELQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1447 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAEL 1526
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1527 EALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELtaaedaklrlevtvQALKAQHERDLQGRDDAGEERRRQ 1606
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARL--------------ERLEDRRERLQQEIEELLKKLEEA 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1607 LAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVE-ETRSSREEMf 1685
Cdd:TIGR02168 434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgFSEGVKALL- 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1686 tLSRESEKRLKGLEAEVLRLQEE----LAASDRARRQAQQDRDE--------------------MAEEVASGNLSKAATL 1741
Cdd:TIGR02168 513 -KNQSGLSGILGVLSELISVDEGyeaaIEAALGGRLQAVVVENLnaakkaiaflkqnelgrvtfLPLDSIKGTEIQGNDR 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1742 EEKRQLEGRLGQLEEELEEEQNNSELLKD-----------------------HYRKLVLQVETLTTELSAERSfSAKAES 1798
Cdd:TIGR02168 592 EILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvvddldnalelakklrpGYRIVTLDGDLVRPGGVITGG-SAKTNS 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1799 GRQQLERQIQELRARLgEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVA 1878
Cdd:TIGR02168 671 SILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1879 DQLRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
938-1329 |
4.38e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 938 TELEARVGEEEECSRQLQSEKKRLQQHIQELETHLE---------AEEGARQKLQLEK-----VTTEAKMKKFEEDLLLL 1003
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISntqtqlnqlKDEQNKIKKQLSEkqkelEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1004 EDQNSKLSKERRllEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELE----KLKRRLDGESSE 1079
Cdd:TIGR04523 294 KSEISDLNNQKE--QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEsensEKQRELEEKQNE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1080 LqEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVaraKAEKQRRDLGE 1159
Cdd:TIGR04523 372 I-EKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII---KNNSEIKDLTN 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1160 ELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQAlVELTEQLEQARRGKSVWEKTR 1239
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK-KELEEKVKDLTKKISSLKEKI 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1240 LSLEAEVSELKTELSSLQTSRQEGEQ--KRRRLESQLQEVQGR-------SSDSERARAEAAEKLQRAQVELESVSTALS 1310
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFelKKENLEKEIDEKNKEieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
410
....*....|....*....
gi 564328072 1311 EAESKAIRLSKELSSAESQ 1329
Cdd:TIGR04523 607 EKEKKISSLEKELEKAKKE 625
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1138-1628 |
5.74e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1138 EDLEAERVARAKAEKQRRDLgEELEALRGELEDTLDSTNAQQELRSK-----REQEVTELKK---TLEEEARTHEVAMQE 1209
Cdd:COG4913 235 DDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAAlrlwfAQRRLELLEAeleELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1210 LRQRHSQALVELtEQLEQARRGKSVwektrlsleAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARA 1289
Cdd:COG4913 314 LEARLDALREEL-DELEAQIRGNGG---------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1290 EAAEKLQRAQVELESVSTALSEAESKAIRlskELSSAESQLHDTQELLQEETRAKLALGSRV---RALEAEAAGLRE--- 1363
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEA---ALRDLRRELRELEAEIASLERRKSNIPARLlalRDALAEALGLDEael 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1364 ---------QMEEEV--VARERAGRELQTT-------QAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEK- 1424
Cdd:COG4913 461 pfvgelievRPEEERwrGAIERVLGGFALTllvppehYAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKl 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1425 -------TEAVERLERARRR-----LQQELDDA----TVDlGQQKQLLSTLEKKQRK------------------FDQLL 1470
Cdd:COG4913 541 dfkphpfRAWLEAELGRRFDyvcvdSPEELRRHpraiTRA-GQVKGNGTRHEKDDRRrirsryvlgfdnraklaaLEAEL 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1471 AEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNR--ALRAELEALLSSKDDVGknvhELERARR 1548
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiaELEAELERLDASSDDLA----ALEEQLE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1549 VAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDlqgRDDAGEERRRQLAKQLRDAEVERDEERKQRALA 1628
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---EDLARLELRALLEERFAAALGDAVERELRENLE 772
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
853-1278 |
7.12e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 70.82 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 853 KVKPLLQVTRQDEVLQARAQELQ-KVQELQQQSAREV-GELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 931 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKL 1010
Cdd:TIGR04523 352 TNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1011 SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEkgrQELEKLKRRLDGESSELQEQMMEQKQR 1090
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK---QNLEQKQKELKSKEKELKKLNEEKKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1091 AEElliqlgrkeeelqsalvraeeeggaraqlLKSLREAQAGLAEAQEDLEAErvaRAKAEKQRRDLGEELEalrgELED 1170
Cdd:TIGR04523 509 EEK-----------------------------VKDLTKKISSLKEKIEKLESE---KKEKESKISDLEDELN----KDDF 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1171 TLDSTNAQQELRSKrEQEVTELKKTLEEEARTHEVAmQELRQRHSQALVELTEQLEQarrgksvWEKTRLSLEAEVSELK 1250
Cdd:TIGR04523 553 ELKKENLEKEIDEK-NKEIEELKQTQKSLKKKQEEK-QELIDQKEKEKKDLIKEIEE-------KEKKISSLEKELEKAK 623
|
410 420
....*....|....*....|....*...
gi 564328072 1251 TELSSLQTSRQEGEQKRRRLESQLQEVQ 1278
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
842-1392 |
1.36e-11 |
|
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: 70.25 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 842 LRNWQWWRLFIKVKP----LLQVTRQDEVLQARAQELQK-VQELQQQSAREVGELQGRVAQLEEERARLAEQLRAE-AEL 915
Cdd:pfam12128 227 IRDIQAIAGIMKIRPeftkLQQEFNTLESAELRLSHLHFgYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKrDEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 916 CSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKk 995
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIK- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 996 fEEDLLLLEDQNSKLSKERrllEERlaefSSQAAEEEEKVKSL-NKLRVKYEATIAdmedRLKKEEKGRQE-LEKLKRRL 1073
Cdd:pfam12128 386 -EQNNRDIAGIKDKLAKIR---EAR----DRQLAVAEDDLQALeSELREQLEAGKL----EFNEEEYRLKSrLGELKLRL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1074 DG-----ESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEeegGARAQLLKSLREAQAGLAE-AQEDLEAERVAR 1147
Cdd:pfam12128 454 NQatatpELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR---KRRDQASEALRQASRRLEErQSALDELELQLF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1148 AKAekqrrdlGEELEALRGELEDTLDSTNaqqELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQ 1227
Cdd:pfam12128 531 PQA-------GTLLHFLRKEAPDWEQSIG---KVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1228 ArrgksvwektrlsLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVST 1307
Cdd:pfam12128 601 E-------------LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKD 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1308 ALSEAESKAIRLS-KELSSAESQL----HDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRE-LQT 1381
Cdd:pfam12128 668 KKNKALAERKDSAnERLNSLEAQLkqldKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSgAKA 747
|
570
....*....|.
gi 564328072 1382 TQAQLSEWRRR 1392
Cdd:pfam12128 748 ELKALETWYKR 758
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
865-1387 |
1.96e-11 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 69.47 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 865 EVLQARAQELQKVQELQQQSAR------EVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRArlaarkqeLELVVT 938
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKA--------LQTVIE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 939 ELEARVGEEEECSRQLQSEKKRL-----------QQHIQELE---THLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE 1004
Cdd:pfam10174 237 MKDTKISSLERNIRDLEDEVQMLktngllhtedrEEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1005 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklRVKYEatiaDMEDRLKKEEKGRQELEKLKRRLDGESSELQeQM 1084
Cdd:pfam10174 317 NQNSDCKQHIEVLKESLTAKEQRAAILQTEVDAL---RLRLE----EKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-DM 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1085 MEQKQRA--------EELLIQLGRKE---EELQSALVRAEEEGGARAQLLKSLREAqagLAEAQEDLEAERVARAKAEKQ 1153
Cdd:pfam10174 389 LDVKERKinvlqkkiENLQEQLRDKDkqlAGLKERVKSLQTDSSNTDTALTTLEEA---LSEKERIIERLKEQREREDRE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1154 RRdlgEELEALRGELEDTLDSTNAQQELRSKREQEVTELKktleEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKS 1233
Cdd:pfam10174 466 RL---EELESLKKENKDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLEN 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1234 VWEKTRlslEAEVSElktelsslqTSRQEGEQKRRRLEsqlQEVQGRSSDSERARAEAA---EKLQRAQVELESVSTALS 1310
Cdd:pfam10174 539 QLKKAH---NAEEAV---------RTNPEINDRIRLLE---QEVARYKEESGKAQAEVErllGILREVENEKNDKDKKIA 603
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1311 EAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRvRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLS 1387
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARR-REDNLADNSQQLQLEELMGALEKTRQELDATKARLS 679
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1261-1943 |
4.05e-11 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 68.66 E-value: 4.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1261 QEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQrAQVELesvstaLSEAESKAIRLSKELSSAESQLHDTQELLQEE 1340
Cdd:pfam01576 15 QKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-AETEL------CAEAEEMRARLAARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1341 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLsewrRRQEEEAAVLEageearrraareaetlaqr 1420
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKI----KKLEEDILLLE------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1421 laektEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEekaavlraVEDRERVEAEGRErearals 1500
Cdd:pfam01576 145 -----DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISD--------LEERLKKEEKGRQ------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1501 ltraleeeqeareelerqnralraeleallsskddvgknvhELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEV 1580
Cdd:pfam01576 205 -----------------------------------------ELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1581 TVQALKAQHErDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQ------TSAAGQ--- 1651
Cdd:pfam01576 244 ELQAALARLE-EETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEledtldTTAAQQelr 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1652 -GKEEAVKQLKKMQAqmkelwrevEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEV 1730
Cdd:pfam01576 323 sKREQEVTELKKALE---------EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAEL 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1731 ASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQEL 1810
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1811 RARLGEEdagarARQKMLIA----ALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLE 1886
Cdd:pfam01576 474 QELLQEE-----TRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1887 KSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:pfam01576 549 RLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
960-1627 |
5.39e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 960 RLQQHIQEL-ETHLEAEEGARQKLQLEKVTTEA-KMKKFEEDLLLLEDQNSKL-----SKERRLLEERLAEFSSQAAEEE 1032
Cdd:COG4913 229 ALVEHFDDLeRAHEALEDAREQIELLEPIRELAeRYAAARERLAELEYLRAALrlwfaQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1033 EKVKSLNKLRVKYEATIADMEDRLkkEEKGRQELEKLKRRLDGESSELQEQMMEQkQRAEELLIQLGrkeeeLQSALVRA 1112
Cdd:COG4913 309 AELERLEARLDALREELDELEAQI--RGNGGDRLEQLEREIERLERELEERERRR-ARLEALLAALG-----LPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1113 EeeggaraqllksLREAQAGLAEAQEDLEAERvarAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTEL 1192
Cdd:COG4913 381 E------------FAALRAEAAALLEALEEEL---EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1193 KKTLEEEARTHEVAMQ------ELRQR------------HSQA---LVElTEQLEQARR--------GKSVWEKTRLSLE 1243
Cdd:COG4913 446 RDALAEALGLDEAELPfvgeliEVRPEeerwrgaiervlGGFAltlLVP-PEHYAAALRwvnrlhlrGRLVYERVRTGLP 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1244 AE----------VSELKTELSSLQ----------------TSRQEGEQKRRRLESQLQEVQGRSS----DSERARAE--- 1290
Cdd:COG4913 525 DPerprldpdslAGKLDFKPHPFRawleaelgrrfdyvcvDSPEELRRHPRAITRAGQVKGNGTRhekdDRRRIRSRyvl 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1291 ---AAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQ------------------EETRAKLALGS 1349
Cdd:COG4913 605 gfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidvasaereiaelEAELERLDASS 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1350 -RVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAetLAQRLAEKTEAv 1428
Cdd:COG4913 685 dDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL--LEERFAAALGD- 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1429 ERLERARRRLQQELDDATvdlGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSltraleee 1508
Cdd:COG4913 762 AVERELRENLEERIDALR---ARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLP-------- 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1509 qeareelerqnrALRAELEALL--SSKDDVGKNVHELERARRVAEQaasdlrtQVTELEDELTAAE---DAKLRLEVTV- 1582
Cdd:COG4913 831 ------------EYEERFKELLneNSIEFVADLLSKLRRAIREIKE-------RIDPLNDSLKRIPfgpGRYLRLEARPr 891
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1583 ---------QALKAQHERDLQGRDDAGEERRRQLA---KQLRDAEVERDEERKQRAL 1627
Cdd:COG4913 892 pdpevrefrQELRAVTSGASLFDEELSEARFAALKrliERLRSEEEESDRRWRARVL 948
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
890-1344 |
5.74e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 67.82 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 890 ELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTE----------LEARVGEEEECSRQLQSEKK 959
Cdd:pfam05483 100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEnnatrhlcnlLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 960 RLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMK-KFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSL 1038
Cdd:pfam05483 180 ETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1039 NKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSE----LQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEE 1114
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDikmsLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1115 EGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNaqqelrsKREQEVTELKK 1194
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKN-------NKEVELEELKK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1195 TLEEEarthEVAMQELRQrhsqaLVELTEQLEQARRGKSVWEKTRlslEAEVSELKTELSSLQTSRQEGEQKRRRLESQL 1274
Cdd:pfam05483 413 ILAED----EKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTEL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1275 QEVQGR----SSDSERARAEAAEKLQRAQ---VELESVSTALSEAESKAIRLSKE---LSSAESQLHDTQELLQEETRAK 1344
Cdd:pfam05483 481 EKEKLKnielTAHCDKLLLENKELTQEASdmtLELKKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQK 560
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
867-1228 |
6.57e-11 |
|
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: 68.06 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 867 LQARAQELQKVQELQQQsarevgelQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE 946
Cdd:COG3096 329 YQAASDHLNLVQTALRQ--------QEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLAD 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 947 EEECSRQLQSEKKRLQQHIQELEThleaeegARQKLQLEKVTTEAkmkkFEEDLLLLEDQNSKLSKERRLLEERLAEFSS 1026
Cdd:COG3096 401 YQQALDVQQTRAIQYQQAVQALEK-------ARALCGLPDLTPEN----AEDYLAAFRAKEQQATEEVLELEQKLSVADA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1027 QAAEEEEKVKSLNKlrvkyeatIADMEDRLKKEEKGRQ------ELEKLKRRLDGESSELQE--QMMEQKQRAEELLIQL 1098
Cdd:COG3096 470 ARRQFEKAYELVCK--------IAGEVERSQAWQTAREllrryrSQQALAQRLQQLRAQLAEleQRLRQQQNAERLLEEF 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1099 GRK-------EEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT 1171
Cdd:COG3096 542 CQRigqqldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEA 621
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1172 LDSTnaqqelrskreQEVTELKKTLEEEARTHEVAMQELRQRhSQALVELTEQLEQA 1228
Cdd:COG3096 622 LADS-----------QEVTAAMQQLLEREREATVERDELAAR-KQALESQIERLSQP 666
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
872-1181 |
6.66e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.46 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 872 QELQKVQELQQQSAREVGElQGRVAQLEEERARLAEQLR--AEAELCSEAEETRA--------RLA-ARKQELELVVTEL 940
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKME-QERLRQEKEEKAREVERRRklEEAEKARQAEMDRQaaiyaeqeRMAmERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 941 EAR----VGEEE---ECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKE 1013
Cdd:pfam17380 358 RKRelerIRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 RRLLEERLAEFSSQAAEEEEKVKSLNKLRvKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEE 1093
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLR-QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1094 LliqLGRKEEELQSALVRAEEEggaraqllkslREAQAGLAEAQEDLEAERVARA--KAEKQRRDLgEELEALRGELEDT 1171
Cdd:pfam17380 517 L---LEKEMEERQKAIYEEERR-----------REAEEERRKQQEMEERRRIQEQmrKATEERSRL-EAMEREREMMRQI 581
|
330
....*....|
gi 564328072 1172 LDSTNAQQEL 1181
Cdd:pfam17380 582 VESEKARAEY 591
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1118-1330 |
8.00e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1118 ARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLE 1197
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1198 E---EARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQL 1274
Cdd:COG4942 101 AqkeELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1275 QEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQL 1330
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1154-1923 |
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 564328072 1154 RRDLGEELEALRGELeDTLDStnAQQELRSKREQevtelKKTLEEEARTHEvAMQELRQRHSQA-LVELTEQLEQARRGK 1232
Cdd:COG4913 220 EPDTFEAADALVEHF-DDLER--AHEALEDAREQ-----IELLEPIRELAE-RYAAARERLAELeYLRAALRLWFAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1233 SVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRssdserARAEAAEKLQRAQVELESVSTALSEA 1312
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD------RLEQLEREIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1313 ESKAIRLSKELSSAESQLHDTQELLQEetraklalgsRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRR 1392
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEAAA----------LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1393 QeeeaAVLEAGEEARRRAareaetLAQRLAEKTEAVERLErarrrlqqELDDatVDLGQQK------QLLSTLekkqrKF 1466
Cdd:COG4913 435 K----SNIPARLLALRDA------LAEALGLDEAELPFVG--------ELIE--VRPEEERwrgaieRVLGGF-----AL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1467 DqLLAEEK--AAVLRAVEDR--------ERVEAEGREREARAL---SLTRALEEEQEareelerqnrALRAELEALLSSK 1533
Cdd:COG4913 490 T-LLVPPEhyAAALRWVNRLhlrgrlvyERVRTGLPDPERPRLdpdSLAGKLDFKPH----------PFRAWLEAELGRR 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1534 DDV------------------------GKNVHELERARRVAEQAA--SDLRTQVTELEDELTAAEDAKLRLEVTVQALKA 1587
Cdd:COG4913 559 FDYvcvdspeelrrhpraitragqvkgNGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEA 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1588 QHERdLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAarkkleleleelkaqtsaagqgkEEAVKQLKKMQAQM 1667
Cdd:COG4913 639 ELDA-LQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-----------------------DASSDDLAALEEQL 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1668 KELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELaasDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQL 1747
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL---EAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1748 EGRL-GQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAK----AESGRQQLERQIQELRARLGEEDAGAr 1822
Cdd:COG4913 772 EERIdALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALldrlEEDGLPEYEERFKELLNENSIEFVAD- 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1823 arqkmLIAALESKLAQAEEQLEQ------------ESRERILSGKLVRRAEKRLKEVVLQVDEERRVADqlRDQLEKSNL 1890
Cdd:COG4913 851 -----LLSKLRRAIREIKERIDPlndslkripfgpGRYLRLEARPRPDPEVREFRQELRAVTSGASLFD--EELSEARFA 923
|
810 820 830
....*....|....*....|....*....|...
gi 564328072 1891 RLKQLKRQLeeaeeeASRAQAGRRRLQRELEDV 1923
Cdd:COG4913 924 ALKRLIERL------RSEEEESDRRWRARVLDV 950
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1079-1844 |
1.10e-10 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 67.30 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1079 ELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQ--AGLAEAQEDLEAERVA-RAKAEKQRR 1155
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQllTLCTPCMPDTYHERKQvLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1156 DLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVW 1235
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1236 EKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQraQVELESVSTALSEAESK 1315
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQ--QHTLTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1316 AIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEE 1395
Cdd:TIGR00618 391 LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1396 EAAVLeageearrraaREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKa 1475
Cdd:TIGR00618 471 REQQL-----------QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA- 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1476 avlRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRvaeqaas 1555
Cdd:TIGR00618 539 ---QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED------- 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1556 dlrtqvteledeltaaedaKLRLEVTVQALKAQHERDLQgrDDAGEERRRQLAKQLRDAEVERDEE----RKQRALAMAA 1631
Cdd:TIGR00618 609 -------------------MLACEQHALLRKLQPEQDLQ--DVRLHLQQCSQELALKLTALHALQLtltqERVREHALSI 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1632 RKKLELELEELKAQTSAAgQGKEEAVKQLKKMQAQMKELWREVEET-RSSREEMFTLSRESEKRLKGLEAEVLRLQEELA 1710
Cdd:TIGR00618 668 RVLPKELLASRQLALQKM-QSEKEQLTYWKEMLAQCQTLLRELETHiEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1711 ASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDH---YRKLVLQVETLTTELS 1787
Cdd:TIGR00618 747 ELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEigqEIPSDEDILNLQCETL 826
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1788 AERsfsakaesgRQQLERQIQELRARLGE-----EDAGARARQKMLIAALESKLAQAEEQLE 1844
Cdd:TIGR00618 827 VQE---------EEQFLSRLEEKSATLGEithqlLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
858-1275 |
1.19e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 858 LQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELV- 936
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLAt 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 937 ---VTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLedqnsklske 1013
Cdd:COG4717 191 eeeLQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLA---------- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 rrlleerLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKE-EKGRQELEKLKRRLDGESSELQEQMMEQ---KQ 1089
Cdd:COG4717 261 -------LLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASlGKEAEELQALPALEELEEEELEELLAALglpPD 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1090 RAEELLIQLGRKEEELQSALVRAEEEgGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELE 1169
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEEL-EEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1170 DTLDSTNAQQELRSKR--EQEVTELKKTLEEEARTHEVAMQELRqrhsqalvELTEQLEQARRGKSVWEKT--RLSLEAE 1245
Cdd:COG4717 413 ELLGELEELLEALDEEelEEELEELEEELEELEEELEELREELA--------ELEAELEQLEEDGELAELLqeLEELKAE 484
|
410 420 430
....*....|....*....|....*....|
gi 564328072 1246 VSELKTELSSLQTSRQEGEQKRRRLESQLQ 1275
Cdd:COG4717 485 LRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1291 |
1.45e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 66.63 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 922 TRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLL 1001
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1002 LLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVkslnklrVKYEATIADMEDRLKKEEKgrQELEKLKRRLDGESSELQ 1081
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDL-------HKLEEALNDLEARLSHSRI--PEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1082 EQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaervaraKAEKQRRDLGEEL 1161
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-------ELEAALRDLESRL 884
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1162 EALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSvwEKTRLS 1241
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDV--QAELQR 962
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1242 LEAEVSELKT-------ELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEA 1291
Cdd:TIGR02169 963 VEEEIRALEPvnmlaiqEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
998-1834 |
2.12e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 66.51 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 998 EDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLnklrvkyEATIADMEDRLKKEEKGRQELEKLKRRLDgES 1077
Cdd:COG3096 285 ERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDL-------EQDYQAASDHLNLVQTALRQQEKIERYQE-DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1078 SELQEQMMEQKQRAEELLIQLGRKEEELQsalvRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDL 1157
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLE----AAEEE----------VDSLKSQLADYQQALDVQQ-TRAIQYQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1158 GEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLE------EEART-HEVAMQELRQ-----RHSQALVELTEQL 1225
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEqklsvaDAARRqFEKAYELVCKiagevERSQAWQTARELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1226 EQARRGKSvwektrlsLEAEVSELKTELSSLqtsRQEgEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESV 1305
Cdd:COG3096 502 RRYRSQQA--------LAQRLQQLRAQLAEL---EQR-LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1306 STALSEAESKAIRLSKELSSAESQ-------------LHDTQELLQEETRAKLAlgsrvraleaEAAGLREQMEEeVVAR 1372
Cdd:COG3096 570 EEQAAEAVEQRSELRQQLEQLRARikelaarapawlaAQDALERLREQSGEALA----------DSQEVTAAMQQ-LLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1373 ERagrELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAReaeTLAQR-----LAEKTEAVErlerarrrlqqeLDDATV 1447
Cdd:COG3096 639 ER---EATVERDELAARKQALESQIERLSQPGGAEDPRLL---ALAERlggvlLSEIYDDVT------------LEDAPY 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1448 ---------------DLGQQKQLLSTL----------EKKQRKFDQLL---AEEKAAVLRAVEDRE-------RVEAEGR 1492
Cdd:COG3096 701 fsalygparhaivvpDLSAVKEQLAGLedcpedlyliEGDPDSFDDSVfdaEELEDAVVVKLSDRQwrysrfpEVPLFGR 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1493 E-REARAlsltraleeeqeareelerqnRALRAELEALLSSKDDVGKNVHELERA-----RRVA-----------EQAAS 1555
Cdd:COG3096 781 AaREKRL---------------------EELRAERDELAEQYAKASFDVQKLQRLhqafsQFVGghlavafapdpEAELA 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1556 DLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHE--RDLQGR-----DDAGEERRRQLAKQLRDAEVERDEERKQRAlA 1628
Cdd:COG3096 840 ALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllNKLLPQanllaDETLADRLEELREELDAAQEAQAFIQQHGK-A 918
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1629 MAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELwREVEETR-----SSREEMFTLSRESEKRLKgleAEVL 1703
Cdd:COG3096 919 LAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL-SEVVQRRphfsyEDAVGLLGENSDLNEKLR---ARLE 994
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1704 RLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGR---LGQLEEELEEEQNNSEllkdhyrklvlqVE 1780
Cdd:COG3096 995 QAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQEleeLGVQADAEAEERARIR------------RD 1062
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1781 TLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALES 1834
Cdd:COG3096 1063 ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1522-1943 |
2.94e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1522 LRAELEALLSSKDDVGKNVHELERARR-VAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAG 1600
Cdd:COG4913 257 IRELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1601 EERRRQLAKQLRDAEVERDeERKQRALAMAarkkleleleelkAQTSAAGQGKEEAVKQLKKMQAQMKELwreVEETRSS 1680
Cdd:COG4913 337 GDRLEQLEREIERLERELE-ERERRRARLE-------------ALLAALGLPLPASAEEFAALRAEAAAL---LEALEEE 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1681 REEMFTLSRESEKRLKGLEAEVLRLQEELAASDRAR----RQAQQDRDEMAEE--------------------------- 1729
Cdd:COG4913 400 LEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALAEAlgldeaelpfvgelievrpeeerwrga 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1730 -------------VASGNLSKAATLEEKRQLEGRL-GQLEEELEEEQNNSELLKDHY-RKLVLQVETLTTELSAE--RSF 1792
Cdd:COG4913 480 iervlggfaltllVPPEHYAAALRWVNRLHLRGRLvYERVRTGLPDPERPRLDPDSLaGKLDFKPHPFRAWLEAElgRRF 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1793 S-AKAESGrQQLER---------QIQELRARlGEEDA----------GARARQKmlIAALESKLAQAEEQLEQ-ESRERI 1851
Cdd:COG4913 560 DyVCVDSP-EELRRhpraitragQVKGNGTR-HEKDDrrrirsryvlGFDNRAK--LAALEAELAELEEELAEaEERLEA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1852 LSGKL-----VRRAEKRLKEV------VLQVDEERRVADQLRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQREL 1920
Cdd:COG4913 636 LEAELdalqeRREALQRLAEYswdeidVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500
....*....|....*....|...
gi 564328072 1921 EDVTESAESMNREVTTLRNRLRR 1943
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEA 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1005-1213 |
3.67e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 64.01 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1005 DQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQM 1084
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1085 MEQKQRAEELLIQLGRKE--------------EELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKA 1150
Cdd:COG4942 100 EAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564328072 1151 EKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQR 1213
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
863-1255 |
4.63e-10 |
|
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: 64.53 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 942
Cdd:pfam07888 43 RAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 943 RVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLA 1022
Cdd:pfam07888 123 QRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1023 EFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELqeqmmeqkqraEELLIQLGRKE 1102
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL-----------SSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1103 EELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDL------EAERVARAKAEKQRRD--LGEEL---EALRGELEDT 1171
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADASLALREGRARWAQERETLqqsaeaDKDRIEKLSAELQRLEerLQEERmerEKLEVELGRE 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1172 LDSTNAQqelRSKREQEVTELKKTLEEEARThevamQELRQRHSQALVELTEQLEQaRRGKSVWEKTRLSLEAEVSELKT 1251
Cdd:pfam07888 352 KDCNRVQ---LSESRRELQELKASLRVAQKE-----KEQLQAEKQELLEYIRQLEQ-RLETVADAKWSEAALTSTERPDS 422
|
....
gi 564328072 1252 ELSS 1255
Cdd:pfam07888 423 PLSD 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1017-1867 |
6.07e-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: 64.75 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1017 LEERLAEFSSQAAEEEEKVKSLNKLRVKYE----ATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQ----- 1087
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTvhele 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1088 --KQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAE--RVARAKAEKQRRDLGEELEA 1163
Cdd:pfam15921 156 aaKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMhfRSLGSAISKILRELDTEISY 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1164 LRGEL---EDTLDSTNAqqELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVE---LTEQLE----QARRGKS 1233
Cdd:pfam15921 236 LKGRIfpvEDQLEALKS--ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQansIQSQLEiiqeQARNQNS 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1234 VWEKTRLSLEAEVSELKTELsslQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAE-------KLQRAQVELESVS 1306
Cdd:pfam15921 314 MYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQesgnlddQLQKLLADLHKRE 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1307 TALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQL 1386
Cdd:pfam15921 391 KELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1387 SEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKF 1466
Cdd:pfam15921 471 ESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTEC 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1467 D--QLLAEEKAAVLRAVedRERVE-----AEGREREARALSLTRALEEEQEAREELERQnralraELEALLSSKDDVGKN 1539
Cdd:pfam15921 551 EalKLQMAEKDKVIEIL--RQQIEnmtqlVGQHGRTAGAMQVEKAQLEKEINDRRLELQ------EFKILKDKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1540 VH------ELERARRVAE-----QAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKaqheRDLQGRDDAGEERRRQLA 1608
Cdd:pfam15921 623 LEarvsdlELEKVKLVNAgserlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK----RNFRNKSEEMETTTNKLK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1609 KQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAgQGKEEAVKQlkKMQAQMKELWREVEETRSSREEMFTLS 1688
Cdd:pfam15921 699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAK-RGQIDALQS--KIQFLEEAMTNANKEKHFLKEEKNKLS 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1689 RE-----SEKRLKGLEAEVLRLQEEL---------AASDRARRQAQQDRDEMA-EEVASGNLSKAATLEEKRQLEGRLGQ 1753
Cdd:pfam15921 776 QElstvaTEKNKMAGELEVLRSQERRlkekvanmeVALDKASLQFAECQDIIQrQEQESVRLKLQHTLDVKELQGPGYTS 855
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1754 LEEELEEEQNNSELLKDHYRklVLQVETLTTELSAE-RSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKML---- 1828
Cdd:pfam15921 856 NSSMKPRLLQPASFTRTHSN--VPSSQSTASFLSHHsRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKgrap 933
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 564328072 1829 -IAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEV 1867
Cdd:pfam15921 934 sLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKSSET 973
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
863-1091 |
1.08e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 942
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 943 RVGE-EEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERL 1021
Cdd:COG4942 98 ELEAqKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE----LRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1022 AEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRA 1091
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
869-1338 |
1.24e-09 |
|
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: 63.22 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 869 ARAQELQKVQELQQQSAREVG---ELQGRVAQLEEERARLAEQLRAEAELC---------------------SEAEET-- 922
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDrnqELQKRIRLLEKREAEAEEALREQAELNrlkkkylealnkklnekesqlADAREVis 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 923 --RARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQH---IQELETHLEAEEGARQKLQlekvTTEAKMKKFE 997
Cdd:pfam05557 108 clKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAeqlRQNLEKQQSSLAEAEQRIK----ELEFEIQSQE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 998 EDLLLLEDQNSKLskerrlleERLAEFSSQAAEEEEKVKSLNKLRVK---YEATIADMEDRLKKEEKGRQELEKLKRRLD 1074
Cdd:pfam05557 184 QDSEIVKNSKSEL--------ARIPELEKELERLREHNKHLNENIENkllLKEEVEDLKRKLEREEKYREEAATLELEKE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1075 GESSELQE-----QMMEQKQRAEELLiqLGRKEEELQSALVRAEEEGGARAQLL---KSLREAQAGLAEAQEDLEAERVA 1146
Cdd:pfam05557 256 KLEQELQSwvklaQDTGLNLRSPEDL--SRRIEQLQQREIVLKEENSSLTSSARqleKARRELEQELAQYLKKIEDLNKK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1147 RAKAEKQRRDL-------GEELEALRGELED-----TLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRH 1214
Cdd:pfam05557 334 LKRHKALVRRLqrrvlllTKERDGYRAILESydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1215 SQALVELTEQLEQARRGKSVWEktRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQL--QEVQGRS----------- 1281
Cdd:pfam05557 414 KQQAQTLERELQALRQQESLAD--PSYSKEEVDSLRRKLETLELERQRLREQKNELEMELerRCLQGDYdpkktkvlhls 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1282 ----SDSERARAEAAEKLQ-----------RAQVELESV----STALSEAESKAIRLSKELSSAESQLHDTQELLQ 1338
Cdd:pfam05557 492 mnpaAEAYQQRKNQLEKLQaeierlkrllkKLEDDLEQVlrlpETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ 567
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
896-1125 |
1.82e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 896 AQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEae 975
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 976 egaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRL--LEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADME 1053
Cdd:COG4942 101 ---AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1054 DRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLiqlgRKEEELQSALVRAEEEGGARAQLLKS 1125
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ----QEAEELEALIARLEAEAAAAAERTPA 245
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
857-1592 |
1.96e-09 |
|
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: 63.21 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVLQARAQELQKVQELQQQSARE-VGELQGRVAQLEEERARLAEQLRAEaelcSEAEETRarlaarKQELEL 935
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQsVIDLQTKLQEMQMERDAMADIRRRE----SQSQEDL------RNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 936 VVTELEArvgeeEECSRQLQSEKKRLQqhIQELETHLEAEEGARQKLQLEKVT-TEAKMKKFEE----DLLLLEDQNSKL 1010
Cdd:pfam15921 150 TVHELEA-----AKCLKEDMLEDSNTQ--IEQLRKMMLSHEGVLQEIRSILVDfEEASGKKIYEhdsmSTMHFRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1011 SKERRLLEERLAEFSSQAAEEEEKVKSL-NKLRVKYEATIADMEDRLkkeekgrqelEKLKRRLDGESSELQEQMMEQKQ 1089
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALkSESQNKIELLLQQHQDRI----------EQLISEHEVEITGLTEKASSARS 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1090 RAEELLIQLGRKEEELQSA----LVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1165
Cdd:pfam15921 293 QANSIQSQLEIIQEQARNQnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQES 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1166 GELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQrhsqalvELTEQLEQARRgksvwektrlsLEAE 1245
Cdd:pfam15921 373 GNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRR-------ELDDRNMEVQR-----------LEAL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1246 VSELKTELSSlqtsrqegeqkrrRLESQLQEVQGRSsdseraraEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSS 1325
Cdd:pfam15921 435 LKAMKSECQG-------------QMERQMAAIQGKN--------ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLES 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1326 AESQLHDTQELLQEETRAklalgsrVRALEAEAAGLREQMEEEVvareragRELQTTQAQLSEWRRRQEEEAAvleagee 1405
Cdd:pfam15921 494 SERTVSDLTASLQEKERA-------IEATNAEITKLRSRVDLKL-------QELQHLKNEGDHLRNVQTECEA------- 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1406 arrraareaetLAQRLAEKTEAVerlerarRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRE 1485
Cdd:pfam15921 553 -----------LKLQMAEKDKVI-------EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKD 614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1486 RVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALL----SSKDDVGKNVHELERARRVAEQAASDLRTQV 1561
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLnevkTSRNELNSLSEDYEVLKRNFRNKSEEMETTT 694
|
730 740 750
....*....|....*....|....*....|.
gi 564328072 1562 TELEDELTAAEDaklRLEVTVQALKAQHERD 1592
Cdd:pfam15921 695 NKLKMQLKSAQS---ELEQTRNTLKSMEGSD 722
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
858-1318 |
2.98e-09 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 62.55 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 858 LQVTRQDEVLQARAQELQKVQELQQQSARE--------VGELQGRVAQLEEErARLAEQLRAEAELCSEAEETrarLAAR 929
Cdd:pfam12128 408 RQLAVAEDDLQALESELREQLEAGKLEFNEeeyrlksrLGELKLRLNQATAT-PELLLQLENFDERIERAREE---QEAA 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 930 KQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELET-------------HLEAEEGARQKLQLEKVTTEAKMKKF 996
Cdd:pfam12128 484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpqagtllHFLRKEAPDWEQSIGKVISPELLHRT 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 997 EEDLLLLEDQNS--------KLSKER----------RLLEERLAEFSSQAAEEEEKVKSLNK----LRVKYEATIADMED 1054
Cdd:pfam12128 564 DLDPEVWDGSVGgelnlygvKLDLKRidvpewaaseEELRERLDKAEEALQSAREKQAAAEEqlvqANGELEKASREETF 643
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1055 RLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEggARAQLLKSLREAQAGLA 1134
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEE--QKEQKREARTEKQAYWQ 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1135 EAQEDLEAErVARAKAEKQRRDLG--EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEE------EARTHEVA 1206
Cdd:pfam12128 722 VVEGALDAQ-LALLKAAIAARRSGakAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERiavrrqEVLRYFDW 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1207 MQELRQRHSQALVELTEQLEQARRgksvweKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSS---- 1282
Cdd:pfam12128 801 YQETWLQRRPRLATQLSNIERAIS------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSklat 874
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564328072 1283 -----DSERARAEAAEKLqRAQVELESVSTALSEAESKAIR 1318
Cdd:pfam12128 875 lkedaNSEQAQGSIGERL-AQLEDLKLKRDYLSESVKKYVE 914
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1149-1748 |
3.68e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1149 KAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKK---TLEEEARTHEVAMQELRQRHsQALVELTEQL 1225
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLReinEISSELPELREELEKLEKEV-KELEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1226 EQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESqLQEVQGRSSDSERARAEAAEKLQRAQVELESV 1305
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1306 STALSEAEskaiRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEaEAAGLREQMEEevVARERAGRELQTTQAQ 1385
Cdd:PRK03918 320 EEEINGIE----ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE-EAKAKKEELER--LKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1386 LSEWRRRQEEeaavleaGEEARRRAAREAETLAQRLAEKTEAVER-------------------LERARRRLQQELDDAT 1446
Cdd:PRK03918 393 LEELEKAKEE-------IEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelteehRKELLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1447 VDLGQQKQLLSTLEKKQRKFDQLLAEEK--------AAVLRAVEDR-ERVEAEGREREARALSLTRALEEEQEAREELER 1517
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESeliklkelAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1518 QN----RALRAELEALLSSKDDVGKNVHELER-ARRVAEQAASDLRTQVTELE---DELTAAEDAKLRLEVTVQALKAQH 1589
Cdd:PRK03918 546 KEleklEELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEpfyNEYLELKDAEKELEREEKELKKLE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1590 ERDLQGRDDAGEE--RRRQLAKQLRDAEVERDEERKQRAlamaarkklELELEELKAQTSAAGQGKEEAVKQLKKMQAQM 1667
Cdd:PRK03918 626 EELDKAFEELAETekRLEELRKELEELEKKYSEEEYEEL---------REEYLELSRELAGLRAELEELEKRREEIKKTL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1668 KELWREVEETRSSREEMFTLSRESEkRLKGLEAEVLRLQEELAasDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQL 1747
Cdd:PRK03918 697 EKLKEELEEREKAKKELEKLEKALE-RVEELREKVKKYKALLK--ERALSKVGEIASEIFEELTEGKYSGVRVKAEENKV 773
|
.
gi 564328072 1748 E 1748
Cdd:PRK03918 774 K 774
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
899-1320 |
3.78e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 899 EEERARLAEQ-LRAEAELcseaEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQhiqelethleAEEG 977
Cdd:PRK04863 278 ANERRVHLEEaLELRREL----YTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNL----------VQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 978 ARQKLQLEkvtteakmkKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLK 1057
Cdd:PRK04863 344 LRQQEKIE---------RYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1058 KEEKGRQELEKLKRRLDGES------SELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEggarAQLLKSlreaqa 1131
Cdd:PRK04863 415 QYQQAVQALERAKQLCGLPDltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQA----YQLVRK------ 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1132 gLAEAQEDLEAERVARAKAEKQR--RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEArthevAMQE 1209
Cdd:PRK04863 485 -IAGEVSRSEAWDVARELLRRLReqRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDED-----ELEQ 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1210 LRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKtelsSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARA 1289
Cdd:PRK04863 559 LQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA----ARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQ 634
|
410 420 430
....*....|....*....|....*....|.
gi 564328072 1290 EAAEKLQRAQVELESVSTALSEAESKAIRLS 1320
Cdd:PRK04863 635 QLLERERELTVERDELAARKQALDEEIERLS 665
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
965-1335 |
9.95e-09 |
|
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: 60.36 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 965 IQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVK 1044
Cdd:COG5185 161 IKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1045 YEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRK--EEELQSALVRAEEEG------ 1116
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKiaEYTKSIDIKKATESLeeqlaa 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1117 -GARAQLLKSLREAQAGLAEAQEDLE------AERVARAKAEKQRRDLGEELEalrgELEDTLDSTNAQQE-LRSKREQE 1188
Cdd:COG5185 321 aEAEQELEESKRETETGIQNLTAEIEqgqeslTENLEAIKEEIENIVGEVELS----KSSEELDSFKDTIEsTKESLDEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1189 VTELKKTLEEEARTHEVAMQElrqrHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKR- 1267
Cdd:COG5185 397 PQNQRGYAQEILATLEDTLKA----ADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEi 472
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1268 -RRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQE 1335
Cdd:COG5185 473 nRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILAL 541
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1103-1503 |
1.45e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1103 EELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRRDLGEELEALRGELEDT---LDSTNA 1177
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELperLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1178 QQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQ 1257
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1258 TSRQEGEQKRR----------------------RLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESK 1315
Cdd:COG4717 234 NELEAAALEERlkearlllliaaallallglggSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1316 AIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRR--- 1392
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAleq 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1393 -QEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDatvdlgQQKQLLSTLEKKQRKFDQLLA 1471
Cdd:COG4717 394 aEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEE------ELEELREELAELEAELEQLEE 467
|
410 420 430
....*....|....*....|....*....|..
gi 564328072 1472 EEKAAVLRAVEDRERVEAEGREREARALSLTR 1503
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAALKLAL 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1021-1230 |
1.64e-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: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1021 LAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQrAEELLIQLGR 1100
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1101 KEEELQSALVRAEEEGGARAQLL--KSLREAQAGLAEAQEDLEAERVAR--AKAEKQRRDLGEELEALRGELEDTLDSTN 1176
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALyrLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1177 AQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARR 1230
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1018-1557 |
2.90e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1018 EERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELliq 1097
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEI--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1098 lgrkeEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaERVARAKAEKQRRDLGEELEALRGE---------- 1167
Cdd:PRK03918 241 -----EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEyldelreiek 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1168 ----LEDTLDSTNAQQELRSKREQEVTELKKTLEE----------------EARTHEVAMQELRQRHSQALVE-LTEQLE 1226
Cdd:PRK03918 315 rlsrLEEEINGIEERIKELEEKEERLEELKKKLKElekrleeleerhelyeEAKAKKEELERLKKRLTGLTPEkLEKELE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1227 QARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLesqlqEVQGRSSDSEraraEAAEKLQRAQVELESVS 1306
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKC-----PVCGRELTEE----HRKELLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1307 TALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLalgsrVRALEAEAAGLR-EQMEEEVVARERAGRELQTTQAQ 1385
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQ-----LKELEEKLKKYNlEELEKKAEEYEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1386 LSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRK 1465
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1466 FDQLLAE-EKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELE 1544
Cdd:PRK03918 621 LKKLEEElDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
570
....*....|...
gi 564328072 1545 RARRVAEQAASDL 1557
Cdd:PRK03918 701 EELEEREKAKKEL 713
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
889-1292 |
2.93e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 889 GELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTelearvgeeeecSRQLQSEKKRLQQHIQEL 968
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQT------------ALRQQEKIERYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 969 ETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFsSQAAEEEEKVKSLNKLRvkyEAT 1048
Cdd:PRK04863 361 EERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQY-QQAVQALERAKQLCGLP---DLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1049 IADMEDRLK----KEEKGRQELEKLKRRLDgesseLQEQMMEQKQRAEELLIQLG----RKE--EELQSALVRAEEEgGA 1118
Cdd:PRK04863 437 ADNAEDWLEefqaKEQEATEELLSLEQKLS-----VAQAAHSQFEQAYQLVRKIAgevsRSEawDVARELLRRLREQ-RH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1119 RAQLLKSLReaqAGLAEAQEDLEAERVA-RAKAEKQRR-----DLGEELEALRGELEDTLDSTNAQQElrskreqEVTEL 1192
Cdd:PRK04863 511 LAEQLQQLR---MRLSELEQRLRQQQRAeRLLAEFCKRlgknlDDEDELEQLQEELEARLESLSESVS-------EARER 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1193 KKTLEEEARTHEVAMQELRQRhSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLES 1272
Cdd:PRK04863 581 RMALRQQLEQLQARIQRLAAR-APAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
410 420
....*....|....*....|.
gi 564328072 1273 QLQEVQGRS-SDSERARAEAA 1292
Cdd:PRK04863 660 EIERLSQPGgSEDPRLNALAE 680
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
853-1082 |
5.08e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.61 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 853 KVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEaelcSEAEETRARLAARKQE 932
Cdd:PTZ00121 1596 EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA----EEENKIKAAEEAKKAE 1671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 933 LELVVTElEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEgARQKLQLEKVTTEAKMKKfeEDLLLLEDQNSKLSK 1012
Cdd:PTZ00121 1672 EDKKKAE-EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE-KKKAEELKKAEEENKIKA--EEAKKEAEEDKKKAE 1747
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1013 ERRLLEERLAEFSSQAAEEEEKVKSLNKLRvkyEATIADMEDrlKKEEKGRQELEKLKRRLDGESSELQE 1082
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELD--EEDEKRRMEVDKKIKDIFDNFANIIE 1812
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
863-1590 |
6.91e-08 |
|
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: 58.13 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEA 942
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 943 RVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKfeedlllledqnSKLSKERRLLEERLA 1022
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI------------ERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1023 EFSSQaaeEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLdgesselqeqmmeqkQRAEELLIQLGRKE 1102
Cdd:TIGR00606 416 DLQSK---ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL---------------QQLEGSSDRILELD 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1103 EElqsalvraeeeggaraqllksLREAQAGLAEAQEDLEAErvarakaekqrrDLGEELEALRGELEDTLDSTNAQQELR 1182
Cdd:TIGR00606 478 QE---------------------LRKAERELSKAEKNSLTE------------TLKKEVKSLQNEKADLDRKLRKLDQEM 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1183 SKREQEVTELKKTlEEEARTHEVAMQELRQRHSQALVELTEQLEQArRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQE 1262
Cdd:TIGR00606 525 EQLNHHTTTRTQM-EMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF-PNKKQLEDWLHSKSKEINQTRDRLAKLNKELAS 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1263 GEQKRRRLESQLQEVQGRSSDSERARAEAAEKlQRAQVELESvstaLSEAESKAIRLSKELSSAESQLHDTQELLQEETR 1342
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLER----LKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1343 AKLALGSRVRALEAEAAGLREQMEEEVVArerAGRELQTTQAQLSEWRRRQEE-------EAAVLEAGEEARRRAAREAE 1415
Cdd:TIGR00606 678 SCCPVCQRVFQTEAELQEFISDLQSKLRL---APDKLKSTESELKKKEKRRDEmlglapgRQSIIDLKEKEIPELRNKLQ 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1416 TLAQRLAEKTEAVERLERARRRLQQELDDATV---DLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGR 1492
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQETLLGTIMPEEESAKVcltDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEK 834
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1493 EREARalSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNvheLERARRVAEQAAsDLRTQVTELEDELTAAE 1572
Cdd:TIGR00606 835 QHELD--TVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN---LQRRQQFEEQLV-ELSTEVQSLIREIKDAK 908
|
730
....*....|....*...
gi 564328072 1573 DAKLRLEVTVQALKAQHE 1590
Cdd:TIGR00606 909 EQDSPLETFLEKDQQEKE 926
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1523-1940 |
1.03e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1523 RAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHErDLQGRDDAGEE 1602
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE-ELEDRDEELRD 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1603 RRRQLAKQLRDAEVERDEERKqRALAMAARKKLELEleelkaQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSRE 1682
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLRE-DADDLEERAEELRE------EAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1683 EMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNL----------SKAATLEEKRQ----LE 1748
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgqpvegsPHVETIEEDRErveeLE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1749 GRLGQLEEELEEEQNNSELLKDhYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGE-----EDAGARA 1823
Cdd:PRK02224 482 AELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAEleaeaEEKREAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1824 RQKML--------IAALESKLAQAEEQLEQESRERILSGKL--VRRAEKRLKEVVLQVDEerrVADQLRDQLEKSNLRLK 1893
Cdd:PRK02224 561 AEAEEeaeeareeVAELNSKLAELKERIESLERIRTLLAAIadAEDEIERLREKREALAE---LNDERRERLAEKRERKR 637
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 564328072 1894 QLKRQLEEAEEEAsrAQAGRRRLQRELEDVTESAESMNREVTTLRNR 1940
Cdd:PRK02224 638 ELEAEFDEARIEE--AREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
864-1228 |
1.24e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 864 DEVLQARAQ------ELQKVQELQQQSAREVGELQGRVAQLEEE----RARLAEQLRAEA-----ELCSEA-EETRARLA 927
Cdd:PRK04863 286 EEALELRRElytsrrQLAAEQYRLVEMARELAELNEAESDLEQDyqaaSDHLNLVQTALRqqekiERYQADlEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 928 ARKQELELV---VTELEARVGEEEECSRQLQSEKKRLQQHIQELETH-------LEAEEGARQKLQLEKVTTEakmkKFE 997
Cdd:PRK04863 366 EQNEVVEEAdeqQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRaiqyqqaVQALERAKQLCGLPDLTAD----NAE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 998 EDLLLLEDQNSKLSKERRLLEERLAeFSSQAAEEEEKVKSLNKlrvkyeaTIADMEDRLKKEEKGRQELEKLK--RRLDG 1075
Cdd:PRK04863 442 DWLEEFQAKEQEATEELLSLEQKLS-VAQAAHSQFEQAYQLVR-------KIAGEVSRSEAWDVARELLRRLReqRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1076 ESSELQ------EQMMEQKQRAEELLIQLGRK-------EEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA 1142
Cdd:PRK04863 514 QLQQLRmrlselEQRLRQQQRAERLLAEFCKRlgknlddEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1143 ERVARAKAEKQRRDLGEELEALRGELEDTLDSTnaqqelrskreQEVTELKKTLEEEARTHEVAMQELRQRhSQALVELT 1222
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARLREQSGEEFEDS-----------QDVTEYMQQLLERERELTVERDELAAR-KQALDEEI 661
|
....*.
gi 564328072 1223 EQLEQA 1228
Cdd:PRK04863 662 ERLSQP 667
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1086-1326 |
1.45e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1086 EQKQRAEELLIQLGRKEEELQSALVRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1165
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1166 GELEDTLDSTnAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQarrgksvwekTRLSLEAE 1245
Cdd:COG4942 97 AELEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA----------DLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1246 VSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSS 1325
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
.
gi 564328072 1326 A 1326
Cdd:COG4942 246 A 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
859-1039 |
1.55e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEE----RARLAEQLRAEAELCSEAE-------ETRARLA 927
Cdd:COG4942 56 QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEleaqKEELAELLRALYRLGRQPPlalllspEDFLDAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 928 ARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQN 1007
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
170 180 190
....*....|....*....|....*....|..
gi 564328072 1008 SKLSKERRLLEERLAEFSSQAAEEEEKVKSLN 1039
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1173-1394 |
1.66e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.56 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1173 DSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSqaLVELTEQLEQarrgksvwektrlsLEAEVSELKTE 1252
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG--LVDLSEEAKL--------------LLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1253 LSSLQTSRQEGEQKRRRLESQLQEVQGRSSD--SERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQl 1330
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPEllQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ- 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1331 hdtqeLLQEETRAKLALGSRVRALEAEAAGLREQMEEevvARERAgRELQTTQAQLSEWRRRQE 1394
Cdd:COG3206 307 -----LQQEAQRILASLEAELEALQAREASLQAQLAQ---LEARL-AELPELEAELRRLEREVE 361
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
919-1277 |
1.71e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 56.06 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 919 AEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLeaeegarQKLQLEKVTTEAKMKKFEE 998
Cdd:pfam07888 29 AELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV-------AELKEELRQSREKHEELEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 999 DLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGE-- 1076
Cdd:pfam07888 102 KYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKlq 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1077 ---------SSELQEQMMEQKQRAEELLiQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVAR 1147
Cdd:pfam07888 182 qteeelrslSKEFQELRNSLAQRDTQVL-QLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1148 AKAEKQRRDLGEELEALRGELEDT----LDSTNAQQELRSKREQEVTELKKTLE----------EEARTHEVAMQELRQR 1213
Cdd:pfam07888 261 SSMAAQRDRTQAELHQARLQAAQLtlqlADASLALREGRARWAQERETLQQSAEadkdrieklsAELQRLEERLQEERME 340
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1214 HSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEV 1277
Cdd:pfam07888 341 REKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETV 404
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1016-1305 |
2.65e-07 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 55.80 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1016 LLEERLAEFSSQAAEEEEkvksLNKLRVKYEATIAdmEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELL 1095
Cdd:pfam05667 208 LLERNAAELAAAQEWEEE----WNSQGLASRLTPE--EYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAELL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1096 IQLGRKEEELQS-----------ALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEA--ERVARAKAEKQRrdLGEELE 1162
Cdd:pfam05667 282 SSFSGSSTTDTGltkgsrfthteKLQFTNEAPAATSSPPTKVETEEELQQQREEELEElqEQLEDLESSIQE--LEKEIK 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1163 ALRGELEDTLDSTNAQQELRSKREQEVTELKKTLE--EEARTHEVAMQELRQRHSQALVELTEQleqarrgksvWEKTRL 1240
Cdd:pfam05667 360 KLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDllPDAEENIAKLQALVDASAQRLVELAGQ----------WEKHRV 429
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1241 SLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVqgrssdSERARAeAAEKLQRAQVELESV 1305
Cdd:pfam05667 430 PLIEEYRALKEAKSNKEDESQRKLEEIKELREKIKEV------AEEAKQ-KEELYKQLVAEYERL 487
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
927-1326 |
2.86e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 55.42 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 927 AARKQELE---LVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE-THLEAEEgarQKLQLEKVTTEAKMKKfeedlll 1002
Cdd:pfam05701 28 AHRIQTVErrkLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELEsTKRLIEE---LKLNLERAQTEEAQAK------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1003 ledQNSKLSKER-RLLEERLAEFSSQAAEEEEKVkslnkLRVKYEATIADMedRLKKEEKG--RQELEKLKRRLDGESSE 1079
Cdd:pfam05701 98 ---QDSELAKLRvEEMEQGIADEASVAAKAQLEV-----AKARHAAAVAEL--KSVKEELEslRKEYASLVSERDIAIKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1080 LQEQMMEQKQ---RAEELLIQLGRKEEELQSAL---VRAEEE--GGARA------QLLKSLREAQAGLAEAQEDLEAERV 1145
Cdd:pfam05701 168 AEEAVSASKEiekTVEELTIELIATKESLESAHaahLEAEEHriGAALAreqdklNWEKELKQAEEELQRLNQQLLSAKD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1146 ARAKAEKQRR---DLGEELEA---------LRGELEDTLDSTNAQQELRSKREqEVTELKKTLE---EEARTHEVAMQEL 1210
Cdd:pfam05701 248 LKSKLETASAlllDLKAELAAymesklkeeADGEGNEKKTSTSIQAALASAKK-ELEEVKANIEkakDEVNCLRVAAASL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1211 R---QRHSQALVELteqleqaRRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVqGRSSDSERA 1287
Cdd:pfam05701 327 RselEKEKAELASL-------RQREGMASIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQA-AQEAEEAKS 398
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 564328072 1288 RAEAA-EKLQRAQVELESVSTALSEAESKAIRLSKELSSA 1326
Cdd:pfam05701 399 LAQAArEELRKAKEEAEQAKAAASTVESRLEAVLKEIEAA 438
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1177-1627 |
3.05e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1177 AQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELK------ 1250
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEeleerl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1251 TELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERAR-AEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQ 1329
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1330 LHDTQELLQ-EETRAKLALGSRVRALEAEAAGLreqmeeevVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARR 1408
Cdd:COG4717 236 LEAAALEERlKEARLLLLIAAALLALLGLGGSL--------LSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1409 RAAREAETLAQRlaEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAvedreRVE 1488
Cdd:COG4717 308 QALPALEELEEE--ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA-----EAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1489 AEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLS--SKDDVGKNVHELERARRVAEQAASDLRTQVTELED 1566
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1567 ELTAAEDaklrlEVTVQALKAQHERDLQGRDDAGEERRR-QLAKQLRDAEVERDEERKQRAL 1627
Cdd:COG4717 461 ELEQLEE-----DGELAELLQELEELKAELRELAEEWAAlKLALELLEEAREEYREERLPPV 517
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1148-1611 |
3.15e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 55.73 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1148 AKAEKQRRDLGEELEALRGELEDTLDSTNAQQELR---SKREQEVTELKKTLEEE---ARTHEVAMQE-LRQ-----RHS 1215
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDyqaASDHLNLVQTaLRQqekieRYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1216 QALVELTEQLEQArrgksvwektrlsleAEVSELKTE-LSSLQTSRQEGEQKRRRLESQLQEVQgRSSDSERARA----E 1290
Cdd:PRK04863 355 ADLEELEERLEEQ---------------NEVVEEADEqQEENEARAEAAEEEVDELKSQLADYQ-QALDVQQTRAiqyqQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1291 AAEKLQRAQ-------VELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGlre 1363
Cdd:PRK04863 419 AVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAW--- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1364 qmeEEVVARERAGRELQTTQAQLSEWRRRQEEeaavleageearrraareaetLAQRLAEKTEAverlerarrrlQQELD 1443
Cdd:PRK04863 496 ---DVARELLRRLREQRHLAEQLQQLRMRLSE---------------------LEQRLRQQQRA-----------ERLLA 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1444 DATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRaleeeqeareeLERQNRALR 1523
Cdd:PRK04863 541 EFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAA-----------RAPAWLAAQ 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1524 AELEALLSSKDDvgknvhELERARRVAEqaasdLRTQVTELEDELTAAEDaklRLEVTVQALKAQHERdLQGRDDAGEER 1603
Cdd:PRK04863 610 DALARLREQSGE------EFEDSQDVTE-----YMQQLLERERELTVERD---ELAARKQALDEEIER-LSQPGGSEDPR 674
|
....*...
gi 564328072 1604 RRQLAKQL 1611
Cdd:PRK04863 675 LNALAERF 682
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
998-1749 |
3.60e-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: 55.75 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 998 EDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEeeKVKSLNKLRVKYEATIADMEDRLKK----EEKGRQELEKLKRRL 1073
Cdd:TIGR00618 179 TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC--MPDTYHERKQVLEKELKHLREALQQtqqsHAYLTQKREAQEEQL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1074 DGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQ 1153
Cdd:TIGR00618 257 KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1154 RRDLGEELEALRgeledtldsTNAQQELRSKREQEVTELKKTLEEEARTHEvamqelrqrhsQALVELTEQLEQARRGKS 1233
Cdd:TIGR00618 337 QSSIEEQRRLLQ---------TLHSQEIHIRDAHEVATSIREISCQQHTLT-----------QHIHTLQQQKTTLTQKLQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1234 VWEKTRLSLEAEVSELKTELSSlqtsrqegeqkRRRLESQLqevqgrssdserARAEAAEKLQRAQVEL-----ESVSTA 1308
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSA-----------FRDLQGQL------------AHAKKQQELQQRYAELcaaaiTCTAQC 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1309 LSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGrELQTTQAQLse 1388
Cdd:TIGR00618 454 EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDID-NPGPLTRRM-- 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1389 wrRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQ 1468
Cdd:TIGR00618 531 --QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1469 LLAEEKAAVLR----AVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSkddvgKNVHELE 1544
Cdd:TIGR00618 609 MLACEQHALLRklqpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLA-----SRQLALQ 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1545 RARRVAEQAASDLRT--QVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAgeerrrqLAKQLRDAEVERDEER 1622
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA-------LNQSLKELMHQARTVL 756
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1623 KQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSREsekRLKGLEAEV 1702
Cdd:TIGR00618 757 KARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCE---TLVQEEEQF 833
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 564328072 1703 LRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEG 1749
Cdd:TIGR00618 834 LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1287-1500 |
4.00e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1287 ARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQE------ETRAKLA-LGSRVRALEAEAA 1359
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaALEAELAeLEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1360 GLREQMEEEVVARERAGR----ELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERAR 1435
Cdd:COG4942 101 AQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1436 RRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALS 1500
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
954-1347 |
4.19e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 954 LQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEE---RLAEFSSQAAE 1030
Cdd:pfam05483 97 IEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKEtcaRSAEKTKKYEY 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1031 EEEKVK---------------SLNKLRVKYEATIADMEDRLKKEEKGRQELEKlkrrldgessELQEQMMEQKQRAEELL 1095
Cdd:pfam05483 177 EREETRqvymdlnnniekmilAFEELRVQAENARLEMHFKLKEDHEKIQHLEE----------EYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1096 IQLGRKE----------EELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLeaeRVARAKAEKQRRDLGEELEALR 1165
Cdd:pfam05483 247 IQITEKEnkmkdltfllEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDI---KMSLQRSMSTQKALEEDLQIAT 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1166 GELEDTLDSTNAQQELRSKREQE----VTELKKT---LEEEARTHevamQELRQRHSQALVELTEQLEQARRGKSVWEKT 1238
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAhsfvVTEFEATtcsLEELLRTE----QQRLEKNEDQLKIITMELQKKSSELEEMTKF 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1239 RLSLEAEVSELKTELSSLQTSRQEGEQKRR---RLESQLQE----VQGRSSDSERARAEAAEKLQRAQVELESVSTALSE 1311
Cdd:pfam05483 400 KNNKEVELEELKKILAEDEKLLDEKKQFEKiaeELKGKEQEliflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE 479
|
410 420 430
....*....|....*....|....*....|....*.
gi 564328072 1312 AESKAIRLSKELSSAESQLHDTQELLQEETRAKLAL 1347
Cdd:pfam05483 480 LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
853-1397 |
5.29e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 853 KVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELqgRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQE 932
Cdd:COG4913 250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 933 LELvvtELEARVGEEEEcsrQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKK----FEEDLLLLEDQNS 1008
Cdd:COG4913 328 LEA---QIRGNGGDRLE---QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAlraeAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1009 KLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLK---------------------KEEKGRQELE 1067
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAealgldeaelpfvgelievrpEEERWRGAIE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1068 ---------------------------KLKRRLDGE--SSELQEQMMEQKQR---AEELLIQLGRKEEELQSAL------ 1109
Cdd:COG4913 482 rvlggfaltllvppehyaaalrwvnrlHLRGRLVYErvRTGLPDPERPRLDPdslAGKLDFKPHPFRAWLEAELgrrfdy 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1110 --VRAEEE-----------------------------------GGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEK 1152
Cdd:COG4913 562 vcVDSPEElrrhpraitragqvkgngtrhekddrrrirsryvlGFDNRAKLAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1153 QRRDLGEELEALRGELEDTLDSTNAQQELRSKrEQEVTELKKTleeearthevamqelrqrhSQALVELTEQLEQArrgk 1232
Cdd:COG4913 642 ALQERREALQRLAEYSWDEIDVASAEREIAEL-EAELERLDAS-------------------SDDLAALEEQLEEL---- 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1233 svwEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAaeklQRAQVELESVSTALSEA 1312
Cdd:COG4913 698 ---EAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE----RFAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1313 ESKAIR-LSKELSSAESQLHDTQELLQEETRAKLA-LGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQ-----AQ 1385
Cdd:COG4913 771 LEERIDaLRARLNRAEEELERAMRAFNREWPAETAdLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENsiefvAD 850
|
650
....*....|..
gi 564328072 1386 LSEWRRRQEEEA 1397
Cdd:COG4913 851 LLSKLRRAIREI 862
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1027-1303 |
5.71e-07 |
|
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: 54.74 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1027 QAAEEEEKVKSlNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSelQEQMMEQKQRAEELLIQLGRKEEELQ 1106
Cdd:pfam17380 288 QQQEKFEKMEQ-ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMERERELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1107 salVRAEE---EGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGE---ELEALRGELEDTldstnAQQE 1180
Cdd:pfam17380 365 ---IRQEEiamEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-----RQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1181 LRSKREQEVTELKKTLEEEARTHEvAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSslqtsr 1260
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQ-QVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI------ 509
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 564328072 1261 qEGEQKRRRLESQLQEVQGRSSDSERARaeAAEKLQRAQVELE 1303
Cdd:pfam17380 510 -EEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEME 549
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1252-1479 |
7.90e-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: 53.61 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1252 ELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLH 1331
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1332 DTQELLQEETRAKLALGSR------VRALEAEAAGLREQMEEEVV-ARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGE 1404
Cdd:COG4942 101 AQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLApARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1405 EARRRAAReaeTLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLR 1479
Cdd:COG4942 181 AELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
874-1230 |
8.24e-07 |
|
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: 54.59 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 874 LQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQ 953
Cdd:pfam02463 645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 954 --LQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERRLLEERLAEFSSQAAEE 1031
Cdd:pfam02463 725 drVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEE--REKTEKLKVEEEKEEKLKAQEEE 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1032 EEKVKSLNKLRVKYEATIADMEDRLKK---EEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSA 1108
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKikeEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1109 LVRAEEEG----GARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRS 1183
Cdd:pfam02463 883 KLKDELESkeekEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKyEEEPEELLLEEADEKEKEENNKEEEEERN 962
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 564328072 1184 KREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARR 1230
Cdd:pfam02463 963 KRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
861-1119 |
1.07e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 861 TRQDEVLQARAQELQkvqelqqqsaREVGELQGRVAQLEEERARLAEQLRAEAELCS---------EAEETRARLAARKQ 931
Cdd:COG4913 609 RAKLAALEAELAELE----------EELAEAEERLEALEAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 932 ELEL---VVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQklQLEKVTTEAKMKKFEEDLLLLEDQNS 1008
Cdd:COG4913 679 RLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD--ELQDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1009 KLSKE------RRLLEERLAEFSSQAAEEEEK-VKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRrldgesselq 1081
Cdd:COG4913 757 AALGDaverelRENLEERIDALRARLNRAEEElERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE---------- 826
|
250 260 270
....*....|....*....|....*....|....*....
gi 564328072 1082 EQMMEQKQRAEELLIQL-GRKEEELQSALVRAEEEGGAR 1119
Cdd:COG4913 827 DGLPEYEERFKELLNENsIEFVADLLSKLRRAIREIKER 865
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
865-1388 |
1.13e-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: 54.19 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 865 EVLQARA-------QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVV 937
Cdd:COG3096 406 DVQQTRAiqyqqavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 938 TELEArvGEEEECSRQL---QSEKKRLQQHIQELETHL-EAEEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQNSKLs 1011
Cdd:COG3096 486 GEVER--SQAWQTARELlrrYRSQQALAQRLQQLRAQLaELEQRLRQQQNAERLLEEfcQRIGQQLDAAEELEELLAEL- 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1012 kerrllEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGE---SSELQEQMMEQK 1088
Cdd:COG3096 563 ------EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEAladSQEVTAAMQQLL 636
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1089 QRAEELLI---QLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAG--LAEAQEDLEAE-------RVARAKAEKQRRD 1156
Cdd:COG3096 637 EREREATVerdELAARKQALESQIERLSQPGGAEDPRLLALAERLGGvlLSEIYDDVTLEdapyfsaLYGPARHAIVVPD 716
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1157 LGEELEALRGeLEDTL--------------DSTNAQQEL-------------------------RSKREQEVTELKKTLE 1197
Cdd:COG3096 717 LSAVKEQLAG-LEDCPedlyliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfpevplfgRAAREKRLEELRAERD 795
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1198 EEARTHevAMQELRQRHSQALVELTEQLeqARRGKSVW-----EKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLES 1272
Cdd:COG3096 796 ELAEQY--AKASFDVQKLQRLHQAFSQF--VGGHLAVAfapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKE 871
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1273 QLQEVQGRSS-------DSERARAEAAE----KLQRAQVELESVSTALSEAESKAIRLSK------ELSSAESQLHDTQE 1335
Cdd:COG3096 872 QLQLLNKLLPqanlladETLADRLEELReeldAAQEAQAFIQQHGKALAQLEPLVAVLQSdpeqfeQLQADYLQAKEQQR 951
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1336 LLQEETRAKLALGSRVRALE-AEAAG-----------LREQMEEEVVARERAGRELQTTQAQLSE 1388
Cdd:COG3096 952 RLKQQIFALSEVVQRRPHFSyEDAVGllgensdlnekLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1347-1959 |
1.24e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.89 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1347 LGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEA---AVLEAGEEARRRAAREAETLAQRLAE 1423
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtleAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1424 KTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARAlsltr 1503
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERA----- 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1504 aleeeqearEELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQ 1583
Cdd:PRK02224 359 ---------EELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1584 ALKAqherDLQGRDDAGEERRRQLA--------KQLRDAE-VERDEERKQRALAMAARKKLELELEELKAQtsaagqgKE 1654
Cdd:PRK02224 430 ELEA----TLRTARERVEEAEALLEagkcpecgQPVEGSPhVETIEEDRERVEELEAELEDLEEEVEEVEE-------RL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1655 EAVKQLKKMQAQMKELwrevEETRSSREEMFTLSRES--EKRLKgleAEVLRLQ-EELAASDRARRQAQQDRDEMAEEVA 1731
Cdd:PRK02224 499 ERAEDLVEAEDRIERL----EERREDLEELIAERRETieEKRER---AEELRERaAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1732 sgnlskaatlEEKRQLEGRLGQLEEELEEEQNNSELLKDhyrklvlqVETLTTELSAERS-FSAKAESGRQQLERqIQEL 1810
Cdd:PRK02224 572 ----------EEVAELNSKLAELKERIESLERIRTLLAA--------IADAEDEIERLREkREALAELNDERRER-LAEK 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1811 RAR---LGEEDAGARarqkmlIAALESKLAQAEEQLEQesreriLSGKLVRRAEKRlkevvlqvdeerrvaDQLRDQLEK 1887
Cdd:PRK02224 633 RERkreLEAEFDEAR------IEEAREDKERAEEYLEQ------VEEKLDELREER---------------DDLQAEIGA 685
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1888 SNLRLKQLKRQLEEAEEEASRAQAgrrrlqreLEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVFRL 1959
Cdd:PRK02224 686 VENELEELEELRERREALENRVEA--------LEALYDEAEELESMYGDLRAELRQRNVETLERMLNETFDL 749
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
860-1399 |
1.41e-06 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 53.68 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 860 VTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAElcSEAEETRARLAArkqELELVVTE 939
Cdd:NF041483 436 VELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAEELLTKAK--ADADELRSTATA---ESERVRTE 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 940 LEARVG----EEEECSRQLQSEKKRLQQHIQEL--ETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLE-DQNSKLSK 1012
Cdd:NF041483 511 AIERATtlrrQAEETLERTRAEAERLRAEAEEQaeEVRAAAERAARELREETERAIAARQAEAAEELTRLHtEAEERLTA 590
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1013 ERRLLEERLAE---FSSQAAEEEEKVKSLNKLRVKYEATIADME-DRLKKE-----EKGRQELEKLKRRLDGESSELQEQ 1083
Cdd:NF041483 591 AEEALADARAEaerIRREAAEETERLRTEAAERIRTLQAQAEQEaERLRTEaaadaSAARAEGENVAVRLRSEAAAEAER 670
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1084 MMEQKQRA-----EELLIQLGRKEEELQSALVRAEEEGGARAqllkslREAQAGLAEAQEDLEAE--------------- 1143
Cdd:NF041483 671 LKSEAQESadrvrAEAAAAAERVGTEAAEALAAAQEEAARRR------REAEETLGSARAEADQErerareqseellasa 744
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1144 --RVARAKAEKQRrdLGEELEALRGELEDTLDSTNAQQE-----LRSKREQEVTELKKTLEEEA-RTHEVAMQELRQRHS 1215
Cdd:NF041483 745 rkRVEEAQAEAQR--LVEEADRRATELVSAAEQTAQQVRdsvagLQEQAEEEIAGLRSAAEHAAeRTRTEAQEEADRVRS 822
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1216 QALVELTEQLEQARRGKSVW----EKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLqeVQGRSSDSERARAEA 1291
Cdd:NF041483 823 DAYAERERASEDANRLRREAqeetEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDT--LASAEQDAARTRADA 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1292 AEKLQRAQVELESVSTAL-SEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLAlgSRVRALEAEAAGLREQMEEEvv 1370
Cdd:NF041483 901 REDANRIRSDAAAQADRLiGEATSEAERLTAEARAEAERLRDEARAEAERVRADAA--AQAEQLIAEATGEAERLRAE-- 976
|
570 580
....*....|....*....|....*....
gi 564328072 1371 ARERAGRELQTTQAQLSEWRRRQEEEAAV 1399
Cdd:NF041483 977 AAETVGSAQQHAERIRTEAERVKAEAAAE 1005
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
860-1395 |
1.59e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 53.22 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 860 VTRQDEVLQARAQELQKVQElQQQSAREVgELQGRVaQLEEERARLAEQLRAEAELCSEAEETRARLA-----------A 928
Cdd:pfam07111 61 LSQQAELISRQLQELRRLEE-EVRLLRET-SLQQKM-RLEAQAMELDALAVAEKAGQAEAEGLRAALAgaemvrknleeG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 929 RKQELELVVT----ELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLlllE 1004
Cdd:pfam07111 138 SQRELEEIQRlhqeQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEEL---E 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1005 DQNSKLSKERRLL-EERLAEFSSQAAEEEEK-----VKSLNKLRVKYEATIADMEDR---------LKKEE--------- 1060
Cdd:pfam07111 215 AQVTLVESLRKYVgEQVPPEVHSQTWELERQelldtMQHLQEDRADLQATVELLQVRvqslthmlaLQEEEltrkiqpsd 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1061 --------KGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEEL------QSALVRAEEEGGARAQLLK-S 1125
Cdd:pfam07111 295 slepefpkKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVtsqsqeQAILQRALQDKAAEVEVERmS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1126 LREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT---LDSTNAQQELRSKREQEVTELKKTLEEeART 1202
Cdd:pfam07111 375 AKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTmtrVEQAVARIPSLSNRLSYAVRKVHTIKG-LMA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1203 HEVAMQELRQRHSQ-------ALVELTEQLEQARRgksvwEKTRLSLEAEVSELKTElSSLQTSRQEGEQKRRRLESQLQ 1275
Cdd:pfam07111 454 RKVALAQLRQESCPppppappVDADLSLELEQLRE-----ERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQ 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1276 EVQgrssdseraraeaaEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQEL----LQE-----ETRAKLA 1346
Cdd:pfam07111 528 QLE--------------QELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIygqaLQEkvaevETRLREQ 593
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1347 LGSRVRALEaeaAGLREQMEEEVVARE---RAGRELQTTQaqlsEWRRRQEE 1395
Cdd:pfam07111 594 LSDTKRRLN---EARREQAKAVVSLRQiqhRATQEKERNQ----ELRRLQDE 638
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
855-1167 |
1.72e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.95 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 855 KPLLQVTRQDEVLQARAQElqKVQELQQQSAREVGELQG---RVAQLEEERA-RLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:pfam02029 27 EPSGQVTESVEPNEHNSYE--EDSELKPSGQGGLDEEEAfldRTAKREERRQkRLQEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 931 QELELV----------VTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLE----KVTTEAKMKKF 996
Cdd:pfam02029 105 ENNEEEensswekeekRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVptenFAKEEVKDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 997 EEDLLLLEDQNSKLSKERRLLEErlaefSSQAAEEEekvksLNKLRVKYEATIADMEDRLKKEEKGR------QELEKLK 1070
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEV-----KSQNGEEE-----VTKLKVTTKRRQGGLSQSQEREEEAEvfleaeQKLEELR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1071 RRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSalVRAEEEggaraqllkslreaqaglaeaQEDLEAERVARAKA 1150
Cdd:pfam02029 255 RRRQEKESEEFEKLRQKQQEAELELEELKKKREERRK--LLEEEE---------------------QRRKQEEAERKLRE 311
|
330
....*....|....*..
gi 564328072 1151 EKQRRDLGEELEALRGE 1167
Cdd:pfam02029 312 EEEKRRMKEEIERRRAE 328
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
865-1384 |
1.74e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.42 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 865 EVLQARAQEL-QKVQELQQQ--SAREVGELQGRVAQL------EEERARLAEQLRaeaELCSEAEETRArLAARKQELEL 935
Cdd:PRK04863 445 EEFQAKEQEAtEELLSLEQKlsVAQAAHSQFEQAYQLvrkiagEVSRSEAWDVAR---ELLRRLREQRH-LAEQLQQLRM 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 936 VVTELEARVGEEEECSRQLQSEKKRLQQHIQ---ELETHLEAEEGARQKLQLEKVTTEAK---MKKFEEDLLLLEDQNSK 1009
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCKRLGKNLDdedELEQLQEELEARLESLSESVSEARERrmaLRQQLEQLQARIQRLAA 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1010 LSKERRLLEERLAEFSSQAAEEEEKVKSLnklrvkyEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQ-------E 1082
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDV-------TEYMQQLLERERELTVERDELAARKQALDEEIERLSqpggsedP 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1083 QMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQL----LKSLREAQAGLAEAQEDL---------------EAE 1143
Cdd:PRK04863 674 RLNALAERFGGVLLSEIYDDVSLEDAPYFSALYGPARHAIvvpdLSDAAEQLAGLEDCPEDLyliegdpdsfddsvfSVE 753
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1144 RVARAKAEKQ-----------------RRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKTLEEEAR---TH 1203
Cdd:PRK04863 754 ELEKAVVVKIadrqwrysrfpevplfgRAAREKRIEQLRAEREEL-------AERYATLSFDVQKLQRLHQAFSRfigSH 826
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1204 ---------EVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSL------------------------------EA 1244
Cdd:PRK04863 827 lavafeadpEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrllprlnlladetladrveeireqldEA 906
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1245 EV------------SELKTELSSLQTSRQEGEQKRRR---LESQLQEVQGRS---------------SDSERARAEAAE- 1293
Cdd:PRK04863 907 EEakrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDyqqAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDl 986
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1294 ------KLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRA-LEAEAAGLREQME 1366
Cdd:PRK04863 987 neklrqRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSgAEERARARRDELH 1066
|
650
....*....|....*...
gi 564328072 1367 EEVVARERAGRELQTTQA 1384
Cdd:PRK04863 1067 ARLSANRSRRNQLEKQLT 1084
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
893-1203 |
2.46e-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: 53.03 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 893 GRVAQleEERArlaEQLRAEAElcsEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEK--KRLQQHIQELET 970
Cdd:COG3096 779 GRAAR--EKRL---EELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAelAALRQRRSELER 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 971 HLEAEEGARQKLQL------EKVTTEAKMKKFEEdLLLLEDQNSKLSKERRLLEER------LAEFSSQAAEEEEKVKSL 1038
Cdd:COG3096 851 ELAQHRAQEQQLRQqldqlkEQLQLLNKLLPQAN-LLADETLADRLEELREELDAAqeaqafIQQHGKALAQLEPLVAVL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1039 NKLRVKYEATIADMEDRLKKEEKGRQELEKLK----RR----------LDGESSELQEQMMEQKQRAEElliQLGRKEEE 1104
Cdd:COG3096 930 QSDPEQFEQLQADYLQAKEQQRRLKQQIFALSevvqRRphfsyedavgLLGENSDLNEKLRARLEQAEE---ARREAREQ 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1105 LQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERV-----ARAKAEKQRRDLGEELEALRG---ELEDTLDSTN 1176
Cdd:COG3096 1007 LRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVqadaeAEERARIRRDELHEELSQNRSrrsQLEKQLTRCE 1086
|
330 340
....*....|....*....|....*..
gi 564328072 1177 AQQELRSKREQEVTELKKTLEEEARTH 1203
Cdd:COG3096 1087 AEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
897-1385 |
3.80e-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: 51.94 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 897 QLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEE 976
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 977 gaRQKLQLEKVTTEAKMKKFEEDLLLLEDQnsKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRL 1056
Cdd:TIGR04523 180 --KEKLNIQKNIDKIKNKLLKLELLLSNLK--KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1057 -----------KKEEKGRQELEKLKRRLDGESSELQEQMME----QKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQ 1121
Cdd:TIGR04523 256 nqlkdeqnkikKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNK 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1122 LLKSLREAQAGLAEAQEDLEAERVARAK--AEKQRrdlgeELEALRGELEDTLDS----TNAQQELRSKReQEVTELKKT 1195
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRelEEKQN-----EIEKLKKENQSYKQEiknlESQINDLESKI-QNQEKLNQQ 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1196 LEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGK---SVWEKTRLSLEAEVSELKTELSSLQTS----RQEGEQKRR 1268
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdSVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1269 RLESQLQEV----------QGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAE----------- 1327
Cdd:TIGR04523 490 ELKSKEKELkklneekkelEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENlekeideknke 569
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1328 -SQLHDTQELLQEETRAKLALgsrVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQ 1385
Cdd:TIGR04523 570 iEELKQTQKSLKKKQEEKQEL---IDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
874-1393 |
3.89e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 874 LQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARlAARKQELELVVTELEARVGEEEECSRQ 953
Cdd:TIGR00606 579 LHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD-VCGSQDEESDLERLKEEIEKSSKQRAM 657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 954 LQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLL----LEDQNSKLSKERRLLEERLAEFSSQAA 1029
Cdd:TIGR00606 658 LAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQS 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1030 EEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLD---------GESSELQEQMMEQKQRAEEL------ 1094
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsakvcltdvTIMERFQMELKDVERKIAQQaaklqg 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1095 ------LIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1168
Cdd:TIGR00606 818 sdldrtVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV 897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1169 EDTLdstnaqQELRSKREQeVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARR----GKSVWEKTRLSLEA 1244
Cdd:TIGR00606 898 QSLI------REIKDAKEQ-DSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNihgyMKDIENKIQDGKDD 970
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1245 EVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQgRSSDSERARaeaaEKLQRAQVELESVSTALSEAEskairlsKELS 1324
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMR-QDIDTQKIQ----ERWLQDNLTLRKRENELKEVE-------EELK 1038
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1325 SAESQLHDTQELLQEETRAKLAlgSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQ 1393
Cdd:TIGR00606 1039 QHLKEMGQMQVLQMKQEHQKLE--ENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYRE 1105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
874-1197 |
4.39e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 874 LQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEE--CS 951
Cdd:TIGR00618 534 EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMlaCE 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 952 RQLQSEKKRLQQHIQELETHLE--AEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLE----------- 1018
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALqkmqsekeqlt 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1019 ---ERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELL 1095
Cdd:TIGR00618 694 ywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAA 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1096 IQLGRKEEELQSALVRAEEEGGARAQLLKSLR-EAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTL-- 1172
Cdd:TIGR00618 774 LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLlk 853
|
330 340
....*....|....*....|....*.
gi 564328072 1173 -DSTNAQQELRSKREQEVTELKKTLE 1197
Cdd:TIGR00618 854 yEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1225 |
4.52e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 894 RVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVgeeeecsrQLQSEKKRLQQHIQELEtHLE 973
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI--------DVASAEREIAELEAELE-RLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 974 AEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKslnklrvkyEATIADME 1053
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR---------LELRALLE 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1054 DRLkKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREaqAGL 1133
Cdd:COG4913 753 ERF-AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEE--DGL 829
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1134 AEAQEDLeaervARAKAEKQRRDLGE---ELEALRGELEDTLDSTNA-------------QQELRSKREQEVTELKKTLE 1197
Cdd:COG4913 830 PEYEERF-----KELLNENSIEFVADllsKLRRAIREIKERIDPLNDslkripfgpgrylRLEARPRPDPEVREFRQELR 904
|
330 340
....*....|....*....|....*...
gi 564328072 1198 EEARTHEVAMQELRQRHSQALVELTEQL 1225
Cdd:COG4913 905 AVTSGASLFDEELSEARFAALKRLIERL 932
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
864-1095 |
5.09e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.47 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 864 DEVLQArAQELQKVQ--ELQQQSAREVGelqGRVAQLEEERARLAEQLRAEAELCSEAEETR-----ARLAARKQELELV 936
Cdd:PRK05771 19 DEVLEA-LHELGVVHieDLKEELSNERL---RKLRSLLTKLSEALDKLRSYLPKLNPLREEKkkvsvKSLEELIKDVEEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 937 VTELEARVGEEEECSRQLQSEKKRLQQHIQELE---------------THLEAEEGARQKLQLEKVTTEAKMKKFEE--- 998
Cdd:PRK05771 95 LEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfKYVSVFVGTVPEDKLEELKLESDVENVEYist 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 999 ----DLLLLEDQNSKLSKERRLLEErlAEFSSQAAEEEEKVKSLnklrvkyeatIADMEDRLKKEEKGRQ----ELEKLK 1070
Cdd:PRK05771 175 dkgyVYVVVVVLKELSDEVEEELKK--LGFERLELEEEGTPSEL----------IREIKEELEEIEKEREslleELKELA 242
|
250 260
....*....|....*....|....*
gi 564328072 1071 RRLDGESSELQEQMMEQKQRAEELL 1095
Cdd:PRK05771 243 KKYLEELLALYEYLEIELERAEALS 267
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1018-1297 |
5.53e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 51.41 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1018 EERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADME-----DRLKKEEKGRQ----ELEKLKRRLDGESSELQEQMMEQK 1088
Cdd:pfam02029 25 EEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeaflDRTAKREERRQkrlqEALERQKEFDPTIADEKESVAERK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1089 QRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEE----LEAL 1164
Cdd:pfam02029 105 ENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKeevkDEKI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1165 RGELEDTLDSTNAQQELRSKREQ-----EVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARR---GKSVWE 1236
Cdd:pfam02029 185 KKEKKVKYESKVFLDQKRGHPEVksqngEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRrrqEKESEE 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564328072 1237 KTRL-----SLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQ-----EVQGRSSDSERARAEAAEKLQR 1297
Cdd:pfam02029 265 FEKLrqkqqEAELELEELKKKREERRKLLEEEEQRRKQEEAERKlreeeEKRRMKEEIERRRAEAAEKRQK 335
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1544-1937 |
6.55e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 6.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1544 ERARRVAEQAASDLRTQV-----TELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGE--ERRRQLAKQLRDAEV 1616
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIeekeeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvlEEHEERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1617 ERDE--------ERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQlKKMQAQMKELWREVEETRSSREEMFTLS 1688
Cdd:PRK02224 259 EIEDlretiaetEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA-EAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1689 RESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELL 1768
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1769 KDHYRKLVLQVETLTTELSAERSFSAKAESGR---------QQLERQ-----IQELRARLGEEDAgARARQKMLIAALES 1834
Cdd:PRK02224 418 REERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSphvetIEEDRERVEELEA-ELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1835 KLAQAEEQLEQESRerilsgklVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLKRQLEEAEEE----ASRAQ 1910
Cdd:PRK02224 497 RLERAEDLVEAEDR--------IERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAE 568
|
410 420 430
....*....|....*....|....*....|
gi 564328072 1911 AGRRR---LQRELEDVTESAESMNREVTTL 1937
Cdd:PRK02224 569 EAREEvaeLNSKLAELKERIESLERIRTLL 598
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
852-1093 |
7.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 852 IKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERarlaeqlraeaelcSEAEETRARLAARKQ 931
Cdd:PRK03918 515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL--------------DELEEELAELLKELE 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 932 ELEL-VVTELEARVGEEEECSRQ---LQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKfeedlllLEDQN 1007
Cdd:PRK03918 581 ELGFeSVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE-------LEELE 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1008 SKLSKER-RLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDgESSELQEQMME 1086
Cdd:PRK03918 654 KKYSEEEyEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELREKVKK 732
|
....*..
gi 564328072 1087 QKQRAEE 1093
Cdd:PRK03918 733 YKALLKE 739
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1049-1737 |
7.13e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 51.38 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1049 IADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLRE 1128
Cdd:pfam12128 243 FTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1129 AQAGLAEAQEDLEAERVARAKAEKQRRD--------LGEELEALRGELEDTLDSTNAQQELRSKREQEVTE-----LKKT 1195
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAAADQEQLPswqselenLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAgikdkLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1196 LEEEARTHEVAM-------QELRQRHSQALVELTEQLEQARRGKSvWEKTRLSLEAEVSELKTEL----SSLQTSRQEGE 1264
Cdd:pfam12128 403 REARDRQLAVAEddlqaleSELREQLEAGKLEFNEEEYRLKSRLG-ELKLRLNQATATPELLLQLenfdERIERAREEQE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1265 QKRRRLES-QLQEVQGRSsdserARAEAAEKLQRAQVELESVSTALSEAEskairlsKELSSAESQLHD---TQELLQEE 1340
Cdd:pfam12128 482 AANAEVERlQSELRQARK-----RRDQASEALRQASRRLEERQSALDELE-------LQLFPQAGTLLHflrKEAPDWEQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1341 TRAKLAlgsrvraleAEAAGLREQMEEEVVARERAGR------ELQTTQAQLSEWRRRQEE----EAAVLEAGEEARRRA 1410
Cdd:pfam12128 550 SIGKVI---------SPELLHRTDLDPEVWDGSVGGElnlygvKLDLKRIDVPEWAASEEElrerLDKAEEALQSAREKQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1411 AREAETLAQRLAEKTEAVERLERARRRLQQELDDatvdlgqQKQLLSTLEKKQRKFDQLLAEEKAavlRAVEDRERVEAE 1490
Cdd:pfam12128 621 AAAEEQLVQANGELEKASREETFARTALKNARLD-------LRRLFDEKQSEKDKKNKALAERKD---SANERLNSLEAQ 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1491 grerearalsltraleeeqeareelerQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTA 1570
Cdd:pfam12128 691 ---------------------------LKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1571 AEDAKLRlevtvqALKAQHERDLQGRdDAGEERRRQLAKQLRD--AEVERDEERKQRALAMAA--RKKLELELEELKAQT 1646
Cdd:pfam12128 744 GAKAELK------ALETWYKRDLASL-GVDPDVIAKLKREIRTleRKIERIAVRRQEVLRYFDwyQETWLQRRPRLATQL 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1647 SAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQE----ELAASDRARRQAQQD 1722
Cdd:pfam12128 817 SNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEdansEQAQGSIGERLAQLE 896
|
730
....*....|....*
gi 564328072 1723 RDEMAEEVASGNLSK 1737
Cdd:pfam12128 897 DLKLKRDYLSESVKK 911
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1159-1893 |
8.44e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1159 EELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWE-K 1237
Cdd:pfam12128 251 NTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEdQ 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1238 TRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESK-A 1316
Cdd:pfam12128 331 HGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRqL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1317 IRLSKELSSAESQLHDTQ-----ELLQEETRAKLALGS-RVRALEAEAAG-LREQMEEEVVARERAGRELQTTQAQLSew 1389
Cdd:pfam12128 411 AVAEDDLQALESELREQLeagklEFNEEEYRLKSRLGElKLRLNQATATPeLLLQLENFDERIERAREEQEAANAEVE-- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1390 rRRQEEEAAvleageearrraareaetLAQRLAEKTEAVERLERARRRLQQELDDA-TVDLGQQKQLLSTLEKKQRKFDQ 1468
Cdd:pfam12128 489 -RLQSELRQ------------------ARKRRDQASEALRQASRRLEERQSALDELeLQLFPQAGTLLHFLRKEAPDWEQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1469 LLAE--EKAAVLRAVEDRERVEAEGRErEARALSLTRALEEEQEAREELERQnrALRAELEALLSSKDDVGKNVHELERA 1546
Cdd:pfam12128 550 SIGKviSPELLHRTDLDPEVWDGSVGG-ELNLYGVKLDLKRIDVPEWAASEE--ELRERLDKAEEALQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1547 rrvAEQAASDLRTQVTELEDELTAAEDAKL---RLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEverdeeRK 1623
Cdd:pfam12128 627 ---LVQANGELEKASREETFARTALKNARLdlrRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD------KK 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1624 QRALamaarkkleleleelkaqtsaagqgKEEAVKQLKKMQAQMKELWREVEETRSSREEMftLSRESEKRLKGLEAEVL 1703
Cdd:pfam12128 698 HQAW-------------------------LEEQKEQKREARTEKQAYWQVVEGALDAQLAL--LKAAIAARRSGAKAELK 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1704 RLQEelaasDRARRQAQQDRDEmaeEVASGNLSKAATLEekRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLT 1783
Cdd:pfam12128 751 ALET-----WYKRDLASLGVDP---DVIAKLKREIRTLE--RKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIE 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1784 TELSaersfsakaeSGRQQLERQIQELRARLGEEDAGARARQKMLIAALESklaQAEEQLEQESRERILSGKLVRRAEKR 1863
Cdd:pfam12128 821 RAIS----------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSEN---LRGLRCEMSKLATLKEDANSEQAQGS 887
|
730 740 750
....*....|....*....|....*....|
gi 564328072 1864 LKEVVLQVDEERRVADQLRDQLEKSNLRLK 1893
Cdd:pfam12128 888 IGERLAQLEDLKLKRDYLSESVKKYVEHFK 917
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1031-1899 |
9.80e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 50.74 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1031 EEEKVKSLNKL-RVKYEATIADMEDRLKKEekGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKE-EELQSA 1108
Cdd:TIGR00618 57 RSEVIRSLNSLyAAPSEAAFAELEFSLGTK--IYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSEtEEVIHD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1109 LVRAEEE---------GGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNaqq 1179
Cdd:TIGR00618 135 LLKLDYKtftrvvllpQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTP--- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1180 elrsKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARrgksvWEKTRLSLEAEVSELKTELSSLQTS 1259
Cdd:TIGR00618 212 ----CMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLK-----KQQLLKQLRARIEELRAQEAVLEET 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1260 RQEGEQKRRRLesqlqevqgRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQE 1339
Cdd:TIGR00618 283 QERINRARKAA---------PLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1340 EtraklalgSRVRALEAEAAGLREQMEEEVVARERAgRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQ 1419
Cdd:TIGR00618 354 E--------IHIRDAHEVATSIREISCQQHTLTQHI-HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQG 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1420 RLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVlravedrERVEAEGREREARAL 1499
Cdd:TIGR00618 425 QLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH-------LQETRKKAVVLARLL 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1500 SLtRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLE 1579
Cdd:TIGR00618 498 EL-QEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILT 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1580 VTVQALKAQherdlqgrddagEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQ 1659
Cdd:TIGR00618 577 QCDNRSKED------------IPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALK 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1660 LKKMQAQMKELWREVEETRSSReemftlSRESEKRLKGleaevlRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAA 1739
Cdd:TIGR00618 645 LTALHALQLTLTQERVREHALS------IRVLPKELLA------SRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1740 TLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLgeeda 1819
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEI----- 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1820 garARQKMLIAALESKLAQAEEQLEQESRERILsgklvrraEKRLKEVVLQVDEErrvadQLRDQLEKSNLRLKQLKRQL 1899
Cdd:TIGR00618 788 ---QFFNRLREEDTHLLKTLEAEIGQEIPSDED--------ILNLQCETLVQEEE-----QFLSRLEEKSATLGEITHQL 851
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1033-1297 |
9.87e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.92 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1033 EKVKSLnklrvkyEATIADMEDRLK-KEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVR 1111
Cdd:pfam00038 18 DKVRFL-------EQQNKLLETKISeLRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1112 AEEEGGARaqllkslREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR-------GELEDTLDSTNAQQELRSK 1184
Cdd:pfam00038 91 YEDELNLR-------TSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKknheeevRELQAQVSDTQVNVEMDAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1185 REQEVT----ELKKTLEEEARTHevaMQELRQRHSQALVELTEQL----EQARRGKSVWEKTRL---SLEAEVSELKTEL 1253
Cdd:pfam00038 164 RKLDLTsalaEIRAQYEEIAAKN---REEAEEWYQSKLEELQQAAarngDALRSAKEEITELRRtiqSLEIELQSLKKQK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564328072 1254 SSLQTSRQEGEQkrrRLESQLQEVQGRSSDSERARAEAAEKLQR 1297
Cdd:pfam00038 241 ASLERQLAETEE---RYELQLADYQELISELEAELQETRQEMAR 281
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
956-1730 |
1.36e-05 |
|
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: 50.43 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 956 SEKKRLQQHIQE---LETHLEAEEGARQKLQlekvTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1032
Cdd:TIGR00606 166 SEGKALKQKFDEifsATRYIKALETLRQVRQ----TQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1033 EKVKSLNKLRVKYE------ATIADMEDRLKKEEKGRQELEKLKrrldgesSELQEQMMEQKQRAEELLIQLgrkeEELQ 1106
Cdd:TIGR00606 242 SYENELDPLKNRLKeiehnlSKIMKLDNEIKALKSRKKQMEKDN-------SELELKMEKVFQGTDEQLNDL----YHNH 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1107 SALVRAEEEGGARAQ--LLKSLREAQAGLAEAQEDLEAERVARAKAEK-QRRDLGEELEALRGELEDTLDSTNAQQELRS 1183
Cdd:TIGR00606 311 QRTVREKERELVDCQreLEKLNKERRLLNQEKTELLVEQGRLQLQADRhQEHIRARDSLIQSLATRLELDGFERGPFSER 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1184 KREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQ-- 1261
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGss 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1262 ----EGEQKRRRLESQLQEVQGRSSDSERARAEAAekLQRAQVELESVSTALSE----------AESKAIRLSKELSSAE 1327
Cdd:TIGR00606 471 drilELDQELRKAERELSKAEKNSLTETLKKEVKS--LQNEKADLDRKLRKLDQemeqlnhhttTRTQMEMLTKDKMDKD 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1328 SQLHDTQELLQEETRAKLALGSRVRALEAEAAGLRE---QMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGE 1404
Cdd:TIGR00606 549 EQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKeinQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1405 EARRRAAREAETLaQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQ----LLSTLEKKQRKFDQLLAEEKAAVLRA 1480
Cdd:TIGR00606 629 FDVCGSQDEESDL-ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLA 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1481 VEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSS----KDDVGKNVHELERArRVAEQAASD 1556
Cdd:TIGR00606 708 PDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDiqrlKNDIEEQETLLGTI-MPEEESAKV 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1557 LRTQVTELEDELTAAEDAKLRLEVTVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERD--EERKQRALAMAARK 1633
Cdd:TIGR00606 787 CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDlDRTVQQVNQEKQEKQHELDTVVSKIELNRKliQDQQEQIQHLKSKT 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1634 KLELELEELKAQTSAAGQGKEEavkQLKKMQAQMKELWREVEEtrsSREEMFTLSRESEKRLKGLEAEVLRLQEElaasd 1713
Cdd:TIGR00606 867 NELKSEKLQIGTNLQRRQQFEE---QLVELSTEVQSLIREIKD---AKEQDSPLETFLEKDQQEKEELISSKETS----- 935
|
810
....*....|....*..
gi 564328072 1714 raRRQAQQDRDEMAEEV 1730
Cdd:TIGR00606 936 --NKKAQDKVNDIKEKV 950
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
947-1097 |
1.39e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.16 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 947 EEECSRQLQSEKKRLQQHIQELEthLEA-EEGARQKLQLEKVTTE--AKMKKFEEDLLLLEDQnskLSKERRLLEERLAE 1023
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEAL--LEAkEEIHKLRNEFEKELRErrNELQKLEKRLLQKEEN---LDRKLELLEKREEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1024 FSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLK------KEEKGRQELEKLKRRLDGESSELQEQMMEQ-----KQRAE 1092
Cdd:PRK12704 112 LEKKEKELEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKEILLEKVEEEARHEAAVLIKEIEEEakeeaDKKAK 191
|
....*
gi 564328072 1093 ELLIQ 1097
Cdd:PRK12704 192 EILAQ 196
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
894-1165 |
1.44e-05 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 50.07 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 894 RVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELV---VTELEA---RVGEEEEcsrqLQSEKKRLQqHIQE 967
Cdd:COG0497 149 AFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLrfqLEELEAaalQPGEEEE----LEEERRRLS-NAEK 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 968 LethLEAEEGARQklqlekvtteakmkkfeedlLLLEDQNS---KLSKERRLLEeRLAEFSSQAAEEEEKVKSLnklrvk 1044
Cdd:COG0497 224 L---REALQEALE--------------------ALSGGEGGaldLLGQALRALE-RLAEYDPSLAELAERLESA------ 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1045 yeatIADMEDrlkkeekGRQELEKLKRRLDGESSELQEqmMEQKQraeELLIQLGRK----EEELqsalvraeeeggarA 1120
Cdd:COG0497 274 ----LIELEE-------AASELRRYLDSLEFDPERLEE--VEERL---ALLRRLARKygvtVEEL--------------L 323
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 564328072 1121 QLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALR 1165
Cdd:COG0497 324 AYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKLSAAR 368
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1177-1398 |
1.48e-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: 49.38 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1177 AQQELRSKREQEVTELKKTLEEEARTHEvAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSL 1256
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1257 QTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQEL 1336
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1337 LQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAA 1398
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1602-1925 |
1.61e-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: 50.34 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1602 ERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMkelwREVEETRSSR 1681
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL----RQQEKIERYQ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1682 EEMftlsRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVAsgNLSKAATLEEKR-----QLEGRLGQLEE 1756
Cdd:COG3096 354 EDL----EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA--DYQQALDVQQTRaiqyqQAVQALEKARA 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1757 ELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGE---EDAGARARQKMLIAALE 1833
Cdd:COG3096 428 LCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEverSQAWQTARELLRRYRSQ 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1834 SKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEksnlrlkQLKRQLEEAEEEASRAQAGR 1913
Cdd:COG3096 508 QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA-------ELEAQLEELEEQAAEAVEQR 580
|
330
....*....|..
gi 564328072 1914 RRLQRELEDVTE 1925
Cdd:COG3096 581 SELRQQLEQLRA 592
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1064-1354 |
1.75e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.30 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1064 QELEKLKRRLDGESSELQEQMME-QKQRAE--ELLIQLGRKEEELQSALVRAeeeggarAQLLKSLREAQAGLAEAQEDL 1140
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAyGKLRRElaGLTRRLSAAEGELEELVARL-------AKLEAALREAEAAKEELRIEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1141 EAERVARAKAEKQ-------RRDLGEELEALRGEL----EDTLDSTNAQQELRSKR---EQEVTELKKTLEE---EARTH 1203
Cdd:pfam19220 114 RDKTAQAEALERQlaaeteqNRALEEENKALREEAqaaeKALQRAEGELATARERLallEQENRRLQALSEEqaaELAEL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1204 EVAMQELRQR---HSQALVELTEQL--EQARRGKSVWEktrlsLEAEVSELKTELSSLQtsrqegeqkrrrleSQLQEVQ 1278
Cdd:pfam19220 194 TRRLAELETQldaTRARLRALEGQLaaEQAERERAEAQ-----LEEAVEAHRAERASLR--------------MKLEALT 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1279 GRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRAL 1354
Cdd:pfam19220 255 ARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEML 330
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
862-1382 |
1.88e-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: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 862 RQDEVLQARAQELQKvqELQQQSAREVG---ELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELEL--- 935
Cdd:COG3096 525 EQRLRQQQNAERLLE--EFCQRIGQQLDaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAArap 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 936 -------VVTELEARVGEEEECSRQLQSEKKRLQQHIQELEThlEAEEGARQKLQLEKVTTEAKMKKFEED--LLLLEDQ 1006
Cdd:COG3096 603 awlaaqdALERLREQSGEALADSQEVTAAMQQLLEREREATV--ERDELAARKQALESQIERLSQPGGAEDprLLALAER 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1007 ---------------------------------NSKLSKERRLLEER---------------LAEFSSQAAEEEEK---V 1035
Cdd:COG3096 681 lggvllseiyddvtledapyfsalygparhaivVPDLSAVKEQLAGLedcpedlyliegdpdSFDDSVFDAEELEDavvV 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1036 KSLNK-LRVKYEATI-----ADMEDRLkkeEKGRQELEKLKRRLDGESSELQEQmmeqkQRAEELLIQLgrkeeeLQSAL 1109
Cdd:COG3096 761 KLSDRqWRYSRFPEVplfgrAAREKRL---EELRAERDELAEQYAKASFDVQKL-----QRLHQAFSQF------VGGHL 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1110 VRAEEEGGARAqllksLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT--LDSTNAQQELRskreq 1187
Cdd:COG3096 827 AVAFAPDPEAE-----LAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQAnlLADETLADRLE----- 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1188 evtelkkTLEEEARTHEVAMQELRQrHSQALVELTEQLeqarrgkSVWEKTRLSLEAevselktelssLQTSRQEGEQKR 1267
Cdd:COG3096 897 -------ELREELDAAQEAQAFIQQ-HGKALAQLEPLV-------AVLQSDPEQFEQ-----------LQADYLQAKEQQ 950
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1268 RRLESQ---LQEVQGRS-----SDSERARAEAA-------EKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHD 1332
Cdd:COG3096 951 RRLKQQifaLSEVVQRRphfsyEDAVGLLGENSdlneklrARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA 1030
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 564328072 1333 TQELLQEETRAKLALGSRVRA-LEAEAAGLREQMEEEVVARERAGRELQTT 1382
Cdd:COG3096 1031 KQQTLQELEQELEELGVQADAeAEERARIRRDELHEELSQNRSRRSQLEKQ 1081
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1014-1196 |
1.95e-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: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 RRLLEerLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRaee 1093
Cdd:COG1579 7 RALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1094 llIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLD 1173
Cdd:COG1579 82 --LGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELE 159
|
170 180
....*....|....*....|...
gi 564328072 1174 stnaqqELRSKREQEVTELKKTL 1196
Cdd:COG1579 160 ------ELEAEREELAAKIPPEL 176
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1071-1695 |
2.01e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 49.75 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1071 RRLDGESSELQEQMMEQKQRAEELLIQLgrkeeelqSALVRAEEEGGARAQllkSLREAQAGlaeaqedleAERVARAKA 1150
Cdd:pfam07111 76 RRLEEEVRLLRETSLQQKMRLEAQAMEL--------DALAVAEKAGQAEAE---GLRAALAG---------AEMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1151 EKQRRDLgEELEALrgeledtldstnaQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARR 1230
Cdd:pfam07111 136 EGSQREL-EEIQRL-------------HQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1231 GKSVWEKTRLSLEAEVSELKT------ELSSLQTSRQEGEQKRRRLESQLQEVQgrssdseRARAEAAEKLQRAQVELES 1304
Cdd:pfam07111 202 LRKQLSKTQEELEAQVTLVESlrkyvgEQVPPEVHSQTWELERQELLDTMQHLQ-------EDRADLQATVELLQVRVQS 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1305 VSTALSEAESKAIRLSKELSSAESQL-HDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVvareragrelqttq 1383
Cdd:pfam07111 275 LTHMLALQEEELTRKIQPSDSLEPEFpKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQV-------------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1384 AQLSEWRRRQEEEAAVLEAGEEARRRAAReaetlAQRLAEKTEAVERLERARRRLQQELDDATVDlGQQKQLLSTLEKKQ 1463
Cdd:pfam07111 341 AELQEQVTSQSQEQAILQRALQDKAAEVE-----VERMSAKGLQMELSRAQEARRRQQQQTASAE-EQLKFVVNAMSSTQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1464 RKFDQLLAEEKAAVLRAVEDRERVEAEGRERE------ARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVG 1537
Cdd:pfam07111 415 IWLETTMTRVEQAVARIPSLSNRLSYAVRKVHtikglmARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1538 KNV--------HELERARRVAEQAASDLRTQVTELEDELTAAEDA----KLRLEVTVQA--------------LKAQHER 1591
Cdd:pfam07111 495 AELqlsahliqQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlasvGQQLEVARQGqqesteeaaslrqeLTQQQEI 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1592 DLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVK-QLKKMQAQMKEL 1670
Cdd:pfam07111 575 YGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELRRLQDEARKeEGQRLARRVQEL 654
|
650 660
....*....|....*....|....*
gi 564328072 1671 WREVEETRSSREEMFTLSRESEKRL 1695
Cdd:pfam07111 655 ERDKNLMLATLQQEGLLSRYKQQRL 679
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1163 |
2.08e-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: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1003 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKgRQELEKLKRRLDGESSELqE 1082
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE-QLGNVRNNKEYEALQKEI-E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1083 QMMEQKQRAEELLIQLGRKEEELQSALVRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAErvaRAKAEKQRRDLGEELE 1162
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAE---LAELEAELEEKKAELDEELAELEAE---LEELEAEREELAAKIP 173
|
.
gi 564328072 1163 A 1163
Cdd:COG1579 174 P 174
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
857-1235 |
2.26e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.37 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVLQARAQELQKVQELQQQSARE------VGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARK 930
Cdd:pfam09731 72 VSAVTGESKEPKEEKKQVKIPRQSGVSSEVAeeekeaTKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 931 QELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NS 1008
Cdd:pfam09731 152 KDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHldNV 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1009 KLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQK 1088
Cdd:pfam09731 232 EEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQLSKKLAELKKREE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1089 QRAEELLIQlgrkeeelqsalvRAEEEGGARAQLLKSLREAQAgLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1168
Cdd:pfam09731 312 KHIERALEK-------------QKEELDKLAEELSARLEEVRA-ADEAQLRLEFEREREEIRESYEEKLRTELERQAEAH 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1169 EDTLDSTNAQQELRSKREQEvTELKKTLEEEARTHEVAMQELRQR---HSQALVELTEQLEQARRGKSVW 1235
Cdd:pfam09731 378 EEHLKDVLVEQEIELQREFL-QDIKEKVEEERAGRLLKLNELLANlkgLEKATSSHSEVEDENRKAQQLW 446
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
856-976 |
2.60e-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: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 856 PLLQVTRQDEVLQArAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELEL 935
Cdd:COG4942 121 PLALLLSPEDFLDA-VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK 199
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564328072 936 VVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEE 976
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1519-1943 |
2.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1519 NRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHE-RDLQGRD 1597
Cdd:COG4717 69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAElAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1598 DAGEERRRQLAKQLRD-AEVERDEERKQRALAMAARKKLELELeelkAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEE 1676
Cdd:COG4717 149 EELEERLEELRELEEElEELEAELAELQEELEELLEQLSLATE----EELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1677 TRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEE 1756
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1757 ELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKaesgrqQLERQIQELRARLgeEDAGARARQKMLIAALESKL 1836
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELL------DRIEELQELLREA--EELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1837 AQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNL--RLKQLKRQLEEAEEEASRAQAGRR 1914
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeeELEELEEELEELEEELEELREELA 456
|
410 420 430
....*....|....*....|....*....|.
gi 564328072 1915 RLQRELEDVTESAE--SMNREVTTLRNRLRR 1943
Cdd:COG4717 457 ELEAELEQLEEDGElaELLQELEELKAELRE 487
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
887-1265 |
2.83e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 887 EVGELQGRVAQLEEERARLAEQLRAEAELCSEAEEtrARLAARKQELELVVTELEARVGEEEECSRQLQS---------- 956
Cdd:PRK04863 751 SVEELEKAVVVKIADRQWRYSRFPEVPLFGRAARE--KRIEQLRAEREELAERYATLSFDVQKLQRLHQAfsrfigshla 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 957 ---------EKKRLQQHIQELETHLEAEEGARQKLQlekvtteAKMKKFEEDLLLLE---DQNSKLSKERrlLEERLAEF 1024
Cdd:PRK04863 829 vafeadpeaELRQLNRRRVELERALADHESQEQQQR-------SQLEQAKEGLSALNrllPRLNLLADET--LADRVEEI 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1025 SSQAAEEEEKVKSLNklrvKYEATIAdmedrlkkeekgrqELEKLKRRLDGESSELqEQMMEQKQRAEELLIQLGRKEEE 1104
Cdd:PRK04863 900 REQLDEAEEAKRFVQ----QHGNALA--------------QLEPIVSVLQSDPEQF-EQLKQDYQQAQQTQRDAKQQAFA 960
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1105 LQSALVRaeeeggaRAQLlkSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtlDSTNAQQELRSK 1184
Cdd:PRK04863 961 LTEVVQR-------RAHF--SYEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLA---QYNQVLASLKSS 1028
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1185 R---EQEVTELKKTLEE-EARTHEVAMQELRQRHSqalvELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQ-TS 1259
Cdd:PRK04863 1029 YdakRQMLQELKQELQDlGVPADSGAEERARARRD----ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLErDY 1104
|
....*.
gi 564328072 1260 RQEGEQ 1265
Cdd:PRK04863 1105 HEMREQ 1110
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1012-1751 |
2.85e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.57 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1012 KERRLLEERLAEFSSQAAEEEEKVKSLnklrvkyEATIADMEDRLKKEEKGRQELEKLKRrLDGESSELQEQMMEQKQRA 1091
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDL-------EQDYQAASDHLNLVQTALRQQEKIER-YQADLEELEERLEEQNEVV 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1092 EELLIQLGRKEEELQsalvRAEEEggaraqllksLREAQAGLAEAQEDLEAERvARAKAEKQRRDLGEELEALRGELEDT 1171
Cdd:PRK04863 372 EEADEQQEENEARAE----AAEEE----------VDELKSQLADYQQALDVQQ-TRAIQYQQAVQALERAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1172 LDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAmqelRQRHSQAL---------VELTEQLEQARRGKSVWEKTRLsL 1242
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAA----HSQFEQAYqlvrkiageVSRSEAWDVARELLRRLREQRH-L 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1243 EAEVSELKTELSSLQTSRQEgeqkRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAirlske 1322
Cdd:PRK04863 512 AEQLQQLRMRLSELEQRLRQ----QQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERR------ 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1323 lssaeSQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEA 1402
Cdd:PRK04863 582 -----MALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQA 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1403 GEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDA---------------TVDLGQQKQLLSTL-------- 1459
Cdd:PRK04863 657 LDEEIERLSQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDApyfsalygparhaivVPDLSDAAEQLAGLedcpedly 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1460 --EKKQRKFDQ--LLAEE-KAAVLRAVEDRE----RVEAE---GRE-REARALSLTRALEEEQEAREELERQNRALR--- 1523
Cdd:PRK04863 737 liEGDPDSFDDsvFSVEElEKAVVVKIADRQwrysRFPEVplfGRAaREKRIEQLRAEREELAERYATLSFDVQKLQrlh 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1524 --------------------AELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVT--------------------- 1562
Cdd:PRK04863 817 qafsrfigshlavafeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSalnrllprlnlladetladrv 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1563 -ELEDELTAAEDAKL----------RLEVTVQALKA---QHERdLQGRDDAGEERRRQLAKQLRdAEVERDEERKQRALA 1628
Cdd:PRK04863 897 eEIREQLDEAEEAKRfvqqhgnalaQLEPIVSVLQSdpeQFEQ-LKQDYQQAQQTQRDAKQQAF-ALTEVVQRRAHFSYE 974
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1629 MAARKKLELELEELK--AQTSAAGQGKEEAVKQLKKMQAQM---------------------KELWREVEET-------- 1677
Cdd:PRK04863 975 DAAEMLAKNSDLNEKlrQRLEQAEQERTRAREQLRQAQAQLaqynqvlaslkssydakrqmlQELKQELQDLgvpadsga 1054
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1678 ----RSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKR--QLEGRL 1751
Cdd:PRK04863 1055 eeraRARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKdnGVERRL 1134
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1178-1713 |
3.14e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.97 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1178 QQELRSKREQEVTELKKTLEEEARTHEVA--------MQELRQRHSQALVELTEQLEQARRGK------SVWEKTRLSLE 1243
Cdd:pfam05557 20 QMELEHKRARIELEKKASALKRQLDRESDrnqelqkrIRLLEKREAEAEEALREQAELNRLKKkylealNKKLNEKESQL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1244 AEVSE----LKTELSSLQTSRQEGEQKRRRLESQLQEVQGRsSDSERARAEAAEKLQRaqvELESVSTALSEAESKAIRL 1319
Cdd:pfam05557 100 ADAREviscLKNELSELRRQIQRAELELQSTNSELEELQER-LDLLKAKASEAEQLRQ---NLEKQQSSLAEAEQRIKEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1320 SKELssaESQLHDTQELlqEETRAKLA----LGSRVRALEAEAAGLREQMEEEVVAREragrELQTTQAQLSEWRRRQeE 1395
Cdd:pfam05557 176 EFEI---QSQEQDSEIV--KNSKSELAripeLEKELERLREHNKHLNENIENKLLLKE----EVEDLKRKLEREEKYR-E 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1396 EAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQElddaTVDLGQQKQLLSTLEKKQRKFDQLLAEEKA 1475
Cdd:pfam05557 246 EAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQR----EIVLKEENSSLTSSARQLEKARRELEQELA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1476 AVLRAVED----RERVEAEGREREARALSLTRALEEeqeareelerqnraLRAELEALLSSKDDVGKNVHELERARRVAE 1551
Cdd:pfam05557 322 QYLKKIEDlnkkLKRHKALVRRLQRRVLLLTKERDG--------------YRAILESYDKELTMSNYSPQLLERIEEAED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1552 ------QAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRdAEVERDEERKQR 1625
Cdd:pfam05557 388 mtqkmqAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSKEEVDSLRRKLETLE-LERQRLREQKNE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1626 ALAMAARKKLELELEELKA-----QTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEMFTLSRESekrLKGLEA 1700
Cdd:pfam05557 467 LEMELERRCLQGDYDPKKTkvlhlSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETT---STMNFK 543
|
570
....*....|...
gi 564328072 1701 EVLRLQEELAASD 1713
Cdd:pfam05557 544 EVLDLRKELESAE 556
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1044-1164 |
3.27e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1044 KYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLgrkEEELQSALVRAEEEGgarAQLL 1123
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEA---EKEAQQAIKEAKKEA---DEII 590
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 564328072 1124 KSLREAQAGLAEAQedleaervARAKAEKQRRDLGEELEAL 1164
Cdd:PRK00409 591 KELRQLQKGGYASV--------KAHELIEARKRLNKANEKK 623
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1003-1229 |
3.52e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1003 LEDQNSKLSKERRLLEERLAEFSSQAAEEEEKvksLNKLRVKYEatIADMEDRLKKEEkgrQELEKLKRRLdgesSELQE 1082
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAA---LEEFRQKNG--LVDLSEEAKLLL---QQLSELESQL----AEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1083 QMMEQKQRAEELLIQLGRKEEELQSALvraeeEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELE 1162
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564328072 1163 AlrgELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELR------QRHSQALVELTEQLEQAR 1229
Cdd:COG3206 309 Q---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlerevEVARELYESLLQRLEEAR 378
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
898-1233 |
3.58e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 898 LEEERARLAEqlraEAELCSEAEETRARLAARKQELELVVTELEA-----RVGEEEECSRQLQSEKKRLQQHIQELEThl 972
Cdd:PLN03188 938 LEEELASLMH----EHKLLKEKYENHPEVLRTKIELKRVQDELEHyrnfyDMGEREVLLEEIQDLRSQLQYYIDSSLP-- 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 973 eaeeGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSklSKERRLLEERLaefssQAAEEEEKVKSL-NKLRVKYEATIAD 1051
Cdd:PLN03188 1012 ----SARKRNSLLKLTYSCEPSQAPPLNTIPESTDE--SPEKKLEQERL-----RWTEAESKWISLaEELRTELDASRAL 1080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1052 MEdrlkkeeKGRQELEKLKRRldgeSSELQE----------QMMEQKQRAEELLIQLGRKEEELQSAlVRAEEEGGARAq 1121
Cdd:PLN03188 1081 AE-------KQKHELDTEKRC----AEELKEamqmameghaRMLEQYADLEEKHIQLLARHRRIQEG-IDDVKKAAARA- 1147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1122 llkSLREAQAGLAEAqedLEAERVA-RAKAEKQRRDLGEELEALRGELEDTLDSTNAQQEL--RSKREQE--VTELKKTL 1196
Cdd:PLN03188 1148 ---GVRGAESKFINA---LAAEISAlKVEREKERRYLRDENKSLQAQLRDTAEAVQAAGELlvRLKEAEEalTVAQKRAM 1221
|
330 340 350
....*....|....*....|....*....|....*....
gi 564328072 1197 EEEARTHEV--AMQELRQRHSQALVELTEQLEQARRGKS 1233
Cdd:PLN03188 1222 DAEQEAAEAykQIDKLKRKHENEISTLNQLVAESRLPKE 1260
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
853-1094 |
3.89e-05 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 49.16 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 853 KVKPLLQVTRQDEVLQAraQELQKVQELQQQSAREvgelqgrvaQLEEERARLAEqlrAEAELCSEAEETRA-----RLA 927
Cdd:PLN03188 1015 KRNSLLKLTYSCEPSQA--PPLNTIPESTDESPEK---------KLEQERLRWTE---AESKWISLAEELRTeldasRAL 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 928 ARKQELELvvtELEARVGEEEECSRQL--QSEKKRLQQ-------HIQELETHLEAEEGARQklqLEKVTTEAKMKKFEE 998
Cdd:PLN03188 1081 AEKQKHEL---DTEKRCAEELKEAMQMamEGHARMLEQyadleekHIQLLARHRRIQEGIDD---VKKAAARAGVRGAES 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 999 DLL-LLEDQNSKL----SKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYE-----ATIAD---MEDRLKKEEKGRQe 1065
Cdd:PLN03188 1155 KFInALAAEISALkverEKERRYLRDENKSLQAQLRDTAEAVQAAGELLVRLKeaeeaLTVAQkraMDAEQEAAEAYKQ- 1233
|
250 260
....*....|....*....|....*....
gi 564328072 1066 LEKLKRRLDGESSELQEQMMEQKQRAEEL 1094
Cdd:PLN03188 1234 IDKLKRKHENEISTLNQLVAESRLPKEAI 1262
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1066-1940 |
4.19e-05 |
|
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: 48.89 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1066 LEKLKRRLDGESSELQEQMMEQK------QRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEd 1139
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKylkqykEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1140 LEAERVARAKAEKQRRDLGEELEALRGELEDTLDST------NAQQELRSKREQEVTELKK--TLEEEARTHEVAMQELR 1211
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlndlyhNHQRTVREKERELVDCQREleKLNKERRLLNQEKTELL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1212 QRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSE----LKTELSSLQTSRQEGEQKRRRLESQL-QEVQGRSSDSER 1286
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFErgpfSERQIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1287 ARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGsrvralEAEAAGLREQME 1366
Cdd:TIGR00606 427 QADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELS------KAEKNSLTETLK 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1367 EEVVAreragreLQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAEtlaqrlaEKTEAVERLERARRRLQQELDDAT 1446
Cdd:TIGR00606 501 KEVKS-------LQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTK-------DKMDKDEQIRKIKSRHSDELTSLL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1447 VDLGQQKQLLSTLEKKQRKFDQL---LAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRaLR 1523
Cdd:TIGR00606 567 GYFPNKKQLEDWLHSKSKEINQTrdrLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLER-LK 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1524 AELEAllSSKDdvgknvhelerarRVAEQAASDLRTQ-VTELEDELTAAEDAKLRLEVTVQALKaQHERDLQGRDDAGEE 1602
Cdd:TIGR00606 646 EEIEK--SSKQ-------------RAMLAGATAVYSQfITQLTDENQSCCPVCQRVFQTEAELQ-EFISDLQSKLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1603 RRRQLAKQLRDAEVERDEerkqrALAMAARKKLELELEelkaqtsaagqgkeeaVKQLKKMQAQMKELWREVEETRSSRE 1682
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDE-----MLGLAPGRQSIIDLK----------------EKEIPELRNKLQKVNRDIQRLKNDIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1683 EMFTL------SRESEKRLKGLEAEVLRLQEELaaSDRARRQAQQdrdemAEEVASGNLSKAATlEEKRQLEGRLGQLEE 1756
Cdd:TIGR00606 769 EQETLlgtimpEEESAKVCLTDVTIMERFQMEL--KDVERKIAQQ-----AAKLQGSDLDRTVQ-QVNQEKQEKQHELDT 840
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1757 ELEEEQNNSELLKDHyRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGE---EDAGARARQKMLIAALE 1833
Cdd:TIGR00606 841 VVSKIELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLETFLE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1834 SKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQV-DEERRVADQLRDQLEKSNLRLKQLKRQLEEAEEEASRAQAG 1912
Cdd:TIGR00606 920 KDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMkDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINED 999
|
890 900
....*....|....*....|....*...
gi 564328072 1913 RRRLQRELeDVTESAESMNREVTTLRNR 1940
Cdd:TIGR00606 1000 MRLMRQDI-DTQKIQERWLQDNLTLRKR 1026
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1698-1943 |
4.60e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1698 LEAEVLRLQEELAASDRARRQAQQDRDEMA--EEVASGNLSKAATLEEKRQLEGRLgqLEEELEEEQNNSELLKDHYRKL 1775
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLR--AALRLWFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1776 VLQVETLTTELSAersfsakAESGRQQLERQIQELRARLgEEDAGARarqkmlIAALESKLAQAEEQLEQESRERilsgk 1855
Cdd:COG4913 301 RAELARLEAELER-------LEARLDALREELDELEAQI-RGNGGDR------LEQLEREIERLERELEERERRR----- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1856 lvRRAEKRLKEVVLQVDEER----RVADQLRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMN 1931
Cdd:COG4913 362 --ARLEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
250
....*....|..
gi 564328072 1932 REVTTLRNRLRR 1943
Cdd:COG4913 440 ARLLALRDALAE 451
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1706-1948 |
4.65e-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: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1706 QEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTE 1785
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1786 LSAERSFSAKAESGRQQLERQiQELRARLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLK 1865
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1866 EVVLQVDEERRVADQLRDQLEKsnlRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGP 1945
Cdd:COG4942 178 ALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
...
gi 564328072 1946 LTF 1948
Cdd:COG4942 255 LPW 257
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1111-1452 |
5.45e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1111 RAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVT 1190
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1191 ELKKTLEEEARTHEVAMQELRQRhSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRL 1270
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL-QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1271 ESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSR 1350
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1351 VRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVER 1430
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALL 322
|
330 340
....*....|....*....|..
gi 564328072 1431 LERARRRLQQELDDATVDLGQQ 1452
Cdd:COG4372 323 ELAKKLELALAILLAELADLLQ 344
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1660-1966 |
5.83e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 5.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1660 LKKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAA 1739
Cdd:pfam07888 47 LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1740 TLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDA 1819
Cdd:pfam07888 127 HEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1820 GARARQKMlIAALESKLAQAE------EQLEQE---SRERI-LSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSN 1889
Cdd:pfam07888 207 QVLQLQDT-ITTLTQKLTTAHrkeaenEALLEElrsLQERLnASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLT 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1890 LRLKQLKRQLeeaEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRgpltftTRTVRQVFRLEEGVASD 1966
Cdd:pfam07888 286 LQLADASLAL---REGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQE------ERMEREKLEVELGREKD 353
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1047-1316 |
5.96e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1047 ATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQsalvraeeeggaraQLLKSL 1126
Cdd:COG3883 9 PTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1127 REAQAGLAEAQEDLEaervARAKAEKQRRDLGEELEALRG--ELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHE 1204
Cdd:COG3883 75 AEAEAEIEERREELG----ERARALYRSGGSVSYLDVLLGseSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1205 VAMQELRQrhsqaLVELTEQLEQARRgksvwektrlSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDS 1284
Cdd:COG3883 151 ELEAKLAE-----LEALKAELEAAKA----------ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
250 260 270
....*....|....*....|....*....|..
gi 564328072 1285 ERARAEAAEKLQRAQVELESVSTALSEAESKA 1316
Cdd:COG3883 216 AAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
873-1315 |
6.19e-05 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 47.76 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 873 ELQKVQELQQQSAREVGELQGRVAQLEEERARLA---EQLRAEAELCSEAEETRARLAARKQELELVVTELearvgeeEE 949
Cdd:pfam05622 1 DLSEAQEEKDELAQRCHELDQQVSLLQEEKNSLQqenKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQL-------QE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 950 CSRQLQSEKKRLQQHIQELETHLeAEEGARQKlQLEKVTTEAKMKKFEEDllLLEDQNSKLSKERRLLE------ERLAE 1023
Cdd:pfam05622 74 ENFRLETARDDYRIKCEELEKEV-LELQHRNE-ELTSLAEEAQALKDEMD--ILRESSDKVKKLEATVEtykkklEDLGD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1024 FSSQaaeeeekVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLdgesSELQEQMMEQKQRAEELLIQLGRKEE 1103
Cdd:pfam05622 150 LRRQ-------VKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQV----QELHGKLSEESKKADKLEFEYKKLEE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1104 ELqSALVRAEEeggaraqllkSLREAQAGLAEAQEDLEAervarakAEKQRRDLGEElEALRGELEDTLDSTNAqqelrs 1183
Cdd:pfam05622 219 KL-EALQKEKE----------RLIIERDTLRETNEELRC-------AQLQQAELSQA-DALLSPSSDPGDNLAA------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1184 krEQEVTELKKTLEEeaRTHEVAMQELRQRHS--QALVELTEQLEQARRGKSVWE-KTRLSLEaEVSELKTELSSLQTSR 1260
Cdd:pfam05622 274 --EIMPAEIREKLIR--LQHENKMLRLGQEGSyrERLTELQQLLEDANRRKNELEtQNRLANQ-RILELQQQVEELQKAL 348
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1261 QEGEQK-------RRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESK 1315
Cdd:pfam05622 349 QEQGSKaedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALRK 410
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
865-1276 |
6.42e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.21 E-value: 6.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 865 EVLQARAQELQKVQELQQQsarevgELQGRVAQLEEERARLAEQLRAEAELCSEAE-ETRARLAARKQELELVVTELEAR 943
Cdd:pfam07111 266 ELLQVRVQSLTHMLALQEE------ELTRKIQPSDSLEPEFPKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVKQLRGQ 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 944 VGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAE 1023
Cdd:pfam07111 340 VAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLET 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1024 FSSQAAEEEEKVKSLNK---LRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGR 1100
Cdd:pfam07111 420 TMTRVEQAVARIPSLSNrlsYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQL 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1101 KEEELQSALVRAEEEGGA-RAQLLKSLREAQAGLAEAQEDLEAervarakaekqrrdLGEELE-ALRGELEDTLDSTNAQ 1178
Cdd:pfam07111 500 SAHLIQQEVGRAREQGEAeRQQLSEVAQQLEQELQRAQESLAS--------------VGQQLEvARQGQQESTEEAASLR 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1179 QELRSKRE-------QEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTE-QLEQARRGKSVWEKTRLSLEAEvselK 1250
Cdd:pfam07111 566 QELTQQQEiygqalqEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQiQHRATQEKERNQELRRLQDEAR----K 641
|
410 420
....*....|....*....|....*.
gi 564328072 1251 TELSSLQTSRQEGEQKRRRLESQLQE 1276
Cdd:pfam07111 642 EEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
863-1071 |
6.62e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.93 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 863 QDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARlaeqLRAE-AELCSEAEETRARLAARKQELELVVTELE 941
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVER----LEAEvEELEAELEEKDERIERLERELSEARSEER 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 942 ARVGEEEECSR------QLQSEKKRLQQHIQELETHLEAEEGARQKLQ---------LEKVTTEA------KMKKFEEDL 1000
Cdd:COG2433 459 REIRKDREISRldreieRLERELEEERERIEELKRKLERLKELWKLEHsgelvpvkvVEKFTKEAirrleeEYGLKEGDV 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1001 LLLEDQNSKLSKERRLLEE-------RLAEFSSQAAE------------EEEKVKSLNKLRV----KYEATIADMEDRLK 1057
Cdd:COG2433 539 VYLRDASGAGRSTAELLAEagpraviVPGELSEAADEvlfeegipvlpaEDVTIQEVDDLAVvdeeELEAAIEDWEERAE 618
|
250
....*....|....
gi 564328072 1058 KEEKgRQELEKLKR 1071
Cdd:COG2433 619 ERRR-EKKAEMLER 631
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1215-1445 |
6.82e-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: 47.45 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1215 SQALVELTEQLEQARRGKSvwektrlSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEK 1294
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1295 LQRAQVELESVSTALSEAESKAIRLSKelSSAESQLHDTQELLQEETRAKLaLGSRVRALEAEAAGLREQMEEEVVARER 1374
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGR--QPPLALLLSPEDFLDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564328072 1375 AGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDA 1445
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1049-1225 |
7.54e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.46 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1049 IADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEeggARAQL--LKSL 1126
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK---YEEQLgnVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1127 REAQAglaeAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTldstnaqQELRSKREQEVTELKKTLEEEARTHEVA 1206
Cdd:COG1579 89 KEYEA----LQKEIESLKRRISDLEDEILELMERIEELEEELAEL-------EAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....*....
gi 564328072 1207 MQELRQRHSQALVELTEQL 1225
Cdd:COG1579 158 LEELEAEREELAAKIPPEL 176
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1293-1887 |
8.23e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1293 EKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSR---VRALEAEAAGLREQMEEev 1369
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegsKRKLEEKIRELEERIEE-- 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1370 vaRERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAqRLAEKTEAVERLERARRRLQQELDDATVDL 1449
Cdd:PRK03918 271 --LKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLS-RLEEEINGIEERIKELEEKEERLEELKKKL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1450 GQQKQLLSTLEKKQRKFdqllaeEKAAVLRAVEDRERVEAEGREREAralsltraleeeqeareelerqnraLRAELEAL 1529
Cdd:PRK03918 348 KELEKRLEELEERHELY------EEAKAKKEELERLKKRLTGLTPEK-------------------------LEKELEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1530 LSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDeltaaedAKLRLEVTVQALKAQHERDLQGRDDAG--------- 1600
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK-------AKGKCPVCGRELTEEHRKELLEEYTAElkriekelk 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1601 --EERRRQLAKQLRDAEVERDEERKQRALamaarkkleleleelkaqtsaagqgkEEAVKQLKKMQAQMKEL-WREVEET 1677
Cdd:PRK03918 470 eiEEKERKLRKELRELEKVLKKESELIKL--------------------------KELAEQLKELEEKLKKYnLEELEKK 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1678 RSSREEMFTLSRESEKRLKGLEAEVLRLQE---ELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEK-RQLEGRLGQ 1753
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkKLAELEKKLDELEEELAELLKELEELGFESVEELEERlKELEPFYNE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1754 LEEELEEEQNNSELLKdhyrklvlQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAgARARQKMLiaALE 1833
Cdd:PRK03918 604 YLELKDAEKELEREEK--------ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEY-EELREEYL--ELS 672
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1834 SKLAQAEEQLEQesrerilsgklvrrAEKRLKEVvlqvdeeRRVADQLRDQLEK 1887
Cdd:PRK03918 673 RELAGLRAELEE--------------LEKRREEI-------KKTLEKLKEELEE 705
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
907-1336 |
9.59e-05 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 47.63 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 907 EQLRAEAELCSEAEETRARLAARKQELELvvtELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGarqKLQLEK 986
Cdd:pfam15818 14 EELRMRREAETQYEEQIGKIIVETQELKW---QKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEKG---KYQLAT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 987 VTTEAKMKKFEEDLLLLedQNSKLSKERRLLE-ERLAEFSSQAAEEEEKvkSLNKLRvKYEATIADM-----EDRLKKE- 1059
Cdd:pfam15818 88 EIKEKEIEGLKETLKAL--QVSKYSLQKKVSEmEQKLQLHLLAKEDHHK--QLNEIE-KYYATITGQfglvkENHGKLEq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1060 ----------------EKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQsalvraeeeggaraqll 1123
Cdd:pfam15818 163 nvqeaiqlnkrlsalnKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQ----------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1124 kslreaqaglaEAQEDLEAERVARAKaekqrrdLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELK---KTLEEEA 1200
Cdd:pfam15818 226 -----------ELQERLNMELELNKK-------INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEaelKALKENN 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1201 RTHEVAMQELRQR---HSQALVELTEQLEQARRgksVWEKTRLSLEAEVSELKTELSSLQTSR--------QEGEQKRRR 1269
Cdd:pfam15818 288 QTLERDNELQREKvkeNEEKFLNLQNEHEKALG---TWKKHVEELNGEINEIKNELSSLKETHiklqehynKLCNQKKFE 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564328072 1270 LESQLQEVQGRSSDSERARAEAAEKL------QRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQEL 1336
Cdd:pfam15818 365 EDKKFQNVPEVNNENSEMSTEKSENLiiqkynSEQEIREENTKSFCSDTEYRETEKKKGPPVEEIIIEDLQVL 437
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
862-1201 |
1.04e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 47.59 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 862 RQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLaEQLRAEAElcseaeETRARLAARKQELELVVTELE 941
Cdd:PLN02939 104 RDEAIAAIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLL-NQARLQAL------EDLEKILTEKEALQGKINILE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 942 ARVGEEEECSRQLQSEKKrlqqHIQELETHLEAeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERL 1021
Cdd:PLN02939 177 MRLSETDARIKLAAQEKI----HVEILEEQLEK---LRNELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAEL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1022 AEFssqaAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKrrldgesselQEQMMEqkqraeelliqlgrK 1101
Cdd:PLN02939 250 IEV----AETEERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQ----------YDCWWE--------------K 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1102 EEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRdLGEELEALRGELEDTLDSTNAQQEL 1181
Cdd:PLN02939 302 VENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVEL-LQQKLKLLEERLQASDHEIHSYIQL 380
|
330 340
....*....|....*....|
gi 564328072 1182 RSKREQEVTELKKTLEEEAR 1201
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESK 400
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
857-1101 |
1.09e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVLQARAQELQKVQELQ------QQSAREVGELQGRVAQLEEERARLAEQLraeaelcseaeetrarlaark 930
Cdd:COG0497 137 LLDPDAQRELLDAFAGLEELLEEYReayrawRALKKELEELRADEAERARELDLLRFQL--------------------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 931 QELElvvtELEARVGEEEEcsrqLQSEKKRLqQHIQELETHL--------EAEEGARQKL-----QLEKVTT-----EAK 992
Cdd:COG0497 196 EELE----AAALQPGEEEE----LEEERRRL-SNAEKLREALqealealsGGEGGALDLLgqalrALERLAEydpslAEL 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 993 MKKFEEDLLLLEDQNSKLSKERRLLE---ERLAEFssqaaeeEEKVKSLNKLRVKYEATIADMedrLKKEEKGRQELEKL 1069
Cdd:COG0497 267 AERLESALIELEEAASELRRYLDSLEfdpERLEEV-------EERLALLRRLARKYGVTVEEL---LAYAEELRAELAEL 336
|
250 260 270
....*....|....*....|....*....|..
gi 564328072 1070 KrrldgESSELQEQMMEQKQRAEELLIQLGRK 1101
Cdd:COG0497 337 E-----NSDERLEELEAELAEAEAELLEAAEK 363
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1498-1738 |
1.24e-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: 46.68 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1498 ALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLR 1577
Cdd:COG4942 8 ALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1578 LEVTVQALKAQHerdlqgrddagEERRRQLAKQLRDAEVE------------RDEERKQRALAM-----AARKKLELELE 1640
Cdd:COG4942 88 LEKEIAELRAEL-----------EAQKEELAELLRALYRLgrqpplalllspEDFLDAVRRLQYlkylaPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1641 ELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRSSREEmftLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQ 1720
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250
....*....|....*...
gi 564328072 1721 QDRDEMAEEVASGNLSKA 1738
Cdd:COG4942 234 AEAAAAAERTPAAGFAAL 251
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
862-1616 |
1.33e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.35 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 862 RQDEVLQARAQELQKVQELQQQS-AREVGELQGRVAQLEEERARLAEQLRAEAELcsEAEETRARLAARKQELELVVTEL 940
Cdd:TIGR00606 426 EQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQEL--RKAERELSKAEKNSLTETLKKEV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 941 EARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLL---------LEDQNSKLS 1011
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqLEDWLHSKS 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1012 KERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMED----------------RLKKE-EKGRQELEKL----- 1069
Cdd:TIGR00606 584 KEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDklfdvcgsqdeesdleRLKEEiEKSSKQRAMLagata 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1070 --------------------------KRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLL 1123
Cdd:TIGR00606 664 vysqfitqltdenqsccpvcqrvfqtEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKE 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1124 KSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRS---KREQEVTELKKTleEEA 1200
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDverKIAQQAAKLQGS--DLD 821
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1201 RTHEVAMQElRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGR 1280
Cdd:TIGR00606 822 RTVQQVNQE-KQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL 900
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1281 SSDSERAR------AEAAEKLQRAQVEL-ESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLalgsrvRA 1353
Cdd:TIGR00606 901 IREIKDAKeqdsplETFLEKDQQEKEELiSSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL------KQ 974
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1354 LEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEwRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTE-AVERLE 1432
Cdd:TIGR00606 975 KETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT-QKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQmQVLQMK 1053
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1433 RARRRLQQELD----DATVDLGQQKQLlstlEKKQRKFDQLLAEekaavlravedRERVEAEGREREARALSLTRALEEE 1508
Cdd:TIGR00606 1054 QEHQKLEENIDlikrNHVLALGRQKGY----EKEIKHFKKELRE-----------PQFRDAEEKYREMMIVMRTTELVNK 1118
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1509 QEAREElerqnRALRAELEALLSSK-DDVGKNVHELERArrvaEQAASDLRT-QVTELEDELTAAEDAKLRLEVTVQALK 1586
Cdd:TIGR00606 1119 DLDIYY-----KTLDQAIMKFHSMKmEEINKIIRDLWRS----TYRGQDIEYiEIRSDADENVSASDKRRNYNYRVVMLK 1189
|
810 820 830
....*....|....*....|....*....|
gi 564328072 1587 AQHERDLQGRDDAGEERRRQLAKQLRDAEV 1616
Cdd:TIGR00606 1190 GDTALDMRGRCSAGQKVLASLIIRLALAET 1219
|
|
| HAUS5 |
pfam14817 |
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. ... |
1097-1395 |
1.54e-04 |
|
HAUS augmin-like complex subunit 5; This family includes HAUS augmin-like complex subunit 5. The HAUS augmin-like complex contributes to mitotic spindle assembly, maintenance of chromosome integrity and completion of cytokinesis.
Pssm-ID: 464332 [Multi-domain] Cd Length: 643 Bit Score: 46.58 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1097 QLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEE---LEALRGELEDTLD 1173
Cdd:pfam14817 64 QDKGKAESRQSAAARRLELQKEIERLRAEISRLDKQLEARELELSREEAERERALDEISDSRHRqllLEAYDQQCEEARK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1174 S-----------TNAQQELRSKREQEVT-------ELKKTLEEEARTHEVA---------MQELRQRHSQALVELTEQL- 1225
Cdd:pfam14817 144 IlaedhqrlqgqLQQLRDAARKAEKEVVfgdskgsKSSVIALEPQVLRDVReacelraqfLQELLESSLKAYEGSGIHMn 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1226 -EQARRGKSVWEKTR-------------LSLEAEVSELKTELSSLQTS---RQEGEQKRRRLESQlqEVQGRSSDSERAR 1288
Cdd:pfam14817 224 rDQRRAVIQHWLSAVetlltshppshllQALEHLAAREKTAIQEETESldvRADAEALRFRYESN--HLLDVSSDESSDL 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1289 AEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSS----AESQLHDTQELLQEET--RAKLALGSRVRALEAEAAGLR 1362
Cdd:pfam14817 302 PSVRQLLERQWAHVQQFLNELAETRSRCQQLQARLQGlkdeAELESLGIGDTSQNDSllRQVLELELQAAGLAASRDTLR 381
|
330 340 350
....*....|....*....|....*....|....*.
gi 564328072 1363 EQMEE-EVVARER--AGRELQTTQAQLSEWRRRQEE 1395
Cdd:pfam14817 382 SECQQlNKLARERqeALRSLQKKWQRILDFRQLVSE 417
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1129-1398 |
1.59e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1129 AQAGLAEAQEDL--EAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQelrsKREQEVTELKKTLEEeartheva 1206
Cdd:PRK11281 24 SAFARAASNGDLptEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAQ-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1207 mqelrqrhsqalveLTEQLEQARRgksvwEKTRLSlEAEVSELKTELSSLQTsrqegeqkrRRLESQLQEVQgrssdser 1286
Cdd:PRK11281 92 --------------APAKLRQAQA-----ELEALK-DDNDEETRETLSTLSL---------RQLESRLAQTL-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1287 araeaaEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLAL-GSRVRALEAEAAGLREQM 1365
Cdd:PRK11281 135 ------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALrPSQRVLLQAEQALLNAQN 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1366 E--------------------EEVVAR-ERAGRELQTTQAQLSEWRRRQEEEAA 1398
Cdd:PRK11281 209 DlqrkslegntqlqdllqkqrDYLTARiQRLEHQLQLLQEAINSKRLTLSEKTV 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1738-1943 |
1.61e-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: 46.30 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1738 AATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEe 1817
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1818 dagARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLKR 1897
Cdd:COG4942 95 ---LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 564328072 1898 QLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRR 1943
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
849-1027 |
1.66e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 849 RLFIKVKPLLQVTRQD----EVLQARAQELQKVQELQQQSAREVGE--------------------------LQGRVAQL 898
Cdd:PRK04863 918 NALAQLEPIVSVLQSDpeqfEQLKQDYQQAQQTQRDAKQQAFALTEvvqrrahfsyedaaemlaknsdlnekLRQRLEQA 997
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 899 EEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGE-----EEECSRQLQSEKKRLQQHIQELETHLE 973
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDlgvpaDSGAEERARARRDELHARLSANRSRRN 1077
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564328072 974 AEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQ--NSKLSK------------ERRLLEERLAEFSSQ 1027
Cdd:PRK04863 1078 QLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQvvNAKAGWcavlrlvkdngvERRLHRRELAYLSAD 1145
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1254-1464 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1254 SSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAE--AAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLH 1331
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1332 DTQELLQEETRAKLALGS--RVRALEAEAAGLREQMEEEvvaRERAGRE---LQTTQAQLSEWRRR-QEEEAAVLEAGEE 1405
Cdd:COG3206 244 ALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAEL---SARYTPNhpdVIALRAQIAALRAQlQQEAQRILASLEA 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1406 ARRRAAREAETLAQRLAEKTEAVerleRARRRLQQELDDATVDLGQQKQLLSTLEKKQR 1464
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVARELYESLLQRLE 375
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
865-1166 |
2.11e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 865 EVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARV 944
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 945 GEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEF 1024
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1025 SSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEE 1104
Cdd:COG4372 184 ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1105 LQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRG 1166
Cdd:COG4372 264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
857-1094 |
2.11e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.57 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEErarLAEQLRAEAELCSEAEETRARLAARKQELELV 936
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQ---LLELTRVNELLKAKFSEDGTQKKMSSLSMELM 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 937 VTELEARVGEEEECSRQLQSEKKrlqqhIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRL 1016
Cdd:pfam15905 163 KLRNKLEAKMKEVMAKQEGMEGK-----LQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQ 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1017 LEE------RLAEFSSQAAEEEEKVK-SLNKLRVKYEATIADMEDRLKKEEKGRQEL----EKLKRRLDGESSELQEQMM 1085
Cdd:pfam15905 238 VEKykldiaQLEELLKEKNDEIESLKqSLEEKEQELSKQIKDLNEKCKLLESEKEELlreyEEKEQTLNAELEELKEKLT 317
|
....*....
gi 564328072 1086 EQKQRAEEL 1094
Cdd:pfam15905 318 LEEQEHQKL 326
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
670-694 |
2.31e-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: 2.31e-04
10 20
....*....|....*....|....*
gi 564328072 670 YKESLSRLMATLSNTNPSFVRCIVP 694
Cdd:cd01363 146 INESLNTLMNVLRATRPHFVRCISP 170
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
923-1239 |
2.44e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 46.07 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 923 RARLAARKQELELVVTEL-EARVGEEEECSRQLQSEKKR-LQQHIQELETHLEaeegarqklqlekvtteaKMKKFEEDL 1000
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALhELGVVHIEDLKEELSNERLRkLRSLLTKLSEALD------------------KLRSYLPKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1001 LLLEDQNSKLSKERrlLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKkeekgrqELEKLKRrLDGESSEL 1080
Cdd:PRK05771 70 NPLREEKKKVSVKS--LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIE-------RLEPWGN-FDLDLSLL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1081 QEQmmeqkqraEELLIQLGRKEEELQSALVRAEEEGGAraqllkslreaqaglAEAQEDLEAERVARAKAEKQRRDLGEE 1160
Cdd:PRK05771 140 LGF--------KYVSVFVGTVPEDKLEELKLESDVENV---------------EYISTDKGYVYVVVVVLKELSDEVEEE 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1161 LEALRGELEDTLDSTNAQQELRSKrEQEVTELKKtlEEEARTHEVAmqELRQRHSQALVELTEQLEQARRGKSVWEKTR 1239
Cdd:PRK05771 197 LKKLGFERLELEEEGTPSELIREI-KEELEEIEK--ERESLLEELK--ELAKKYLEELLALYEYLEIELERAEALSKFL 270
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1204-1929 |
2.54e-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: 46.12 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1204 EVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRssd 1283
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEE--- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1284 seraRAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQlhdtQELLQEETRAKLALGSRVRALEAEAAGLRE 1363
Cdd:pfam02463 238 ----RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEK----EKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1364 QMEEEVVARERAgrELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQQELD 1443
Cdd:pfam02463 310 VDDEEKLKESEK--EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1444 DATVDLGQQKQLLSTLEKKQRKFDQLL-AEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRAL 1522
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEAQLLLELArQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1523 RaELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEdeltAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEE 1602
Cdd:pfam02463 468 K-KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL----KVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1603 RRRQLAKQLRDAEVERDEE---RKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRS 1679
Cdd:pfam02463 543 VAISTAVIVEVSATADEVEerqKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRA 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1680 SReemFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELE 1759
Cdd:pfam02463 623 KV---VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQL 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1760 EEQNNSELLKDHYRKLVLQVETLTTELSaersfsaKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKlaqa 1839
Cdd:pfam02463 700 EIKKKEQREKEELKKLKLEAEELLADRV-------QEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSE---- 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1840 EEQLEQESRERilsgklvRRAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRE 1919
Cdd:pfam02463 769 LSLKEKELAEE-------REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
730
....*....|
gi 564328072 1920 LEDVTESAES 1929
Cdd:pfam02463 842 LKEEQKLEKL 851
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1174-1495 |
2.75e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 45.88 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1174 STNAQQELRSKREQEvtELKKTLEEEARthevamqELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEvselkTEL 1253
Cdd:pfam17380 285 SERQQQEKFEKMEQE--RLRQEKEEKAR-------EVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERE-----REL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1254 SSLQTSRQEGEQKRRRLESQLQEVQgRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDT 1333
Cdd:pfam17380 351 ERIRQEERKRELERIRQEEIAMEIS-RMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1334 QELLQEETRAklalgsrvraleaeaagLREQMEEEVvarERAGRELQTTQAQLSewRRRQEEE------AAVLEAGEEAR 1407
Cdd:pfam17380 430 EEARQREVRR-----------------LEEERAREM---ERVRLEEQERQQQVE--RLRQQEEerkrkkLELEKEKRDRK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1408 RRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQllSTLEKKQRKFDQLLAEEK---AAVLRAVEDR 1484
Cdd:pfam17380 488 RAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--RREAEEERRKQQEMEERRriqEQMRKATEER 565
|
330
....*....|.
gi 564328072 1485 ERVEAEGRERE 1495
Cdd:pfam17380 566 SRLEAMERERE 576
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1128-1338 |
2.77e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1128 EAQAGLAEAQEDLEAERVARAKAEKQRRDLgeELEALRGELEDTLdstNAQQELRSKREQEVTELKKTLEEEARTHE-VA 1206
Cdd:pfam17045 27 EGQTRALETRLDIREEELLSARNTLERKHK--EIGLLRQQLEELE---KGKQELVAKYEQQLQKLQEELSKLKRSYEkLQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1207 MQELRQRHSQA---------LVELTEQLEQARRGKSVWEKTRL-------SLEAEVSELKTELSSLQTS--RQEGEQKRR 1268
Cdd:pfam17045 102 RKQLKEAREEAksreedrseLSRLNGKLEEFRQKSLEWEQQRLqyqqqvaSLEAQRKALAEQSSLIQSAayQVQLEGRKQ 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1269 RLESQLQEVQGRSSDSERARaeaaEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQ 1338
Cdd:pfam17045 182 CLEASQSEIQRLRSKLERAQ----DSLCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELRMSQRQLQ 247
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1084-1295 |
3.57e-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: 44.15 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1084 MMEQKQRAeelLIQLgrkeEELQSALVRAEEEggaRAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEA 1163
Cdd:COG1579 1 AMPEDLRA---LLDL----QELDSELDRLEHR---LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1164 LRGELEdtlDSTNAQQELRSKREQevtelkktleeEARTHEVAMQELRQR-HSQALVELTEQLEQArrgksvwEKTRLSL 1242
Cdd:COG1579 71 VEARIK---KYEEQLGNVRNNKEY-----------EALQKEIESLKRRISdLEDEILELMERIEEL-------EEELAEL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564328072 1243 EAEVSELKTELsslqtsrqegEQKRRRLESQLQEVQGRSSDSERARAEAAEKL 1295
Cdd:COG1579 130 EAELAELEAEL----------EEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
857-1457 |
3.61e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVlqarAQELQKVQELQQQSAREVGELQGRVAQLEeeRARLAEQLRAEAELCSEAEetrARLAARKQELELV 936
Cdd:PRK10246 246 LNWLTRLDEL----QQEASRRQQALQQALAAEEKAQPQLAALS--LAQPARQLRPHWERIQEQS---AALAHTRQQIEEV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 937 VTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQlEKVTTEAKMKKFEEDLLLLEDQNSKLSKERR- 1015
Cdd:PRK10246 317 NTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRAQFSQQTSDREQLRQWQQQLTHAEQk 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1016 ---LLEERLAEFSSQAAEEEEKVKSLNKLRvkyeatiadmeDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAE 1092
Cdd:PRK10246 396 lnaLPAITLTLTADEVAAALAQHAEQRPLR-----------QRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALN 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1093 ELLIQLGRKEEELQSALVRAEEEggARAQLLKSLR-EAQAG------------LAEAQEDLE--AERVARAKAEKQRRDL 1157
Cdd:PRK10246 465 EMRQRYKEKTQQLADVKTICEQE--ARIKDLEAQRaQLQAGqpcplcgstshpAVEAYQALEpgVNQSRLDALEKEVKKL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1158 GEELEALRGELEdtldsTNAQQELRSKRE-QEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWE 1236
Cdd:PRK10246 543 GEEGAALRGQLD-----ALTKQLQRDESEaQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1237 ktRLSLEAEVSELKTELSSLQtsrQEGEQKRRRLESQLQEVQGRSSDSER------ARAEAAEKLQRAQVELESVSTALS 1310
Cdd:PRK10246 618 --RHELQGQIAAHNQQIIQYQ---QQIEQRQQQLLTALAGYALTLPQEDEeaswlaTRQQEAQSWQQRQNELTALQNRIQ 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1311 EAESkairLSKELSSAESQLHDTQELLQEETRaklalgsrvraleaeaaglreQMEEEVVARERagrELQTTQAQLSEWR 1390
Cdd:PRK10246 693 QLTP----LLETLPQSDDLPHSEETVALDNWR---------------------QVHEQCLSLHS---QLQTLQQQDVLEA 744
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1391 RRQEEEAAVLEAGEEARRRAAREAEtLAQRLAEktEAVERLERARRRLQQELDDATVDLGQQKQLLS 1457
Cdd:PRK10246 745 QRLQKAQAQFDTALQASVFDDQQAF-LAALLDE--ETLTQLEQLKQNLENQRQQAQTLVTQTAQALA 808
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
859-1467 |
3.73e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.56 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQA---------------------------RAQELQKVQELQQQSAREVGELQGRVAQLeeERARLAEQLRA 911
Cdd:PRK10246 217 QVQSLTASLQVltdeekqlltaqqqqqqslnwltrldeLQQEASRRQQALQQALAAEEKAQPQLAAL--SLAQPARQLRP 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 912 EAELCSEAEetrARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQlEKVTTEA 991
Cdd:PRK10246 295 HWERIQEQS---AALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNN-ELAGWRA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 992 KMKKFEEDLLLLEDQNSKLSKERR----LLEERLAEFSSQAAEEEEKVKSLNKLRvkyeatiadmeDRLKKEEKGRQELE 1067
Cdd:PRK10246 371 QFSQQTSDREQLRQWQQQLTHAEQklnaLPAITLTLTADEVAAALAQHAEQRPLR-----------QRLVALHGQIVPQQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1068 KLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEggARAQLLKSLR-EAQAG------------LA 1134
Cdd:PRK10246 440 KRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQE--ARIKDLEAQRaQLQAGqpcplcgstshpAV 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1135 EAQEDLE--AERVARAKAEKQRRDLGEELEALRGELeDTLDSTNAQQELRSKR----EQEVTELKKTLEE---------- 1198
Cdd:PRK10246 518 EAYQALEpgVNQSRLDALEKEVKKLGEEGAALRGQL-DALTKQLQRDESEAQSlrqeEQALTQQWQAVCAslnitlqpqd 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1199 -------EARTHEVAMQELRQRHSQALvELTEQLEQARRGKSVWEKTRLSLEAEVSELKTEL------SSLQTSRQEGEQ 1265
Cdd:PRK10246 597 diqpwldAQEEHERQLRLLSQRHELQG-QIAAHNQQIIQYQQQIEQRQQQLLTALAGYALTLpqedeeASWLATRQQEAQ 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1266 KRRRLESQLQEVQgrssdseraraeaaEKLQRAQVELESV---STALSEAESKAI----RLSKELSSAESQLHDTQE-LL 1337
Cdd:PRK10246 676 SWQQRQNELTALQ--------------NRIQQLTPLLETLpqsDDLPHSEETVALdnwrQVHEQCLSLHSQLQTLQQqDV 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1338 QEETRAKLALGSRVRALEA-----EAAGLREQMEEEVVAR-----ERAGRELQTTQAQLSEWRRRQEEEAAvleaGEEAR 1407
Cdd:PRK10246 742 LEAQRLQKAQAQFDTALQAsvfddQQAFLAALLDEETLTQleqlkQNLENQRQQAQTLVTQTAQALAQHQQ----HRPDG 817
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1408 RRAAREAETLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFD 1467
Cdd:PRK10246 818 LDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1126-1329 |
3.88e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1126 LREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEAR---- 1201
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalyr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1202 ---------------------THEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSR 1260
Cdd:COG3883 98 sggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1261 QEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQ 1329
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
901-1400 |
3.97e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.62 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 901 ERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARV---------GEEEECSRQLQSEKKRLQQHIQELETH 971
Cdd:COG3899 733 ELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARAlaalaalrhGNPPASARAYANLGLLLLGDYEEAYEF 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 972 LEAEEGARQKLQLEKVTTEAKMkKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIAD 1051
Cdd:COG3899 813 GELALALAERLGDRRLEARALF-NLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAA 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1052 MEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQA 1131
Cdd:COG3899 892 AAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAA 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1132 GLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDStnAQQELRSKREQEVTELKKTLEEEARTHEVAMQELR 1211
Cdd:COG3899 972 LAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAA--LAAALLAAALAALAAAAAAAALLAAAAALALLAAL 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1212 QRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEA 1291
Cdd:COG3899 1050 AAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAA 1129
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1292 AEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVA 1371
Cdd:COG3899 1130 RAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAAL 1209
|
490 500
....*....|....*....|....*....
gi 564328072 1372 RERAGRELQTTQAQLSEWRRRQEEEAAVL 1400
Cdd:COG3899 1210 LALALLALEAAALLLLLLLAALALAAALL 1238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1026-1261 |
4.23e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1026 SQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEEL 1105
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1106 Q---------SALVRAEEEGGA--RAQLLKSLREAQAGLAEAQEDLEAE-RVARAKAEKQRrdlgEELEALRGELEDTLD 1173
Cdd:COG3883 96 YrsggsvsylDVLLGSESFSDFldRLSALSKIADADADLLEELKADKAElEAKKAELEAKL----AELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1174 STNAQQElrskreqEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTEL 1253
Cdd:COG3883 172 ELEAQQA-------EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
....*...
gi 564328072 1254 SSLQTSRQ 1261
Cdd:COG3883 245 SAAGAGAA 252
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
890-1194 |
4.24e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 890 ELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELE 969
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 970 THLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEErlaefssqaaeeeekvkslnklrvkyeatI 1049
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEK-----------------------------I 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1050 ADMEDRLKKEEKGRQELEKLKRrLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEeggaraqLLKSLREA 1129
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKE-LRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADE-------LRKEADEL 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564328072 1130 QAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLdSTNAQQELRSKREQEVTELKK 1194
Cdd:COG1340 215 HKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK-REKEKEELEEKAEEIFEKLKK 278
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
896-1255 |
4.26e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 896 AQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAE 975
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 976 EGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDR 1055
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1056 LKKEEKGRQELEKLKRRldgesSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAE 1135
Cdd:COG4372 166 LAALEQELQALSEAEAE-----QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1136 AQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHS 1215
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 564328072 1216 QALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSS 1255
Cdd:COG4372 321 LLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLS 360
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1086-1290 |
4.51e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1086 EQKQRAEELLIQLGRKEEELqsalvraeeeggarAQLLKSLREAQAGLAEAQEDLEAERVARAKAEK----QRRDLGEEL 1161
Cdd:PRK11637 65 QQQQQRASLLAQLKKQEEAI--------------SQASRKLRETQNTLNQLNKQIDELNASIAKLEQqqaaQERLLAAQL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1162 EAL--RGE---LEDTLDSTNAQQE---------LRSKREQEVTELKKTLEeearthEVAMQ--ELRQRHSQALVELTEQL 1225
Cdd:PRK11637 131 DAAfrQGEhtgLQLILSGEESQRGerilayfgyLNQARQETIAELKQTRE------ELAAQkaELEEKQSQQKTLLYEQQ 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564328072 1226 EQARRgksvwektrlsLEAEVSELKTELSSLQTSRQEGEQK---RRRLESQLQEVQGRSSDSERARAE 1290
Cdd:PRK11637 205 AQQQK-----------LEQARNERKKTLTGLESSLQKDQQQlseLRANESRLRDSIARAEREAKARAE 261
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1074-1394 |
5.09e-04 |
|
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: 44.89 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1074 DGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEaERVARAKAE-K 1152
Cdd:pfam07888 12 ESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELE-SRVAELKEElR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1153 QRRDLGEELE-------ALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQL 1225
Cdd:pfam07888 91 QSREKHEELEekykelsASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1226 EQARRGKSVWEKTrlslEAEVSELKTELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQraqvELESV 1305
Cdd:pfam07888 171 AERKQLQAKLQQT----EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE----ELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1306 STALSEAESKAIRLSKELSSAESQLHDTQ-----------ELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARER 1374
Cdd:pfam07888 243 QERLNASERKVEGLGEELSSMAAQRDRTQaelhqarlqaaQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEK 322
|
330 340
....*....|....*....|
gi 564328072 1375 AGRELQTTQAQLSEWRRRQE 1394
Cdd:pfam07888 323 LSAELQRLEERLQEERMERE 342
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1322-1824 |
5.33e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.23 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1322 ELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARE--------RAGRELQTTQAQLSEWRRRQ 1393
Cdd:COG3899 733 ELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRhgnppasaRAYANLGLLLLGDYEEAYEF 812
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1394 EEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVERLERARRRLQ--QELDDATVDLGQQKQLLSTLEKKQRKFDQLLA 1471
Cdd:COG3899 813 GELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEagLETGDAALALLALAAAAAAAAAAAALAAAAAA 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1472 EEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAE 1551
Cdd:COG3899 893 AARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAAL 972
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1552 QAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAA 1631
Cdd:COG3899 973 AAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAA 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1632 RKKLELELEELKAQTSAAGQGKEEAVkQLKKMQAQMKELWREVEETRSSREEMFTLSRESEKRLKGLEAEVLRLQEELAA 1711
Cdd:COG3899 1053 AAAAAAAAALAAAAALLAAAAAAAAA-AAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARA 1131
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1712 SDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERS 1791
Cdd:COG3899 1132 AAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLA 1211
|
490 500 510
....*....|....*....|....*....|...
gi 564328072 1792 FSAKAESGRQQLERQIQELRARLGEEDAGARAR 1824
Cdd:COG3899 1212 LALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1047-1364 |
5.36e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.29 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1047 ATIADME---DRLKKEEKGRQELEKLKRRLDGESSELQEqmmeqkqrAEELLIQLGRKEeelqSALVRAEEEGGARAQLL 1123
Cdd:PRK11281 60 LVQQDLEqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQ--------AQAELEALKDDN----DEETRETLSTLSLRQLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1124 KSLREAQAGLAEAQEDLEaervarakaekqrrDLGEELEALRGELEdtldstNAQQEL--RSKREQEVTELKKTLEEEAR 1201
Cdd:PRK11281 128 SRLAQTLDQLQNAQNDLA--------------EYNSQLVSLQTQPE------RAQAALyaNSQRLQQIRNLLKGGKVGGK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1202 THEVAMQELRQRHsQALVELteQLEQARRgksvwektrlslEAEVSELKTELssLQTSRQEGEQKRRRLESQLQEVQGRS 1281
Cdd:PRK11281 188 ALRPSQRVLLQAE-QALLNA--QNDLQRK------------SLEGNTQLQDL--LQKQRDYLTARIQRLEHQLQLLQEAI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1282 SDSERARAEA-AEKLQRAQVELESVSTALSEAESKA-IRLSKELSSAESQLHdtqELLQEETRAKLALGsrvRALEAEAA 1359
Cdd:PRK11281 251 NSKRLTLSEKtVQEAQSQDEAARIQANPLVAQELEInLQLSQRLLKATEKLN---TLTQQNLRVKNWLD---RLTQSERN 324
|
....*
gi 564328072 1360 gLREQ 1364
Cdd:PRK11281 325 -IKEQ 328
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
881-1068 |
5.46e-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: 43.76 E-value: 5.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 881 QQQSAREVGELQGRVAQLEEERARLAEQLraeAELCSEAEETRARLAARKQELElvvtelearvgeeeecsrQLQSEKKR 960
Cdd:COG1579 5 DLRALLDLQELDSELDRLEHRLKELPAEL---AELEDELAALEARLEAAKTELE------------------DLEKEIKR 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 961 LQQHIQELETHLEaeegaRQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKS--- 1037
Cdd:COG1579 64 LELEIEEVEARIK-----KYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAElea 138
|
170 180 190
....*....|....*....|....*....|..
gi 564328072 1038 -LNKLRVKYEATIADMEDRLKKEEKGRQELEK 1068
Cdd:COG1579 139 eLEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1071-1222 |
5.87e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.34 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1071 RRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQL---LKSLREAQAGLAEAQEDLEAERVAR 1147
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLraaQAAVKAAQAQLAQAQIDLARRRVLA 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1148 AKAEKQRRDLgEELEALRGELEDTLDSTNAQQE-LRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELT 1222
Cdd:pfam00529 134 PIGGISRESL-VTAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLE 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1688-1921 |
6.06e-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: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1688 SRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDemaeeVASGNLSKAATLEEKRQLEGRLGQLEEELEEEQNNSEL 1767
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAA 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1768 LKdhyRKLVLQVETLTTELSAERSFSAKAEsgRQQLERQIQELRARLGEEDAgararqkmLIAALESKLAQAEEQLEQEs 1847
Cdd:COG3206 245 LR---AQLGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARYTPNHP--------DVIALRAQIAALRAQLQQE- 310
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1848 rerilsgklvrrAEKRLKEVVLQVDEERRVADQLRDQLEKSNLRLKQLkrqleeaeeeaSRAQAGRRRLQRELE 1921
Cdd:COG3206 311 ------------AQRILASLEAELEALQAREASLQAQLAQLEARLAEL-----------PELEAELRRLEREVE 361
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1439-1885 |
6.52e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.96 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1439 QQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQ 1518
Cdd:COG4995 7 LALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1519 NRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDD 1598
Cdd:COG4995 87 LALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1599 AGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETR 1678
Cdd:COG4995 167 ALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1679 SSREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEEL 1758
Cdd:COG4995 247 AAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1759 EEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKLAQ 1838
Cdd:COG4995 327 LAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAA 406
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 564328072 1839 AEEQLEQESRERILSGKLVRRAEKRLKEVV--LQVDEERRVADQLRDQL 1885
Cdd:COG4995 407 QLLRLLLAALALLLALAAYAAARLALLALIeyIILPDRLYAFVQLYQLL 455
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
882-1170 |
7.96e-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: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 882 QQSAREVGELQGRVAQLEEERARLAEQLRAeaelcseaeeTRARLAARKQELELVV----TELEARVGEEEECSRQLQSE 957
Cdd:COG3096 839 AALRQRRSELERELAQHRAQEQQLRQQLDQ----------LKEQLQLLNKLLPQANlladETLADRLEELREELDAAQEA 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 958 KKRLQQH---IQELETHLEA--------EEGARQKLQLEKVTTEAKMKKFE-------------EDLLLLEDQNSKLSKE 1013
Cdd:COG3096 909 QAFIQQHgkaLAQLEPLVAVlqsdpeqfEQLQADYLQAKEQQRRLKQQIFAlsevvqrrphfsyEDAVGLLGENSDLNEK 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1014 rrlLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLkkeEKGRQELEKLKRRLD---------------GESS 1078
Cdd:COG3096 989 ---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELEelgvqadaeaeerarIRRD 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1079 ELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAE-----AQEDLEAERVARA----K 1149
Cdd:COG3096 1063 ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAvlrlaRDNDVERRLHRRElaylS 1142
|
330 340
....*....|....*....|.
gi 564328072 1150 AEKQRRDLGEELEALRGELED 1170
Cdd:COG3096 1143 ADELRSMSDKALGALRLAVAD 1163
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
873-1049 |
7.99e-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: 43.37 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 873 ELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLraeaelcSEAEETRARLAARKQELELVVTELEARVGEEEEcsR 952
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARL-------EAAKTELEDLEKEIKRLELEIEEVEARIKKYEE--Q 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 953 QLQSEKKRLQQHIQElethlEAEEGARQKLQLEKVTTEAkMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEE 1032
Cdd:COG1579 82 LGNVRNNKEYEALQK-----EIESLKRRISDLEDEILEL-MERIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
|
170
....*....|....*..
gi 564328072 1033 EKVKSLNKLRVKYEATI 1049
Cdd:COG1579 156 AELEELEAEREELAAKI 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1211-1612 |
8.66e-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: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1211 RQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKRRRLES--QLQEVQGRSSDserAR 1288
Cdd:COG3096 280 RRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalRQQEKIERYQE---DL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1289 AEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALE-----AEAAGLRE 1363
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQALEkaralCGLPDLTP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1364 QMEEEVVARERAGRELQT-------TQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEaverlerarr 1436
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATeevleleQKLSVADAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRS---------- 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1437 rlQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTraleeeqEAREELE 1516
Cdd:COG3096 507 --QQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE-------EQAAEAV 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1517 RQNRALRAELEALLSSKDDVGKnvheLERARRVAEQAASDLRTQVTEledELTAAEDaklrLEVTVQALkAQHERDLQGR 1596
Cdd:COG3096 578 EQRSELRQQLEQLRARIKELAA----RAPAWLAAQDALERLREQSGE---ALADSQE----VTAAMQQL-LEREREATVE 645
|
410
....*....|....*.
gi 564328072 1597 DDAGEERRRQLAKQLR 1612
Cdd:COG3096 646 RDELAARKQALESQIE 661
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
875-1155 |
8.98e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 875 QKVQELQQqsarEVGELQGRVAQLEEERARLAEQLRAEAELCSEA----EETRARLAARKQELELV---VTELEARVGEE 947
Cdd:PRK11637 47 DQLKSIQQ----DIAAKEKSVRQQQQQRASLLAQLKKQEEAISQAsrklRETQNTLNQLNKQIDELnasIAKLEQQQAAQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 948 EE-CSRQLQSeKKRLQQHiQELETHLEAEEGARQK--LQLEKVTTEAKMKKFEEdlllLEDQNSKLSKERRLLEERLAEF 1024
Cdd:PRK11637 123 ERlLAAQLDA-AFRQGEH-TGLQLILSGEESQRGEriLAYFGYLNQARQETIAE----LKQTREELAAQKAELEEKQSQQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1025 SSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEekgrqeleklkrrldgesselQEQMMEQKQraeelliqlgrKEEE 1104
Cdd:PRK11637 197 KTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKD---------------------QQQLSELRA-----------NESR 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 564328072 1105 LQSALVRAEEEGGARAQllkslREAQaglaeaqedlEAERVARAKAEKQRR 1155
Cdd:PRK11637 245 LRDSIARAEREAKARAE-----REAR----------EAARVRDKQKQAKRK 280
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
859-1164 |
9.63e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVT 938
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 939 ELEARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMkkfeedllLLEDQNSKLSKERRLLE 1018
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE--------LLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1019 ERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQL 1098
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1099 GRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEAL 1164
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1653-1941 |
9.67e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 9.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1653 KEEAVKQLKKMQAQMKELWREVEETRSSR----EEMFTLSRESEKRLKGLEAEVLRLQEElaasDRARRQAQQDRDEMAE 1728
Cdd:pfam17380 297 EQERLRQEKEEKAREVERRRKLEEAEKARqaemDRQAAIYAEQERMAMERERELERIRQE----ERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1729 EVasgnlSKAATLEEKRQLEGRLGQLEEELEEEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQ 1808
Cdd:pfam17380 373 EI-----SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERARE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1809 ELRARLGEEDagaRARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRA-EKRLKEVVLQVDEERRVADQLRDQLEK 1887
Cdd:pfam17380 448 MERVRLEEQE---RQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEE 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1888 snlrlkqlkRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMnREVTTLRNRL 1941
Cdd:pfam17380 525 ---------RQKAIYEEERRREAEEERRKQQEMEERRRIQEQM-RKATEERSRL 568
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
892-1059 |
9.80e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 892 QGRVAQLEEERARLAEQLRAEAELCSEAEETRArlaarKQELELVVTELEARVGEEEecsRQLQSEKKRLQQHIQELETH 971
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEA-----KEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 972 LEAEEGARQKLQLEKVTTEAKMKKFEEdllLLEDQNSKLSKERRLLeERLAEFSSQAAEEE--EKVKSlnKLRVKYEATI 1049
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEK---KEEELEELIEEQLQEL-ERISGLTAEEAKEIllEKVEE--EARHEAAVLI 175
|
170
....*....|
gi 564328072 1050 ADMEDRLKKE 1059
Cdd:PRK12704 176 KEIEEEAKEE 185
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1788-1883 |
1.02e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1788 AERSFSAKAESGRQQLERQIQELRAR--LGEEDAGARARQKMLIAALESKLAQAEEQLEQ-----ESRERILSGKLVRRA 1860
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSqaLAEAQQQELVALEGLAAELEEKQQELEAQLEQlqekaAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|....
gi 564328072 1861 EKRLKEVVLQVDEERRVAD-QLRD 1883
Cdd:PRK11448 223 DQAAKRLELSEEETRILIDqQLRK 246
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
880-1139 |
1.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 880 LQQQSAREVGELQGRVAQLEEERARLAEQLraeaelcseaEETRARLAARKQELELVvtelearvgeeeecsrQLQSEKK 959
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKEL----------EEAEAALEEFRQKNGLV----------------DLSEEAK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 960 RLQQHIQELEThleaeegARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRL--LEERLAEFSSQAAEEEEKVKS 1037
Cdd:COG3206 216 LLLQQLSELES-------QLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIqqLRAQLAELEAELAELSARYTP 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1038 LNKLRVKYEATIADMEDRLKKE-EKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLiQLGRKEEELQSALVRAEEeg 1116
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEaQRILASLEAELEALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEVARE-- 365
|
250 260
....*....|....*....|...
gi 564328072 1117 gARAQLLKSLREAQAGLAEAQED 1139
Cdd:COG3206 366 -LYESLLQRLEEARLAEALTVGN 387
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
859-1337 |
1.29e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 859 QVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaelcsEAEETRARLAARKQELELVVT 938
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERER-------EATVERDELAARKQALESQIE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 939 ELEARVGEEeecSRQLQSEKKR----LQQHIQELETHLEAEE------GARQKLQLEKVTT-EAKMKKFE---EDLLLLE 1004
Cdd:COG3096 662 RLSQPGGAE---DPRLLALAERlggvLLSEIYDDVTLEDAPYfsalygPARHAIVVPDLSAvKEQLAGLEdcpEDLYLIE 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1005 ------DQNSKLSKE--------------------------RRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADM 1052
Cdd:COG3096 739 gdpdsfDDSVFDAEEledavvvklsdrqwrysrfpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAF 818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1053 EDRLKK------EEKGRQELEKLKRR---LDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARaqll 1123
Cdd:COG3096 819 SQFVGGhlavafAPDPEAELAALRQRrseLERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADR---- 894
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1124 ksLREAQAGLAEAQEdleaervarAKAEKQRRdlGEELEALRgELEDTLDSTNAQQElrsKREQEVTELKKTLeEEARTH 1203
Cdd:COG3096 895 --LEELREELDAAQE---------AQAFIQQH--GKALAQLE-PLVAVLQSDPEQFE---QLQADYLQAKEQQ-RRLKQQ 956
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1204 EVAMQELRQR--------------HSQALVE-LTEQLEQARRGKSvweKTRLSLE---AEVSELKTELSSLQTSRQEGEQ 1265
Cdd:COG3096 957 IFALSEVVQRrphfsyedavgllgENSDLNEkLRARLEQAEEARR---EAREQLRqaqAQYSQYNQVLASLKSSRDAKQQ 1033
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564328072 1266 KRRRLESQLQE--VQGRSSDSERARAEAAE---KLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELL 1337
Cdd:COG3096 1034 TLQELEQELEElgVQADAEAEERARIRRDElheELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1129-1385 |
1.31e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1129 AQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEearthevamq 1208
Cdd:COG3883 7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1209 eLRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAE-VSELkteLSSLQTSRQEGEQKRRRLESQLQEVQgrssDSERA 1287
Cdd:COG3883 77 -AEAEIEERREELGERARALYRSGGSVSYLDVLLGSEsFSDF---LDRLSALSKIADADADLLEELKADKA----ELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1288 RAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEE 1367
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*...
gi 564328072 1368 EVVARERAGRELQTTQAQ 1385
Cdd:COG3883 229 AAAAAAAAAAAAAAAASA 246
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
872-1155 |
1.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 872 QELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRaeaELCSEAEETRARlaaRKQELELVvtelearvgeeeecs 951
Cdd:COG1340 15 EKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVK---ELREEAQELREK---RDELNEKV--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 952 RQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEdlLLLEDQNSKLSKERrllEERLAEFSSQAAEE 1031
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIER--LEWRQQTEVLSPEE---EKELVEKIKELEKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1032 EEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKrrldGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVR 1111
Cdd:COG1340 149 LEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELA----EEAQELHEEMIELYKEADELRKEADELHKEIVEAQEK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 564328072 1112 AEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRR 1155
Cdd:COG1340 225 ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEK 268
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1012-1227 |
1.52e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 43.53 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1012 KERRLLEERLAEFSSQAAEEEEK-------VKSLNKLRVKyeatiADMEDRLKKE-------EKGRQELEKLKRRLDGES 1077
Cdd:COG0497 165 RAWRALKKELEELRADEAERAREldllrfqLEELEAAALQ-----PGEEEELEEErrrlsnaEKLREALQEALEALSGGE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1078 SELQEQMmeqkQRAEELLIQLGRKEEELQSALVRAEEeggARAQLlkslREAQAGLAEAQEDLEA---------ERVARA 1148
Cdd:COG0497 240 GGALDLL----GQALRALERLAEYDPSLAELAERLES---ALIEL----EEAASELRRYLDSLEFdperleeveERLALL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1149 KAEKQR-RDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARthevAMQELRQRHSQALVE-LTEQLE 1226
Cdd:COG0497 309 RRLARKyGVTVEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAE----KLSAARKKAAKKLEKaVTAELA 384
|
.
gi 564328072 1227 Q 1227
Cdd:COG0497 385 D 385
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1120-1326 |
1.55e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.32 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1120 AQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDT---LDSTNAQQELRSKREQEVTELKKTL 1196
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTeerLAEALEKLEEAEKAADESERGRKVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1197 EEEARTHEVAMQELRQRHSQA-----------------LVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTS 1259
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLKEAkeiaeeadrkyeevarkLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLEAS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564328072 1260 RQEGEQKRRRLESQLQEVQGRSSDSErARAEAAE-KLQRAQVELESVSTALSEAESKAIRLSKELSSA 1326
Cdd:pfam00261 164 EEKASEREDKYEEQIRFLTEKLKEAE-TRAEFAErSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
865-984 |
1.82e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 865 EVLQARAQELQKVQElqqQSAREVGELQGRVAQLEEERARLAEQLRA-EAELCSEAEET-RARLAARKQELELVVTELEA 942
Cdd:PRK00409 519 NELIASLEELERELE---QKAEEAEALLKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEaQQAIKEAKKEADEIIKELRQ 595
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 564328072 943 RVGEEEEC--SRQLQSEKKRLQQHIQELETHLEAEEGARQKLQL 984
Cdd:PRK00409 596 LQKGGYASvkAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1176-1345 |
1.89e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1176 NAQQELRSKREQEVTELKKTLEEEARTHEvamQELRQRHSQaLVELTEQLEQarrgksvwektrlsleaEVSELKTELSS 1255
Cdd:PRK12704 46 EAKKEAEAIKKEALLEAKEEIHKLRNEFE---KELRERRNE-LQKLEKRLLQ-----------------KEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1256 LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAqvelesvsTALSEAESKAIRLSKelssAESQL-HDTQ 1334
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI--------SGLTAEEAKEILLEK----VEEEArHEAA 172
|
170
....*....|..
gi 564328072 1335 ELLQE-ETRAKL 1345
Cdd:PRK12704 173 VLIKEiEEEAKE 184
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1106-1579 |
2.22e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 43.08 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1106 QSALVRAEEEGGARAQLLKSLRE-AQAGLAEAQEDLEAER---------VARAKAEKQRRDLGEELEALRGELEDTLDst 1175
Cdd:COG3903 453 KSLLEVEGGGGGPRYRLLETVREyAAERLAEAGERAAARRrhadyylalAERAAAELRGPDQLAWLARLDAEHDNLRA-- 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1176 nAQQELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSS 1255
Cdd:COG3903 531 -ALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAA 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1256 LQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQE 1335
Cdd:COG3903 610 AAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAA 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1336 LLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAE 1415
Cdd:COG3903 690 AAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAA 769
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1416 TLAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGRERE 1495
Cdd:COG3903 770 AALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAA 849
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1496 ARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAK 1575
Cdd:COG3903 850 AAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAA 929
|
....
gi 564328072 1576 LRLE 1579
Cdd:COG3903 930 AAAA 933
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1166-1335 |
2.40e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 43.13 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1166 GELEDTLDSTNAQQELRSKREQEVTEL-KKTLEEEARTHEVAMQELR---QRHSQALVELTEQLEQARRGKSVWEkTRL- 1240
Cdd:pfam05911 669 GPLVSGSNDLKTEENKRLKEEFEQLKSeKENLEVELASCTENLESTKsqlQESEQLIAELRSELASLKESNSLAE-TQLk 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1241 -------SLEAEVSELKTELSSLQtsrqegeQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRaqVELESVSTALSEAE 1313
Cdd:pfam05911 748 cmaesyeDLETRLTELEAELNELR-------QKFEALEVELEEEKNCHEELEAKCLELQEQLER--NEKKESSNCDADQE 818
|
170 180
....*....|....*....|..
gi 564328072 1314 SKAIRLSKELSSAESQLHDTQE 1335
Cdd:pfam05911 819 DKKLQQEKEITAASEKLAECQE 840
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
902-1089 |
2.55e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.63 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 902 RARLAEQLRAEAELCSEAEETRARLAARKQELElvvteleARVGEEEECSRQLQSEKKRLQQHIQELETHLEAEEGARQK 981
Cdd:pfam15709 339 RAERAEMRRLEVERKRREQEEQRRLQQEQLERA-------EKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 982 LQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEE---RLAEFSSQAAEEEEKVKSLNKlrvkyEATIADMEDRLKK 1058
Cdd:pfam15709 412 LQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAekqRQKELEMQLAEEQKRLMEMAE-----EERLEYQRQKQEA 486
|
170 180 190
....*....|....*....|....*....|.
gi 564328072 1059 EEKGRQELEKLKRRLDGESSELQEQMMEQKQ 1089
Cdd:pfam15709 487 EEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
980-1495 |
2.59e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.70 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 980 QKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKyeatiadmedrLKKE 1059
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSK-----------INSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1060 EKGRQElekLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSALVRAEEEGGARAQLLKSLREAQAGLAEAQED 1139
Cdd:TIGR04523 112 IKNDKE---QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1140 LEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLEEEARTHEVAMQ--ELRQRHSQA 1217
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQlkDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1218 LVELTEQLEQArrgksvwEKTRLSLEAEVSELKTELSSLQTSRQEGEQKrrRLESQLQEVQGRSSDSERARAEAAEKLQR 1297
Cdd:TIGR04523 269 LSEKQKELEQN-------NKKIKELEKQLNQLKSEISDLNNQKEQDWNK--ELKSELKNQEKKLEEIQNQISQNNKIISQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1298 AQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAE---AAGLREQMEEEVVARER 1374
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnQEKLNQQKDEQIKKLQQ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1375 AGRELQTTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAVerlERARRRLQQELDDATVDLGQQKQ 1454
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL---SRSINKIKQNLEQKQKELKSKEK 496
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 564328072 1455 LLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGRERE 1495
Cdd:TIGR04523 497 ELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
866-1327 |
2.87e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 866 VLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVG 945
Cdd:COG5278 70 LLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 946 EEEECsRQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFS 1025
Cdd:COG5278 150 LMDEI-RARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1026 SQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEEL 1105
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1106 QSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKR 1185
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1186 EQEVTELKKTLEEEARTHEVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQ 1265
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1266 KRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAE 1327
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1417-1626 |
3.11e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1417 LAQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLA--EEKAAVLRAVEDRERVEAEGRER 1494
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAelEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1495 EARALSLTRALEEEQEAREELERQNRA--LRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAE 1572
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1573 DAKLRLEVTVQALKAQhERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRA 1626
Cdd:COG4942 192 ALKAERQKLLARLEKE-LAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1216-1350 |
3.73e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1216 QALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLqtsrqegEQKRRRLESQLQEVQGrssdserARAEAAEKL 1295
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA-------EAERSRLQALLAELAG-------AGAAAEGRA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1296 QRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQ------EETRAKLA-LGSR 1350
Cdd:PRK09039 119 GELAQELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDasekrdRESQAKIAdLGRR 180
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1129-1377 |
3.80e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1129 AQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKTLE---EEARTHEV 1205
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEerrEELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1206 AMQE-------------------------LRQRHSQALVELTEQLEQARRgksvwektrlSLEAEVSELKTELSSLQTSR 1260
Cdd:COG3883 94 ALYRsggsvsyldvllgsesfsdfldrlsALSKIADADADLLEELKADKA----------ELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1261 QEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEE 1340
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 564328072 1341 TRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGR 1377
Cdd:COG3883 244 ASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAAS 280
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
863-1051 |
4.54e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.72 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 863 QDEVLQARAQELQKVQELQQQS--AREVGELQGRVAQLEEER-ARLAEQLRAEAELCSEAEETRARLAARKQELELVVTE 939
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEelQQKQAAEQERLKQLEKERlAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 940 LEARVGEEEECSRQLQSEKKRL----QQHIQELETHLEAEEGARQKLQLE---KVTTEAKMKKFEEDlllledqNSKLSK 1012
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKaeaeAAKKAAAEAKKKAEAEAAAKAAAEakkKAEAEAKKKAAAEA-------KKKAAA 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 564328072 1013 ERRLLEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIAD 1051
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
849-957 |
4.60e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 849 RLFIKVKP--LLQVTRQDEVLQARAQELQKvqELQQQSAREVGELQGRVAQLEEERARLAEQLRAEAELCSEAEETRARL 926
Cdd:COG0542 403 RMEIDSKPeeLDELERRLEQLEIEKEALKK--EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110
....*....|....*....|....*....|.
gi 564328072 927 AARKQELELVVTELEARVGEEEECSRQLQSE 957
Cdd:COG0542 481 EQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1419-1710 |
5.01e-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: 42.03 E-value: 5.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1419 QRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLStleKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARA 1498
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAM---ERERELERIRQEERKRELERIRQEEIAMEISRMRELER 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1499 LSLTRALeeeqeareelerQNRALRAELEALLSSK-------DDVGKNVHELERARRVAEQAAS-DLRTQVTELEDELTA 1570
Cdd:pfam17380 383 LQMERQQ------------KNERVRQELEAARKVKileeerqRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1571 AEDAKLRLEVTVQALKAQH-ERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAA 1649
Cdd:pfam17380 451 VRLEEQERQQQVERLRQQEeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564328072 1650 GQGKEEAVKQLKKMQAQMKELWREVEETRSSREE---MFTLSRESEKRLKGLEAEVLRLQEELA 1710
Cdd:pfam17380 531 EEERRREAEEERRKQQEMEERRRIQEQMRKATEErsrLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
915-1255 |
5.10e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.97 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 915 LCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELET--HLEAEEGARQKLQLEKVTTEAK 992
Cdd:pfam13166 87 LGEESIEIQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLDECWKKIKrkKNSALSEALNGFKYEANFKSRL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 993 MKKFEEDLlllEDQNSKLSKERRllEERLAEFSSQAAEEEEKVKSLNKLRVKYEATIADMEDRLKKEekgrQELEKLKRR 1072
Cdd:pfam13166 167 LREIEKDN---FNAGVLLSDEDR--KAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQKVIGKS----SAIEELIKN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1073 LD-----GESSELQEQMMEQ---------KQRAEELLIQLGRKEEELQSAL-VRAEEEGGARAQLLKSLreaQAGLAEAQ 1137
Cdd:pfam13166 238 PDladwvEQGLELHKAHLDTcpfcgqplpAERKAALEAHFDDEFTEFQNRLqKLIEKVESAISSLLAQL---PAVSDLAS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1138 EDLEAERvARAKAEKQRRDLGEELEALRGELE-----------------------DTLDSTNAQQELRSKREQEVTELKK 1194
Cdd:pfam13166 315 LLSAFEL-DVEDIESEAEVLNSQLDGLRRALEakrkdpfksieldsvdakiesinDLVASINELIAKHNEITDNFEEEKN 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1195 TLEEEARTHEVA-MQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSS 1255
Cdd:pfam13166 394 KAKKKLRLHLVEeFKSEIDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEAQLRD 455
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
952-1209 |
6.26e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 6.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 952 RQLQSEKKRLQQHIQELETHLEAEEGARQKLQLEKVTTEAKMKKfeedlllLEDQNSKLSKERRLLEERLAEFSSQ---A 1028
Cdd:pfam15905 83 RALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVAS-------LEKQLLELTRVNELLKAKFSEDGTQkkmS 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1029 AEEEEKVKSLNKLRVKYEATIA---DMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLgrkeEEL 1105
Cdd:pfam15905 156 SLSMELMKLRNKLEAKMKEVMAkqeGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYI----TEL 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1106 QSALVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVArakAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKr 1185
Cdd:pfam15905 232 SCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQE---LSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNA- 307
|
250 260
....*....|....*....|....
gi 564328072 1186 eqEVTELKKTLEEEARTHEVAMQE 1209
Cdd:pfam15905 308 --ELEELKEKLTLEEQEHQKLQQK 329
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
857-1168 |
7.65e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 857 LLQVTRQDEVLQ--ARAQELQKVQELQQQSAREVGELQGRV------AQLEEERARLAEQLRAEAELCSEAEETRARLAA 928
Cdd:PRK04863 790 QLRAEREELAERyaTLSFDVQKLQRLHQAFSRFIGSHLAVAfeadpeAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 929 RKQELELV-----------VTELEARVGEEEECSRQLQSEKKRLQQH---IQELETHLEA--------EEGARQKLQLEK 986
Cdd:PRK04863 870 AKEGLSALnrllprlnllaDETLADRVEEIREQLDEAEEAKRFVQQHgnaLAQLEPIVSVlqsdpeqfEQLKQDYQQAQQ 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 987 VTTEAKMKKF--------------EEDLLLLE---DQNSKLSK-------ERRLLEERLAEFSSQAAEEEEKVKSLNKLR 1042
Cdd:PRK04863 950 TQRDAKQQAFaltevvqrrahfsyEDAAEMLAknsDLNEKLRQrleqaeqERTRAREQLRQAQAQLAQYNQVLASLKSSY 1029
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1043 VKYEATIADMEDRLkkEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSalvraeeeggaraqL 1122
Cdd:PRK04863 1030 DAKRQMLQELKQEL--QDLGVPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDN--------------L 1093
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 564328072 1123 LKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGEL 1168
Cdd:PRK04863 1094 TKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRREL 1139
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1029-1375 |
7.68e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1029 AEEEEKVKSLNKLRVKYEATIADMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMMEQKQRAEELLIQLGRKEEELQSA 1108
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1109 LVRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQE 1188
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1189 VTELKKTLEEEARTH-EVAMQELRQRHSQALVELTEQLEQARRGKSVWEKTRLSLEAEVSELKTELSSLQTSRQEGEQKR 1267
Cdd:COG4372 166 LAALEQELQALSEAEaEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1268 RRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLAL 1347
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340
....*....|....*....|....*...
gi 564328072 1348 GSRVRALEAEAAGLREQMEEEVVARERA 1375
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDN 353
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1252-1400 |
8.05e-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: 8.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1252 ELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQlH 1331
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-K 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564328072 1332 DTQELLQEETRAKLalgsRVRALEAEAAGLREQMEEEVVARERAGRELQTTQAQLSEWRRRQEEEAAVL 1400
Cdd:COG1579 90 EYEALQKEIESLKR----RISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1788-1923 |
8.43e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1788 AERSFSAKAESGRQQLERQIQElrarlGEEDAGARARQKMLIAalESKLAQAEEQLEQESRERIlsgKLVRRAEKRLKEV 1867
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE-----AKKEAEAIKKEALLEA--KEEIHKLRNEFEKELRERR---NELQKLEKRLLQK 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1868 VLQVDEERRVADQLRDQLEKSNLRLKQLKRQLEEAEEEASRAQAgrrRLQRELEDV 1923
Cdd:PRK12704 95 EENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIE---EQLQELERI 147
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
920-1061 |
8.82e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 41.20 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 920 EETRARLAARKQELELVVteLEARVGEE---------EECSRQLQSEKKRLQQHIQElethleaeegARQKL--QLEKVT 988
Cdd:pfam05911 20 EKAEAEALALKQQLESVT--LQKLTAEEraahldgalKECMQQLRNVKEEQEQKIHD----------VVLKKtkEWEKIK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 989 T--EAKMKKFEEDLLLLEDQNSKLSK---ERRLLEERLAEFSSQAAEEEEKVKS--------LNKLrvKYEATIADMEDR 1055
Cdd:pfam05911 88 AelEAKLVETEQELLRAAAENDALSRslqERENLLMKLSEEKSQAEAEIEALKSrlescekeINSL--KYELHVLSKELE 165
|
....*.
gi 564328072 1056 LKKEEK 1061
Cdd:pfam05911 166 IRNEEK 171
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1100-1245 |
9.65e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1100 RKEEELQSALVRAEEEGgARAQLLKSLREAQAglaEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEdtldstnAQQ 1179
Cdd:COG2268 198 IRDARIAEAEAERETEI-AIAQANREAEEAEL---EQEREIETARIAEAEAELAKKKAEERREAETARAE-------AEA 266
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564328072 1180 ELRSKREQEVTELKKTLEEEARTHEVAMQELRQRHSQAlvelteQLEQARRGKSVWEKTRLSLEAE 1245
Cdd:COG2268 267 AYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEA------ELEADVRKPAEAEKQAAEAEAE 326
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1287-1498 |
9.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1287 ARAEAAEKLQRAQVELESVSTALSEAESKAIRLSKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQME 1366
Cdd:COG3883 10 TPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1367 EEVVARERAGRELQTTQAQLSewrrrQEEEAAVLEAGEEARRRAAREAETLAQRLAEKTEAverlERARRRLQQELDDAT 1446
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLG-----SESFSDFLDRLSALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564328072 1447 VDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARA 1498
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1440-1874 |
9.71e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 40.66 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1440 QELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERVEAEGREREARALSLTRALEEEQEAREELERQN 1519
Cdd:COG5278 93 AELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1520 RALRAELEALLSSKDDVGKNVHELERARRVAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDA 1599
Cdd:COG5278 173 AALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1600 GEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQAQMKELWREVEETRS 1679
Cdd:COG5278 253 LLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALA 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1680 SREEMFTLSRESEKRLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLGQLEEELE 1759
Cdd:COG5278 333 LATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAA 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564328072 1760 EEQNNSELLKDHYRKLVLQVETLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKLAQA 1839
Cdd:COG5278 413 AAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAA 492
|
410 420 430
....*....|....*....|....*....|....*
gi 564328072 1840 EEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEE 1874
Cdd:COG5278 493 LAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| |
