|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
92-763 |
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: 1268.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAaqqnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGK------KKGTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd01377 155 STGKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDPSYYFFLSQGeLTIDGVDDAEEFKLTD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd01377 235 EAFDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRThRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd01377 315 GQNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTK-SKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKP-MGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKS 569
Cdd:cd01377 394 MFVLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPnMGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKKPKPKKS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 570 --HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefagicaAEMNETAFGMRSRKGMFRTVSQ 647
Cdd:cd01377 474 eaHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDY-------EESGGGGGKKKKKGGSFRTVSQ 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 648 LHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDV 727
Cdd:cd01377 547 LHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNA 626
|
650 660 670
....*....|....*....|....*....|....*.
gi 1767286957 728 IPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd01377 627 IPKGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
92-763 |
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: 1167.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAA--AQQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRIN 249
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPhpAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 250 FDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHST 329
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVN 409
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 410 KAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNN 489
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 490 TMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKS 569
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 570 HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGICAAEMNETAFGMRSRKGMFRTVSQLH 649
Cdd:cd14911 481 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLY 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 650 KEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVIP 729
Cdd:cd14911 561 KEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIP 640
|
650 660 670
....*....|....*....|....*....|....
gi 1767286957 730 KNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14911 641 KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
80-763 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1072.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 80 IEDMSELTYLNEASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSML 159
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 160 QEREDQSILCTGESGAGKTENTKKVIQYLAHVAGAtrnkslnaaaqQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNS 239
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGS-----------GSAGNVGRLEEQILQSNPILEAFGNAKTVRNNNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 240 SRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLP 318
Cdd:pfam00063 150 SRFGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGcYTID 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 319 NVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLR 398
Cdd:pfam00063 230 GIDDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 399 PRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINY 478
Cdd:pfam00063 310 RRIKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINY 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 479 TNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKH 557
Cdd:pfam00063 390 VNEKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKH 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 558 PKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGICAAEMNETAFGMRS 637
Cdd:pfam00063 469 PHFQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPKRT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 638 RKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 717
Cdd:pfam00063 549 KKKRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFV 628
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1767286957 718 HRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:pfam00063 629 QRYRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
92-763 |
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: 1071.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAaqqnivqKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASSHKGRKDHNI-------PGELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTIN 331
Cdd:cd14920 154 VTGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETME 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd14920 234 AMHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd14920 314 QTKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP-DMRS 567
Cdd:cd14920 394 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE----FAGICAAEMNETAFGMRSRKGMFR 643
Cdd:cd14920 474 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrivgLDQVTGMTETAFGSAYKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 644 TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd14920 554 TVGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1767286957 724 TPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14920 634 TPNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
73-775 |
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: 1025.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 73 NPPKFDKIEDMSELTYLNEASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIAD 152
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 153 TAYRSMLQEREDQSILCTGESGAGKTENTKKVIQYLAHVAGATRnkslnaaaqqnivQKGELEHQLLQANPILEAFGNSK 232
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNT-------------EVGSVEDQILESNPILEAFGNAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 233 TVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvN 312
Cdd:smart00242 148 TLRNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYL-N 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 313 RG--ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAM-LQDDRVIQKVCHLLGLPV 389
Cdd:smart00242 227 QGgcLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAStVKDKEELSNAAELLGVDP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 390 IELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDIN 469
Cdd:smart00242 307 EELEKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDGS-TYFIGVLDIYGFEIFEVN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 470 SFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVE 548
Cdd:smart00242 386 SFEQLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIEkKPPGILSLLDEECRFPKGTDQTFLE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 549 KLQKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaem 628
Cdd:smart00242 465 KLNQHHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV--------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 629 netafGMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFP 708
Cdd:smart00242 536 -----SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFP 610
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767286957 709 NRVPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFRTGVLAHLEEERD 775
Cdd:smart00242 611 YRLPFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
92-763 |
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: 1002.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAqqnIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSFKTKKDQSSI---ALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTIN 331
Cdd:cd14932 158 VNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAETME 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd14932 238 AFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQKA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd14932 318 QTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP-DMRS 567
Cdd:cd14932 398 FILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKPkKLKD 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAFG-MRSRKGMFRT 644
Cdd:cd14932 478 DADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrIVGLdKVAGMGESLHGaFKTRKGMFRT 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 645 VSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILT 724
Cdd:cd14932 558 VGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 1767286957 725 PDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14932 638 PNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
92-763 |
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: 947.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKslnaaaqQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSHKGK-------KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTIN 331
Cdd:cd14921 154 VTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd14921 234 AMSIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd14921 314 QTKEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTM 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP-DMRS 567
Cdd:cd14921 394 FILEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPkQLKD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAF--GMRSRKGMFR 643
Cdd:cd14921 474 KTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLdQMAKMTESSLpsASKTKKGMFR 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 644 TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd14921 554 TVGQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEIL 633
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1767286957 724 TPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14921 634 AANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
92-763 |
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: 939.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaAQQNIV-QKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSHKTKK----DQNSLAlSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTI 330
Cdd:cd15896 157 DVNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd15896 237 EAFRIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd15896 317 AQTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHT 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP-DMR 566
Cdd:cd15896 397 MFILEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPkKLK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 567 SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAFGMRSRKGMFRT 644
Cdd:cd15896 477 DEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrIVGLdKVSGMSEMPGAFKTRKGMFRT 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 645 VSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILT 724
Cdd:cd15896 557 VGQLYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 636
|
650 660 670
....*....|....*....|....*....|....*....
gi 1767286957 725 PDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd15896 637 PNAIPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
92-763 |
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: 930.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKK----------DQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTIN 331
Cdd:cd14919 151 VNGYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETME 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd14919 231 AMRIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd14919 311 QTKEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP-DMRS 567
Cdd:cd14919 391 FILEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPkQLKD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAE-FAGI-CAAEMNETAF--GMRSRKGMFR 643
Cdd:cd14919 471 KADFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLdQVAGMSETALpgAFKTRKGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 644 TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd14919 551 TVGQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1767286957 724 TPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14919 631 TPNSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
92-763 |
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: 912.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAqqnivqkGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASSPKGRKEPGVP-------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNvDDVQEFHSTIN 331
Cdd:cd14930 154 VAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd14930 233 SLRVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd14930 313 QTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPM---GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP-DMRS 567
Cdd:cd14930 393 FVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHLRD 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfaGICAAE----MNETAFGMRSRKGMFR 643
Cdd:cd14930 473 QADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVE--GIVGLEqvssLGDGPPGGRPRRGMFR 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 644 TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd14930 551 TVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEIL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1767286957 724 TPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14930 631 TPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
29-1126 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 902.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 29 CWVPDQNEGFLIGSI-KRETNDEVLVELVDTSRQVTISRD----DVQKANPPKFDKIEDMSELTYLNEASVLHNLKDRYY 103
Cdd:COG5022 12 CWIPDEEKGWIWAEIiKEAFNKGKVTEEGKKEDGESVSVKkkvlGNDRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 104 SSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGESGAGKTENTKK 183
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 184 VIQYLAHVAGAtrnkslnaaaqqNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMSGYISGANIEF 263
Cdd:COG5022 172 IMQYLASVTSS------------STVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIET 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 264 YLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTINSMRIMGFADDE 342
Cdd:COG5022 240 YLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGcDKIDGIDDAKEFKITLDALKTIGIDEEE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 343 ISSIMRVVSAVLLLGNLEFtQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVE 422
Cdd:COG5022 320 QDQIFKILAAILHIGNIEF-KEDRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 423 AIAKASYERLFKWLVTRINKSLDRTHRQGaSFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQRE 502
Cdd:COG5022 399 SLAKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 503 GIEWDFIDFgLDLQPTIDLIEK--PMGVLALLDEECLFPKANDKSFVEKLQKTHNKH--PKFIVPDMRSKShFAVVHYAG 578
Cdd:COG5022 478 GIEWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRLNKNsnPKFKKSRFRDNK-FVVKHYAG 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 579 RVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaemnetafgMRSRKGMFRTVSQLHKEQLTKLMT 658
Cdd:COG5022 556 DVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE---------------NIESKGRFPTLGSRFKESLNSLMS 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 659 TLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDV----IPKNFID 734
Cdd:COG5022 621 TLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKED 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 735 GKESVRKMITALDIDTNLYRIGQSKVFFRTGVLAHLEEERDLKLTALIMNFQAQCRGFLSRRLYTRRQQQSSAIRIIQRN 814
Cdd:COG5022 701 TKNAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHG 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 815 GLAYLKLRNWQWWRLFTKVKPLLQVTRTDDEIRAKDDELRaTKERLLKMEHDFRENEKkldqviVERAVIQEQLQQESEN 894
Cdd:COG5022 781 FRLRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACII-KLQKTIKREKKLRETEE------VEFSLKAEVLIQKFGR 853
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 895 SAELDDIRGRLQTRNQELEY--IVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRL 972
Cdd:COG5022 854 SLKAKKRFSLLKKETIYLQSaqRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARL 933
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 973 -RNLEERLVELQdaydkLLKEKRLLEEKVEglttqLLDHEERAKHGVKAKGRLENQLHELEQDLNRERqykSELEQHKRK 1051
Cdd:COG5022 934 kKLLNNIDLEEG-----PSIEYVKLPELNK-----LHEVESKLKETSEEYEDLLKKSTILVREGNKAN---SELKNFKKE 1000
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1052 lLAELEDSKDHLAEKMGKVEELNNQLMkRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNAR 1126
Cdd:COG5022 1001 -LAELSKQYGALQESTKQLKELPVEVA-ELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRR 1073
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
92-763 |
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: 846.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRH-EMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGatRNKSLNAAAQQNIVQkgelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSG--SGSSKSSSSASSIEQ------QILQSNPILEAFGNAKTVRNDNSSRFGKFIELQF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-----ITLPNVDDVQE 325
Cdd:cd00124 153 DPTGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLNDYLnssgcDRIDGVDDAEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 326 FHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ--EKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 403
Cdd:cd00124 233 FQELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFEEdeEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 404 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQ-GASFIGILDIAGFEIFDINSFEQICINYTNEK 482
Cdd:cd00124 313 GGETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 483 LQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 561
Cdd:cd00124 393 LQQFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFF 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 562 VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDpfvagiwkdaefagicaaemnetafgmrsrkgm 641
Cdd:cd00124 472 SKKRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSGSQ--------------------------------- 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 642 frtvsqlHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYE 721
Cdd:cd00124 519 -------FRSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYR 591
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1767286957 722 ILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd00124 592 ILAPGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
92-763 |
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: 789.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVA--GATRNKSLNAAAQQnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRIN 249
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAalGDGPGKKAQFLATK---TGGTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 250 FDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDDVQEFH 327
Cdd:cd14927 158 FGPTGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSG-KKPELQDMLLVSMNpyDYHFCSQGVTTVDNMDDGEELM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 328 STINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREF 407
Cdd:cd14927 237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEY 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 408 VNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQgaSFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd14927 317 VTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDtKLPRQ--FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVP-- 563
Cdd:cd14927 395 FNHHMFILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKPrp 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 564 DMRSK--SHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDaeFAGICAAEMNETAFGMRSRKGM 641
Cdd:cd14927 475 DKKRKyeAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN--YVGSDSTEDPKSGVKEKRKKAA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 642 -FRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 720
Cdd:cd14927 553 sFQTVSQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRY 632
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1767286957 721 EILTPDVIPKN-FIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14927 633 RILNPSAIPDDkFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
92-763 |
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: 758.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVaGATRNKSLNAAaqqnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATV-GASKKTDEAAK------SKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLL-EGVDNYRFLVNRGITLPNVDDVQEFHSTI 330
Cdd:cd14909 154 PTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd14909 234 QAFDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd14909 314 GRNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHH 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM---- 565
Cdd:cd14909 393 MFVLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKPpkpg 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefAGICAAEmnETAFGMRSRKGM-FRT 644
Cdd:cd14909 473 QQAAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADH--AGQSGGG--EQAKGGRGKKGGgFAT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 645 VSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILT 724
Cdd:cd14909 549 VSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILN 628
|
650 660 670
....*....|....*....|....*....|....*....
gi 1767286957 725 PDVIPKNfIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14909 629 PAGIQGE-EDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
93-763 |
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: 755.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAGatrnkSLNAAAQQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAA-----TGDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd14913 157 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLITTNPYDYpFISQGeILVASIDDAEELLATD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd14913 236 SAIDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQgaSFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNN 489
Cdd:cd14913 316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDtKLPRQ--HFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 490 TMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM--- 565
Cdd:cd14913 394 HMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKVvkg 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWkdAEFAGICAAEmnETAFGMRSRKGMFRTV 645
Cdd:cd14913 474 RAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLY--ATFATADADS--GKKKVAKKKGSSFQTV 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 646 SQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd14913 550 SALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNA 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 1767286957 726 DVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14913 630 SAIPEgQFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
840-1912 |
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: 740.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 840 TRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDM 919
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 920 RDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEK 999
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1000 VEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMK 1079
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1080 RDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQD 1159
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1160 LMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASR 1239
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1240 ADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEE 1319
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1320 TRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE--SVNQQLEELRKKNLRDVEHLQKQ 1397
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEdaGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1398 LEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLS 1477
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1478 LLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEV 1557
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1558 TNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQL 1637
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1638 KKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEN---DELEELRAKGGGIS 1714
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERdelADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1715 SEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESG 1794
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1795 AQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLD 1874
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 1767286957 1875 EAEDEMSRERTKHRNVQREADDLLDANEQLTRELMNLR 1912
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLK 1078
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
92-763 |
0e+00 |
|
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.
Pssm-ID: 276896 [Multi-domain] Cd Length: 659 Bit Score: 737.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNaaaqqnivqKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDG---------KGSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILrgcsAKEKSEyLLEGV------DNYRFLVNRGITLPNVDDVQE 325
Cdd:cd14934 152 TTGKLAGADIESYLLEKSRVISQQAAERGYHIFYQIL----SNKKPE-LIESLllvpnpKEYHWVSQGVTVVDNMDDGEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 326 FHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGR 405
Cdd:cd14934 227 LQITDVAFDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 406 EFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQ 485
Cdd:cd14934 307 EFVQKGQNMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 486 LFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPD 564
Cdd:cd14934 386 FFNHHMFVLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 565 ----MRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGicaaemnetAFGMRSRKG 640
Cdd:cd14934 466 ggkgKGPEAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPA---------GSKKQKRGS 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 641 MFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 720
Cdd:cd14934 537 SFMTVSNFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRY 616
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1767286957 721 EILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14934 617 QVLNPNVIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
92-763 |
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: 720.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAAMIESKK----------KLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcsAKEKSEYLL--EGVDNYRFLVNRGITLPNVDDVQEFHST 329
Cdd:cd14929 151 ARGMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSG--KKELRDLLLvsANPSDFHFCSCGAVAVESLDDAEELLAT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVN 409
Cdd:cd14929 229 EQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 410 KAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQgaSFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFN 488
Cdd:cd14929 309 RSQNIEQVTYAVGALSKSIYERMFKWLVARINRVLDaKLSRQ--FFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 489 NTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDMRS 567
Cdd:cd14929 387 QHMFVLEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFDNHfGKSVHFQKPKPDK 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KS---HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGicaaemNETAFGMRSRK--GMF 642
Cdd:cd14929 467 KKfeaHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTD------SAIQFGEKKRKkgASF 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 643 RTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEI 722
Cdd:cd14929 541 QTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCI 620
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1767286957 723 LTPDVIPKN-FIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14929 621 LNPRTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
93-763 |
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: 702.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAG-ATRNKSLNAAAqqnivqKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAiGDRSKKDQTPG------KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILrgcsAKEKSEYL-----LEGVDNYRFLVNRGITLPNVDDVQEF 326
Cdd:cd14917 156 ATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQIL----SNKKPELLdmlliTNNPYDYAFISQGETTVASIDDAEEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 327 HSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGRE 406
Cdd:cd14917 232 MATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 407 FVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd14917 312 YVTKGQNVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVP-- 563
Cdd:cd14917 391 FNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHlGKSNNFQKPrn 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 564 -DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWkdAEFAGicAAEMNETAFGMRSRKGMF 642
Cdd:cd14917 471 iKGKPEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLF--ANYAG--ADAPIEKGKGKAKKGSSF 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 643 RTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEI 722
Cdd:cd14917 547 QTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRI 626
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1767286957 723 LTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14917 627 LNPAAIPEgQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
93-763 |
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: 695.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYY-SSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01380 2 AVLHNLKVRFCqRNAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnivqkgELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET-------------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd01380 149 KNYRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGsPVIDGVDDAAEFEETR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd01380 229 KALTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGA-SFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNN 489
Cdd:cd01380 309 PLTLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 490 TMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPK--FIVPDMrS 567
Cdd:cd01380 389 HVFKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRF-S 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaefagicaaemnetafgmrSRKgmfRTVSQ 647
Cdd:cd01380 467 NTAFIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASK-----------------------------NRK---KTVGS 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 648 LHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDV 727
Cdd:cd01380 515 QFRDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSK 594
|
650 660 670
....*....|....*....|....*....|....*.
gi 1767286957 728 iPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd01380 595 -EWLRDDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
93-763 |
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: 687.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAGATRNKSlnaaAQQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKK----EQQPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd14923 158 TGKLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLISTNPFDFpFVSQGeVTVASIDDSEELLATD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd14923 237 NAIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd14923 317 GQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM---R 566
Cdd:cd14923 396 MFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlGKSNNFQKPKPakgK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 567 SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDaeFAGICAAEMNETAFGMRSRKGMFRTVS 646
Cdd:cd14923 476 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN--YAGAEAGDSGGSKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14923 554 AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAS 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 727 VIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14923 634 AIPEgQFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
93-763 |
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: 686.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAgATRNKSLNAAAQQNIvqKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIA-VTGEKKKEEATSGKM--QGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDDVQEFHSTI 330
Cdd:cd14910 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd14910 238 SAIEILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd14910 318 GQTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM---R 566
Cdd:cd14910 397 MFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPakgK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 567 SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAgicAAEMNETAFGMRSRKGMFRTVS 646
Cdd:cd14910 477 VEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAAAA---EAEEGGGKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14910 554 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 727 VIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14910 634 AIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
93-763 |
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: 684.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAG-ATRNKSLNAAAQqnivqKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAiGDRSKKENPNAN-----KGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDDVQEFHST 329
Cdd:cd14916 157 ATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLVTNNpyDYAFVSQGEVSVASIDDSEELLAT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVN 409
Cdd:cd14916 236 DSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 410 KAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNN 489
Cdd:cd14916 316 KGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 490 TMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVP---DM 565
Cdd:cd14916 395 HMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYDNHlGKSNNFQKPrnvKG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWkdAEFAGICAAEMNETAfGMRSRKGMFRTV 645
Cdd:cd14916 475 KQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLF--STYASADTGDSGKGK-GGKKKGSSFQTV 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 646 SQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd14916 552 SALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNP 631
|
650 660 670
....*....|....*....|....*....|....*....
gi 1767286957 726 DVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14916 632 AAIPEgQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
94-763 |
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: 683.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 94 VLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGES 173
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 174 GAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQnivqkGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMS 253
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVTGEKKKEESGKMQ-----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 254 GYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVD--NYRFLVNRGITLPNVDDVQEFHSTIN 331
Cdd:cd14918 158 GKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLITTNpyDYAFVSQGEITVPSIDDQEELMATDS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd14918 237 AIDILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd14918 317 QTVQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHM 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM---RS 567
Cdd:cd14918 396 FVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYDQHlGKSANFQKPKVvkgKA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETA-FGMRSRKGMFRTVS 646
Cdd:cd14918 476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASL-----FSTYASAEADSGAkKGAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14918 551 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 727 VIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14918 631 AIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
93-763 |
0e+00 |
|
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276879 [Multi-domain] Cd Length: 671 Bit Score: 679.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAASGK---MQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd14915 159 TGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLITTNPYDFaFVSQGeITVPSIDDQEELMATD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNK 410
Cdd:cd14915 238 SAVDILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd14915 318 GQTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM---R 566
Cdd:cd14915 397 MFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSNNFQKPKPakgK 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 567 SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAgicAAEMNETAFGMRSRKGMFRTVS 646
Cdd:cd14915 477 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSGMKTLAFLFSGGQTA---EAEGGGGKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14915 554 ALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 727 VIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14915 634 AIPEgQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
93-763 |
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: 677.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVA--GATRNKSLNAAAQQnivqkGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAvtGEKKKEEITSGKMQ-----GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcSAKEKSEYLLEGVDNYRF-LVNRG-ITLPNVDDVQEFHS 328
Cdd:cd14912 157 GTTGKLASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLITTNPYDYpFVSQGeISVASIDDQEELMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 329 TINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFV 408
Cdd:cd14912 236 TDSAIDILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 409 NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFN 488
Cdd:cd14912 316 TKGQTVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFN 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 489 NTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTH-NKHPKFIVPDM-- 565
Cdd:cd14912 395 HHMFVLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlGKSANFQKPKVvk 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 -RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETAFGMR---SRKG- 640
Cdd:cd14912 475 gKAEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYL-----FSGAQTAEGASAGGGAKkggKKKGs 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 641 MFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 720
Cdd:cd14912 550 SFQTVSALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRY 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1767286957 721 EILTPDVIPK-NFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14912 630 KVLNASAIPEgQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
93-763 |
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: 666.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAGATRNKslnaaaqqniVQKGelEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd01378 82 SGAGKTEASKRIMQYIAAVSGGSESE----------VERV--KDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTIN 331
Cdd:cd01378 150 KGEPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGcFDVDGIDDAADFKEVLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFtQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREF---V 408
Cdd:cd01378 230 AMKVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvY 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 409 NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFN 488
Cdd:cd01378 309 EVPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 489 NTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFP-KANDKSFVEKLQKTHNKHPKFIVPDMR 566
Cdd:cd01378 389 ELTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFECPSGH 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 567 ---SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGicaaemnetafgmrSRKgmfR 643
Cdd:cd01378 468 felRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVDLD--------------SKK---R 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 644 --TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYE 721
Cdd:cd01378 531 ppTAGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYK 610
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1767286957 722 ILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd01378 611 LLSPKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
93-763 |
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: 658.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVagaTRNKSlnaaaqqnivqkgELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd14883 82 SGAGKTETTKLILQYLCAV---TNNHS-------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSA-KE-KSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHST 329
Cdd:cd14883 146 SGHIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAKHsKElKEKLKLGEPEDYHYLNQSGcIRIDNINDKKDFDHL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDR-VIQKVCHLLGLPVIELQKAFLRPRIKVGREFV 408
Cdd:cd14883 226 RLAMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDIDGETGALTVEDKeILKIVAKLLGVDPDKLKKALTIRQINVRGNVT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 409 NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKsldRTH--RQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd14883 306 EIPLKVQEARDNRDAMAKALYSRTFAWLVNHINS---CTNpgQKNSRFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEK-PMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDM 565
Cdd:cd14883 383 FNHYVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDR 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 R-SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWK---DAEFAGICAAEMNETAFGMRSRKGm 641
Cdd:cd14883 462 RrWKTEFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypdLLALTGLSISLGGDTTSRGTSKGK- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 642 fRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYE 721
Cdd:cd14883 541 -PTVGDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYL 619
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1767286957 722 ILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14883 620 CLDPRARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
92-763 |
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: 636.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGATrnkslnaaaqqniVQKGE-LEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRIN 249
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMGGRA-------------VTEGRsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 250 FDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG--ITLPNVDDVQEFH 327
Cdd:cd01384 148 FDDAGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYL-NQSkcFELDGVDDAEEYR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 328 STINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRV---IQKVCHLLGLPVIELQKAFLRPRIKVG 404
Cdd:cd01384 227 ATRRAMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 405 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDINSFEQICINYTNEKLQ 484
Cdd:cd01384 307 DGIITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 485 QLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVP 563
Cdd:cd01384 386 QHFNQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 564 DmRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAgicAAEMNETafgmrSRKGMFR 643
Cdd:cd01384 465 K-LSRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL-----FP---PLPREGT-----SSSSKFS 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 644 TVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd01384 531 SIGSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLL 610
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1767286957 724 TPDVIPKNFiDGKESVRKMITALDIDTnlYRIGQSKVFFR 763
Cdd:cd01384 611 APEVLKGSD-DEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
92-763 |
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: 631.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGatrnkslnaaaqqnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAISG----------------QHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd01381 145 KNGVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNcLTCEGRDDAAEFADIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKS--DQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFV 408
Cdd:cd01381 225 SAMKVLMFTDEEIWDIFKLLAAILHLGNIKFEATVVDnlDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 409 NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGAS--FIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd01381 305 VSPLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQF 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDM 565
Cdd:cd01381 385 FVRHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKS 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFvagiwkdaeFAGICAAEMNETAfGMRSRKgmfRTV 645
Cdd:cd01381 464 DLNTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKF---------LKQLFNEDISMGS-ETRKKS---PTL 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 646 SQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd01381 531 SSQFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP 610
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 726 DVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd01381 611 GIPPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
93-763 |
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: 626.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKgkKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAGATRNkslnaaaqqnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGGGSSG----------------IENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTIN 331
Cdd:cd01383 144 AGKICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNcLTIDGVDDAKKFHELKE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKA 411
Cdd:cd01383 224 ALDTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 412 QNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTM 491
Cdd:cd01383 304 LTLQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 492 FILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFivpDMRSKSH 570
Cdd:cd01383 384 FKLEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCF---KGERGGA 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 571 FAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNS----TDPFVAGIWKDAEfagicAAEMNETAFGMRSRKgmfRTVS 646
Cdd:cd01383 460 FTIRHYAGEVTYDTSGFLEKNRDLLHSDLIQLLSSCscqlPQLFASKMLDASR-----KALPLTKASGSDSQK---QSVA 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd01383 532 TKFKGQLFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPE 611
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 727 viPKNFIDGKESVRKMI-TALDIDTNLYRIGQSKVFFR 763
Cdd:cd01383 612 --DVSASQDPLSTSVAIlQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
92-763 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 569.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGATrnkslnaaaqqnivqKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESWGSG---------------AGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEyLLEGvdnyrflvnrgitlPNVDDVQEFHSTI 330
Cdd:cd01382 146 NEKSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREK-LLKD--------------PLLDDVGDFIRMD 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQE-----------KKSDQAmlqddrvIQKVCHLLGLPVIELQKAfLRP 399
Cdd:cd01382 211 KAMKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENgsdsgggcnvkPKSEQS-------LEYAAELLGLDQDELRVS-LTT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 400 R-------------IKVGREFvnkaqnqEQAEFAVEAIAKASYERLFKWLVTRINKSLdrTHRQGASFIGILDIAGFEIF 466
Cdd:cd01382 283 RvmqttrggakgtvIKVPLKV-------EEANNARDALAKAIYSKLFDHIVNRINQCI--PFETSSYFIGVLDIAGFEYF 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 467 DINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKS 545
Cdd:cd01382 354 EVNSFEQFCINYCNEKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQH 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 546 FVEKLQKTHNKHPKFIVP---------DMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWk 616
Cdd:cd01382 433 FTSAVHQKHKNHFRLSIPrksklkihrNLRDDEGFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLF- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 617 daefagiCAAEMNETAFGMRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGV 696
Cdd:cd01382 512 -------ESSTNNNKDSKQKAGKLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGM 584
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767286957 697 LEGIRICRQGFPNRVPFQEFRHRYEILTPDVIPKnfIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd01382 585 VSVLDLMQGGFPSRTSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
92-763 |
0e+00 |
|
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276839 Cd Length: 644 Bit Score: 564.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNkslnaaaqqnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGSTNG----------------VEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGcsAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd14872 145 NRGRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLAS--PDPASRGGWGSSAAYGYLSLSGcIEVEGVDDVADFEEVV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQE------KKSDQAmlqDDRVIQKVCHLLGLPVIELQKAFLRPRIKV- 403
Cdd:cd14872 223 LAMEQLGFDDADINNVMSLIAAILKLGNIEFASGggkslvSGSTVA---NRDVLKEVATLLGVDAATLEEALTSRLMEIk 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 404 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKL 483
Cdd:cd14872 300 GCDPTRIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 484 QQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEK-PMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI- 561
Cdd:cd14872 380 QQHFNQYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVy 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 562 VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFagicaaemnetafgmrSRKGM 641
Cdd:cd14872 459 AEVRTSRTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKLIAVLFPPSEG----------------DQKTS 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 642 FRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYE 721
Cdd:cd14872 523 KVTLGGQFRKQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYR 602
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1767286957 722 ILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14872 603 FLVKTIAKRVGPDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
92-761 |
1.87e-175 |
|
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: 548.62 E-value: 1.87e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEF------KGKKRHEMPPHIFAIADTAYRSMLQERE-- 163
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 164 --DQSILCTGESGAGKTENTKKVIQYLAHVAGATRnKSLNAAAQQNIVQKgelehqLLQANPILEAFGNSKTVKNDNSSR 241
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATT-HGQNATERENVRDR------VLESNPILEAFGNARTNRNNNSSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 242 FGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG---ITLP 318
Cdd:cd14901 154 FGKFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYL-NSSqcyDRRD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 319 NVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF-TQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFL 397
Cdd:cd14901 233 GVDDSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLC 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 398 RPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGAS-FIGILDIAGFEIFDINSFEQICI 476
Cdd:cd14901 313 TREIRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 477 NYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgldlqPTIDLI-----EKPMGVLALLDEECLFPKANDKSFVEKLQ 551
Cdd:cd14901 393 NFANEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PNNDACvamfeARPTGLFSLLDEQCLLPRGNDEKLANKYY 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 552 KTHNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGiwkdaefagicaaemne 630
Cdd:cd14901 468 DLLAKHASFSVSKLqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS----------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 631 tafgmrsrkgmfrTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNR 710
Cdd:cd14901 531 -------------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVR 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 711 VPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNL-----YRIGQSKVF 761
Cdd:cd14901 598 FPHDAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
92-763 |
3.72e-173 |
|
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: 542.44 E-value: 3.72e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQ----EREDQS 166
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQsgvlDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 167 ILCTGESGAGKTENTKKVIQYLAHVAGATR---NKSLNAAAQQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 243
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAqgaSGEGEAASEAIEQTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 244 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLE-GVDNYRFLVNRGiTLPNVDD 322
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQtPVEYFYLRGECS-SIPSCDD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 323 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQamLQDDRVIQ---KVCHLLGLPVIELQKAFLRP 399
Cdd:cd14890 240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESENDTTV--LEDATTLQslkLAAELLGVNEDALEKALLTR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 400 RIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDINSFEQICINYT 479
Cdd:cd14890 318 QLFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 480 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-----KPmGVLALLDEECLFPKAN-DKSFVEKLQKT 553
Cdd:cd14890 397 NEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgkvngKP-GIFITLDDCWRFKGEEaNKKFVSQLHAS 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 554 H-------------NKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaef 620
Cdd:cd14890 475 FgrksgsggtrrgsSQHPHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 621 agicaAEMNETAFGMRsrkgmFRTvsqlhkeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGI 700
Cdd:cd14890 542 -----RSIREVSVGAQ-----FRT-------QLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAI 604
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 701 RICRQGFPNRVPFQEFRHRYEILTPDVipknfIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14890 605 QIRQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
92-763 |
6.12e-171 |
|
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276838 [Multi-domain] Cd Length: 657 Bit Score: 536.26 E-value: 6.12e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVagatrNKSLNAAAQQnivqkgelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAV-----NQRRNNLVTE----------QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 mSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYrFLVNRGIT--LPNVDDVQEFHST 329
Cdd:cd01387 146 -GGVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKY-FYLNQGGNceIAGKSDADDFRRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ---EKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGRE 406
Cdd:cd01387 224 LAAMQVLGFSSEEQDSIFRILASVLHLGNVYFHKrqlRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 407 FVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINkSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd01387 304 RIFTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDM 565
Cdd:cd01387 383 FNKHVFKLEQEEYIREQIDWTEIAFA-DNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 rSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDaefagICAAEMNETAFGMRSR----KGM 641
Cdd:cd01387 462 -PLPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS-----HRAQTDKAPPRLGKGRfvtmKPR 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 642 FRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF--RHR 719
Cdd:cd01387 536 TPTVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFidRYR 615
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1767286957 720 YEILTPDVIPKNFIDGKESVRKMITAldIDTNLYRIGQSKVFFR 763
Cdd:cd01387 616 CLVALKLPRPAPGDMCVSLLSRLCTV--TPKDMYRLGATKVFLR 657
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
93-763 |
1.31e-169 |
|
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: 531.85 E-value: 1.31e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAGATrNKSLnaaaqqnivqkgelEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKAN-NRTL--------------EEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSE-YLLEGVDNYRFLVNRGITLPNVDD----VQEFH 327
Cdd:cd01379 147 TGAVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkYKLPENKPPRYLQNDGLTVQDIVNnsgnREKFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 328 STINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQ----AMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 403
Cdd:cd01379 227 EIEQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEALTSHSVVT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 404 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL--DRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNE 481
Cdd:cd01379 307 RGETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 482 KLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTID-LIEKPMGVLALLDEECLFPKANDKSFVEKLQKthNKHPKF 560
Cdd:cd01379 387 QIQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKFHN--NIKSKY 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 561 IVpdmRSKSH---FAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAgiwkdaefagicaaemnetafgmrs 637
Cdd:cd01379 464 YW---RPKSNalsFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVR------------------------- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 638 rkgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 717
Cdd:cd01379 516 -----QTVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFL 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1767286957 718 HRYEIL----TPDVIPKnfidgKESVRKMITALDIDTnlYRIGQSKVFFR 763
Cdd:cd01379 591 KRYYFLafkwNEEVVAN-----RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
92-763 |
1.82e-168 |
|
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: 528.88 E-value: 1.82e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKK-RHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSvRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGAtrnkslnaaaqqnivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPS---------------DDSDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQE----- 325
Cdd:cd14897 146 TENGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEEleyyr 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 326 --FHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKV 403
Cdd:cd14897 226 qmFHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 404 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL----DRTHRQGASFIGILDIAGFEIFDINSFEQICINYT 479
Cdd:cd14897 306 RGERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 480 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHP 558
Cdd:cd14897 386 NERLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESP 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 559 KFiVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVagiwkdaefagicaaemnetafgmrsr 638
Cdd:cd14897 465 RY-VASPGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFI--------------------------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 639 KGMFrtvSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 718
Cdd:cd14897 517 SDLF---TSYFKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVK 593
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1767286957 719 RYEILTPDViPKNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 763
Cdd:cd14897 594 RYKEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
92-763 |
3.97e-168 |
|
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: 530.03 E-value: 3.97e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAgatrnkslnaaaqqnivQKGE---LEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRI 248
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALS-----------------QKGYgsgVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 249 NFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFL-VNRGITLPNVDDVQEFH 327
Cdd:cd01385 144 NYRENGMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLnQSDCYTLEGEDEKYEFE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 328 STINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEK--KSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGR 405
Cdd:cd01385 224 RLKQAMEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyhRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 406 EFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL----DRTHRQGASfIGILDIAGFEIFDINSFEQICINYTNE 481
Cdd:cd01385 304 ETLILPYKLPEAIATRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 482 KLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKF 560
Cdd:cd01385 383 HLQYYFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 561 IVPDMRSKShFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGI----------WKDAEFAGICAAEMNE 630
Cdd:cd01385 462 EKPQVMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELigidpvavfrWAVLRAFFRAMAAFRE 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 631 TafGMRSRKG--------MFRTVSQLHKEQ---------------LTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLV 687
Cdd:cd01385 541 A--GRRRAQRtaghsltlHDRTTKSLLHLHkkkkppsvsaqfqtsLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELV 618
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 688 LEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILtpdvIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd01385 619 LRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVL----LPKGLISSKEDIKDFLEKLNLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
92-725 |
2.50e-165 |
|
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276853 [Multi-domain] Cd Length: 667 Bit Score: 521.56 E-value: 2.50e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKgKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAhVAGAtrnkslnaaaqQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14888 80 GESGAGKTESTKYVMKFLA-CAGS-----------EDIKKRSLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DM---------SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQIlrgCSAKEKS---EYLLEGVDNYRF--------- 309
Cdd:cd14888 148 SKlkskrmsgdRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQL---CAAAREAkntGLSYEENDEKLAkgadakpis 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 310 ---------LVNRGIT------LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF-TQEKKSDQAMLQ 373
Cdd:cd14888 225 idmssfephLKFRYLTksscheLPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFeNNEACSEGAVVS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 374 D--DRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQG 451
Cdd:cd14888 305 AscTDDLEKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNS 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 452 ASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLA 530
Cdd:cd14888 385 LLFCGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFC 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 531 LLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKShFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPF 610
Cdd:cd14888 464 MLDEECFVPGGKDQGLCNKLCQKHKGHKRFDVVKTDPNS-FVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPF 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 611 VAGIWKdAEFAGICAAEMnetafgmrsRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQ 690
Cdd:cd14888 543 ISNLFS-AYLRRGTDGNT---------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQ 612
|
650 660 670
....*....|....*....|....*....|....*
gi 1767286957 691 LRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd14888 613 LKYGGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
92-763 |
2.66e-163 |
|
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: 515.48 E-value: 2.66e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGATRNKSLNaaaqqnivqkgelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIAGGLNDSTIK---------------KIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKseYLLEGVDNYRFL-VNRGITLPNVDDVQEFHST 329
Cdd:cd14903 146 DKNGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEER--LFLDSANECAYTgANKTIKIEGMSDRKHFART 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQ--AMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREF 407
Cdd:cd14903 224 KEALSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEksAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 408 VNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQgASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLF 487
Cdd:cd14903 304 YTVPLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKF 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 488 NNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRS 567
Cdd:cd14903 383 TQDVFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 568 KSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKD-AEFAGICAAEMNETAFGMRSRKGMFRTVS 646
Cdd:cd14903 462 RTQFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEkVESPAAASTSLARGARRRRGGALTTTTVG 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14903 542 TQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPE 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 727 ViPKNFIDGKESVRKMITALDIDT-NLYRIGQSKVFFR 763
Cdd:cd14903 622 G-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
92-763 |
1.94e-160 |
|
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: 507.76 E-value: 1.94e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSE----DLIEEFKgKKRHEMPPHIFAIADTAYRSMLQER----E 163
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpgfDSQRKEE-ATASSPPPHVFSIAERAYRAMKGVGkgqgT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 164 DQSILCTGESGAGKTENTKKVIQYLA----HVAGATRNKSLNAAAQQnivqkgeLEHQLLQANPILEAFGNSKTVKNDNS 239
Cdd:cd14892 80 PQSIVVSGESGAGKTEASKYIMKYLAtaskLAKGASTSKGAANAHES-------IEECVLLSNLILEAFGNAKTIRNDNS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 240 SRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG--ITL 317
Cdd:cd14892 153 SRFGKYIQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFL-NQGncVEV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 318 PNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQ--KVCHLLGLPVIELQKA 395
Cdd:cd14892 232 DGVDDATEFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFK 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 396 FLRPRIKVGR-EFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQ---------GASFIGILDIAGFEI 465
Cdd:cd14892 312 LVTQTTSTARgSVLEIKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 466 FDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEK-PMGVLALLDEECLFP-KAND 543
Cdd:cd14892 392 MPTNSFEQLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTD 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 544 KSFVEKLQKTH-NKHPKFIVPDMRSkSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQnstdpfvagiwkdaefag 622
Cdd:cd14892 471 KQLLTIYHQTHlDKHPHYAKPRFEC-DEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLR------------------ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 623 icaaemnetafgmRSRKgmFRTvsqlhkeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRI 702
Cdd:cd14892 532 -------------SSSK--FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRI 589
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767286957 703 CRQGFPNRVPFQEFRHRYEILTPDV--IPKNFIDGKESVRKM----ITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14892 590 RREGFPIRRQFEEFYEKFWPLARNKagVAASPDACDATTARKkceeIVARALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
92-763 |
2.10e-159 |
|
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276840 [Multi-domain] Cd Length: 651 Bit Score: 504.71 E-value: 2.10e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSC-------VEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHST 329
Cdd:cd14873 154 CQKGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGcVEDKTISDQESFREV 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQekkSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVN 409
Cdd:cd14873 234 ITAMEVMQFSKEEVREVSRLLAGILHLGNIEFIT---AGGAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 410 KAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLdrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNN 489
Cdd:cd14873 311 TPLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 490 TMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSkS 569
Cdd:cd14873 389 HIFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAV-N 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 570 HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGICAAEMNETAFGMRSRKGmfRTVSQLH 649
Cdd:cd14873 467 NFGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDL-----FEHVSSRNNQDTLKCGSKHRR--PTVSSQF 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 650 KEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDvip 729
Cdd:cd14873 540 KDSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRN--- 616
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 730 knfIDGKESVRKMITAL----DIDTNLYRIGQSKVFFR 763
Cdd:cd14873 617 ---LALPEDVRGKCTSLlqlyDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
92-723 |
8.96e-158 |
|
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: 501.10 E-value: 8.96e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRH--------EMPPHIFAIADTAYRSMLQER 162
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 163 EDQSILCTGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQKGE----LEHQLLQANPILEAFGNSKTVKNDN 238
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSKstksIEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 239 SSRFGKFIRINFDM-SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEG---VDNYRFL-VNR 313
Cdd:cd14907 161 SSRFGKYVSILVDKkKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNqlsGDRYDYLkKSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 314 GITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQA--MLQDDRVIQKVCHLLGLPVIE 391
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSpcCVKNKETLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 392 LQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL-------DRTHRQGASFIGILDIAGFE 464
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 465 IFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDF--IDFgLDLQPTIDLIEK-PMGVLALLDEECLFPKA 541
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 542 NDKSFVEKLQKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFA 621
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSI-----FS 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 622 GICAAEMNETAFGMRSRKGMfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIR 701
Cdd:cd14907 555 GEDGSQQQNQSKQKKSQKKD-KFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660
....*....|....*....|..
gi 1767286957 702 ICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLL 655
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
94-763 |
7.44e-150 |
|
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: 479.02 E-value: 7.44e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 94 VLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSML----QEREDQSILC 169
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 170 TGESGAGKTENTKKVIQYLAHVAGATrnkslnaaaqqnivqkGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRIN 249
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELCRGN----------------SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 250 FdMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRgitLPNVDDVQEF--- 326
Cdd:cd14889 147 F-RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNG---AGCKREVQYWkkk 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 327 -HSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF-TQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 404
Cdd:cd14889 223 yDEVCNAMDMVGFTEQEEVDMFTILAGILSLGNITFeMDDDEALKVENDSNGWLKAAAGQFGVSEEDLLKTLTCTVTFTR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 405 REFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQG--ASFIGILDIAGFEIFDINSFEQICINYTNEK 482
Cdd:cd14889 303 GEQIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQ 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 483 LQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDL-IEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 561
Cdd:cd14889 383 LQYFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYG 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 562 VPDMRSKShFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDP-----FVAGIWKDAEFAGICAA-EMNETAFGm 635
Cdd:cd14889 462 KSRSKSPK-FTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPllsvlFTATRSRTGTLMPRAKLpQAGSDNFN- 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 636 RSRKgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQE 715
Cdd:cd14889 540 STRK---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAE 616
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1767286957 716 FRHRYEILtpdVIPKNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 763
Cdd:cd14889 617 FAERYKIL---LCEPALPGTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
58-761 |
6.48e-147 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 476.44 E-value: 6.48e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 58 TSRQVTISRDDVQKANPP-KFDKIEDMSELTYLNEASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFK 136
Cdd:PTZ00014 75 TNSTFEVKPEHAFNANSQiDPMTYGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 137 GKKRHE-MPPHIFAIADTAYRSMLQEREDQSILCTGESGAGKTENTKKVIQYLAhvAGATRNKSLNaaaqqniVQKGele 215
Cdd:PTZ00014 155 DAKDSDkLPPHVFTTARRALENLHGVKKSQTIIVSGESGAGKTEATKQIMRYFA--SSKSGNMDLK-------IQNA--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 216 hqLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKE 295
Cdd:PTZ00014 223 --IMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEM 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 296 KSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKK---SDQAML 372
Cdd:PTZ00014 301 KEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgglTDAAAI 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 373 QDD--RVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrtHRQ 450
Cdd:PTZ00014 381 SDEslEVFNEACELLFLDYESLKKELTVKVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIE--PPG 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 451 G-ASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLI-EKPMGV 528
Cdd:PTZ00014 459 GfKVFIGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGKSV 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 529 LALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTD 608
Cdd:PTZ00014 538 LSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAKVDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPN 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 609 PFVAGIWKDAEfagicaAEMNETAfgmrsrKGMFRTvSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVL 688
Cdd:PTZ00014 618 PLVRDLFEGVE------VEKGKLA------KGQLIG-SQF-LNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVL 683
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 689 EQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVF 761
Cdd:PTZ00014 684 IQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKYLDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVF 756
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
92-763 |
2.36e-144 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 462.98 E-value: 2.36e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLI--YTYSGLFCVVINPYKKLPiysEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQERE---DQS 166
Cdd:cd14891 1 AGILHNLEERSKLDNQrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMCLGSGrmqNQS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 167 ILCTGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQKG---ELEHQLLQANPILEAFGNSKTVKNDNSSRFG 243
Cdd:cd14891 78 IVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRKLsvtSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 244 KFIRINFDMSGY-ISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVD 321
Cdd:cd14891 158 KFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGcVSDDNID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 322 DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF----TQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFL 397
Cdd:cd14891 238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFdeedTSEGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 398 RPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRtHRQGASFIGILDIAGFEIFDI-NSFEQICI 476
Cdd:cd14891 318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFEQLLI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 477 NYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHN 555
Cdd:cd14891 397 NYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLHKTHK 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 556 KHPKFIVPDMRSKSH-FAVVHYAGRVDYSADQWLMKNMDplnenvvglmqnstdpfvagiwkdaefagICAAEMNETafg 634
Cdd:cd14891 476 RHPCFPRPHPKDMREmFIVKHYAGTVSYTIGSFIDKNND-----------------------------IIPEDFEDL--- 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 635 mrsrkgmFRTvSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQ 714
Cdd:cd14891 524 -------LAS-SAKFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLPTRVTYA 595
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 715 EFRHRY-EILTPDVIP------KNFIDGkesvrkMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14891 596 ELVDVYkPVLPPSVTRlfaendRTLTQA------ILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
92-763 |
1.73e-142 |
|
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: 459.37 E-value: 1.73e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFK--GKKRHE-------MPPHIFAIADTAYRSMLQE- 161
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMSEi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 162 REDQSILCTGESGAGKTENTKKVIQYLAHVaGATRNKSLNAAAQqniVQKGELEHQLLQANPILEAFGNSKTVKNDNSSR 241
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTL-GNGEEGAPNEGEE---LGKLSIMDRVLQSNPILEAFGNARTLRNDNSSR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 242 FGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEY--------LLEGVDNYRFlVNR 313
Cdd:cd14908 157 FGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYefhdgitgGLQLPNEFHY-TGQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 314 G--ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAML---QDDRVIQKVCHLLGLP 388
Cdd:cd14908 236 GgaPDLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFESKEEDGAAEIaeeGNEKCLARVAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 389 VIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGA-SFIGILDIAGFEIFD 467
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIrSSVGVLDIFGFECFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 468 INSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFP-KANDKS 545
Cdd:cd14908 396 HNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDAN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 546 FVEKL--------QKTHNKHPKFIVPD-MRSKSHFAVVHYAGRVDYSADQWLM-KNMDPLnenvvglmqnstdPFVAGIw 615
Cdd:cd14908 475 YASRLyetylpekNQTHSENTRFEATSiQKTKLIFAVRHFAGQVQYTVETTFCeKNKDEI-------------PLTADS- 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 616 kdaefagicaaemnetafgmrsrkgMFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNG 695
Cdd:cd14908 541 -------------------------LFESGQQF-KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYGG 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 696 VLEGIRICRQGFPNRVPFQEFRHRYEILTP----DVIPKNFID---GKESVRKMITAL-------------DIDTNLYRI 755
Cdd:cd14908 595 VLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipeVVLSWSMERldpQKLCVKKMCKDLvkgvlspamvsmkNIPEDTMQL 674
|
....*...
gi 1767286957 756 GQSKVFFR 763
Cdd:cd14908 675 GKSKVFMR 682
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
93-726 |
1.10e-140 |
|
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: 452.07 E-value: 1.10e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEF-----------KGKKRHEMPPHIFAIADTAYRSM-- 158
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstRNKGSDPMPPHIYQVAGEAYKAMml 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 159 --LQEREDQSILCTGESGAGKTENTKKVIQYLAHvAGATRNkslnAAAQQNIVQKGELEHQLLQANPILEAFGNSKTVKN 236
Cdd:cd14900 82 glNGVMSDQSILVSGESGSGKTESTKFLMEYLAQ-AGDNNL----AASVSMGKSTSGIAAKVLQTNILLESFGNARTLRN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 237 DNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEyllegvDNYRflvnrgit 316
Cdd:cd14900 157 DNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKR------DMYR-------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 317 lpnvddvqefhSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSD-QAMLQDDRVIQKV------CHLLGLPV 389
Cdd:cd14900 223 -----------RVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDrLGQLKSDLAPSSIwsrdaaATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 390 IELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRIN---KSLDRTHRQGAS-FIGILDIAGFEI 465
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSSKSHGGLhFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 466 FDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI-EKPMGVLALLDEECLFPKANDK 544
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLIsQRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 545 SFVEKLQKTHNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNStdpfvagiwkdaefagi 623
Cdd:cd14900 451 TLASKLYRACGSHPRFSASRIqRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFVYG----------------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 624 caaemnetafgmrsrkGMFrtvsqlhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRIC 703
Cdd:cd14900 514 ----------------LQF-------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
|
650 660
....*....|....*....|...
gi 1767286957 704 RQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14900 571 RAGFPIRLLHDEFVARYFSLARA 593
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
92-763 |
4.63e-140 |
|
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: 451.32 E-value: 4.63e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAHVAGATRNKSLNaaaqqnivqkgelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA---------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNR--GITLPNVDDVQEFHS 328
Cdd:cd14904 146 DGRGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSlaQMQIPGLDDAKLFAS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 329 TINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQkVCHLLGLPVIELQKAFLRPRIKVGREFV 408
Cdd:cd14904 226 TQKSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 409 NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFN 488
Cdd:cd14904 305 TVPLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 489 NTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHN---KHPKFIVPDM 565
Cdd:cd14904 385 TDVFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkDNESIDFPKV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 RsKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagiCAAEMNETAFGmRSRKGMFRTV 645
Cdd:cd14904 464 K-RTQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE----APSETKEGKSG-KGTKAPKSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 646 SQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd14904 538 SQF-KTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFP 616
|
650 660 670
....*....|....*....|....*....|....*....
gi 1767286957 726 DVIPKNfiDGKESVRKMITALDIDTNL-YRIGQSKVFFR 763
Cdd:cd14904 617 PSMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
92-716 |
2.85e-139 |
|
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: 451.65 E-value: 2.85e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFK--------GKKRHEMPPHIFAIADTAYRSMLQ-E 161
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 162 REDQSILCTGESGAGKTENTKKVIQYLAHVaGATRNKSLNAAAQQNIVQKgelehQLLQANPILEAFGNSKTVKNDNSSR 241
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSV-GRDQSSTEQEGSDAVEIGK-----RILQTNPILESFGNAQTIRNDNSSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 242 FGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSaKEKSEYL-LEGVDNYRFLVNRGIT---- 316
Cdd:cd14902 155 FGKFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGAD-KTLLDLLgLQKGGKYELLNSYGPSfark 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 317 -LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRV---IQKVCHLLGLPVIEL 392
Cdd:cd14902 234 rAVADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASrfhLAKCAELMGVDVDKL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 393 QKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD--------RTHRQGASFIGILDIAGFE 464
Cdd:cd14902 314 ETLLSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFE 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 465 IFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKAND 543
Cdd:cd14902 394 SLNRNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYP-SNAACLALFDdKSNGLFSLLDQECLMPKGSN 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 544 KSFVEKLQKTHNKHPKFIVPdmrskshfavvHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAGI 623
Cdd:cd14902 473 QALSTKFYRYHGGLGQFVVH-----------HFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSP 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 624 CAaemnETAFGMRSRKGMFRT--VSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIR 701
Cdd:cd14902 542 GA----DNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVR 617
|
650
....*....|....*
gi 1767286957 702 ICRQGFPNRVPFQEF 716
Cdd:cd14902 618 IARHGYSVRLAHASF 632
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
92-761 |
7.77e-138 |
|
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: 445.20 E-value: 7.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRH-EMPPHIFAIADTAYRSMLQEREDQSILCT 170
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAhvagATRNKSLNAAAQQNIvqkgelehqlLQANPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14876 81 GESGAGKTEATKQIMRYFA----SAKSGNMDLRIQTAI----------MAANPVLEAFGNAKTIRNNNSSRFGRFMQLDV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTI 330
Cdd:cd14876 147 ASEGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKK---SDQAMLQDD--RVIQKVCHLLGLPVIELQKAFLRPRIKVGR 405
Cdd:cd14876 227 ESLKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEqgvDDAAAISNEslEVFKEACSLLFLDPEALKRELTVKVTKAGG 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 406 EFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGAsFIGILDIAGFEIFDINSFEQICINYTNEKLQQ 485
Cdd:cd14876 307 QEIEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIEPPGGFKN-FMGMLDIFGFEVFKNNSLEQLFINITNEMLQK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 486 LFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTID-LIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPD 564
Cdd:cd14876 386 NFIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 565 MRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIwkdaeFAGIcAAEMNETAfgmrsrKGMFrT 644
Cdd:cd14876 465 VDSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKAL-----FEGV-VVEKGKIA------KGSL-I 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 645 VSQLHKeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILT 724
Cdd:cd14876 532 GSQFLK-QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLD 610
|
650 660 670
....*....|....*....|....*....|....*..
gi 1767286957 725 PDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVF 761
Cdd:cd14876 611 LGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
92-763 |
8.44e-130 |
|
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: 422.27 E-value: 8.44e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLahvagatrnkslnAAAQQNivQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFd 251
Cdd:cd14896 81 HSGSGKTEAAKKIVQFL-------------SSLYQD--QTEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRLHL- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYrFLVNRGIT--LPNVDDVQEFHST 329
Cdd:cd14896 145 QHGVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETY-YYLNQGGAcrLQGKEDAQDFEGL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQ--AMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREF 407
Cdd:cd14896 224 LKALQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 408 VNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGA-SFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd14896 304 VSRPLPVEGAIDARDALAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERLQLF 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDfGLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDM 565
Cdd:cd14896 384 SSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQL 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 566 rSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefagicaaemnETAFGMRSRKGmfrTV 645
Cdd:cd14896 463 -PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEA-----------EPQYGLGQGKP---TL 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 646 SQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd14896 528 ASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALGS 607
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 726 DVIPkNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14896 608 ERQE-ALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
92-763 |
4.75e-128 |
|
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: 419.02 E-value: 4.75e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSlnaaaqqnIVQKgelehqlLQA-NPILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGGVL--------SVEK-------LNAaLTVLEAFGNVRTALNGNATRFSQLFSLDF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLE--GVDNYRFLVnrgiTLPNVDDVQ---- 324
Cdd:cd01386 146 DQAGQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNqlAESNSFGIV----PLQKPEDKQkaaa 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 325 EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 404
Cdd:cd01386 222 AFSKLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAIFKHHLSGG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 405 REFVNKAQNQEQAEF------------AVEAIAKASYERLFKWLVTRINKSLDRTHRQGASfIGILDIAGFE------IF 466
Cdd:cd01386 302 PQQSTTSSGQESPARsssggpkltgveALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQnpahsgSQ 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 467 DINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEK---------------PMGVLAL 531
Cdd:cd01386 381 RGATFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVEVDFDLPELSPGALVALIDQapqqalvrsdlrdedRRGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 532 LDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKS----HFAVVHYAGR--VDYSADQWLMK-NMDPLNENVVGLMQ 604
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSegplQFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 605 NSTDPfvagiwkdaefagicaaemnetaFGMRSRKGMFrtvSQLhKEQLTKLMTTLRNTSPHFVRCIIPNH--EKKSGK- 681
Cdd:cd01386 541 ESQKE-----------------------TAAVKRKSPC---LQI-KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERSt 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 682 ---------INSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVIPKNF-----IDGKESVRKMITALD 747
Cdd:cd01386 594 sspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELD 673
|
730
....*....|....*.
gi 1767286957 748 IDTNLYRIGQSKVFFR 763
Cdd:cd01386 674 LEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
92-763 |
2.37e-121 |
|
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: 399.18 E-value: 2.37e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYS-SLIYTYSGLFCVVINPYKKLPIYSEDLIEEF-KGKKRHEMPPHIFAIADTAYRSM-LQEREDQSIL 168
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYlALPDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 169 CTGESGAGKTENTKKVIQYLahvaGATRNKSLNAAAQQNIVQKgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRI 248
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYL----GQLSYMHSSNTSQRSIADK--IDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 249 NFD-MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEY-LLEGVDNYRFL------VNRGITLPNV 320
Cdd:cd14875 155 YFDpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLnggntfVRRGVDGKTL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 321 DDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKkSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLrpr 400
Cdd:cd14875 235 DDAHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQ-NDKAQIADETPFLTACRLLQLDPAKLRECFL--- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 401 IKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLD-RTHRQGASFIGILDIAGFEIFDINSFEQICINYT 479
Cdd:cd14875 311 VKSKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 480 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKL-QKTHNKHP 558
Cdd:cd14875 391 NESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLwDQWANKSP 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 559 KFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaemnetafGMRSR 638
Cdd:cd14875 471 YFVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEK--------------GLARR 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 639 KgmfRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRH 718
Cdd:cd14875 537 K---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCR 613
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 719 RYEILTPDVIPKNFIDGKESvRKMITALDIDTNLYR-------IGQSKVFFR 763
Cdd:cd14875 614 YFYLIMPRSTASLFKQEKYS-EAAKDFLAYYQRLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
92-763 |
2.83e-121 |
|
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: 398.49 E-value: 2.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRH-----EMPPHIFAIADTAYRSMLQEREDQ 165
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQADTSrgfpsDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 166 SILCTGESGAGKTENTKKVIQYLAHvagatrNKSLNAAAQQNIVqkgelehqlLQANPILEAFGNSKTVKNDNSSRFGKF 245
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAY------GHSTSSTDVQSLI---------LGSNPLLESFGNAKTLRNNNSSRFGKF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 246 IRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRG--ITLPNVDDV 323
Cdd:cd14886 146 IKLLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFL-NASkcYDAPGIDDQ 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 324 QEFHSTINSMRIMgFADDEISSIMRVVSAVLLLGNLEFTQEKKS---DQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPR 400
Cdd:cd14886 225 KEFAPVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKV 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 401 IKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINK--SLDRTHRQgasFIGILDIAGFEIFDINSFEQICINY 478
Cdd:cd14886 304 VVINNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEiiQFDADARP---WIGILDIYGFEFFERNTYEQLLINY 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 479 TNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIEKP-MGVLALLDEECLFPKANDKSFVEKLqKTHNKH 557
Cdd:cd14886 381 ANERLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPnLSIFSFLEEQCLIQTGSSEKFTSSC-KSKIKN 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 558 PKFIvPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaaemNETAfgmrS 637
Cdd:cd14886 459 NSFI-PGKGSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNKAFSDIP---------NEDG----N 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 638 RKGMFrtVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFR 717
Cdd:cd14886 525 MKGKF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFF 602
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1767286957 718 HRYEILT--PDVIPKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14886 603 HRNKILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
92-725 |
3.76e-121 |
|
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: 398.45 E-value: 3.76e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKR-HEMPPHIFAIADTAYRSMLQERE--DQSI 167
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 168 LCTGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 247
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASPTSWESHKIAER-------IEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 248 INFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLpnvdDVQEFH 327
Cdd:cd14880 154 LQLNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNL----EEDCFE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 328 STINSMRIMGFADDEISSIMRVVSAVLLLGNLEFT---QEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVG 404
Cdd:cd14880 230 VTREAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFAdseDEAQPCQPMDDTKESVRTSALLLKLPEDHLLETLQIRTIRAG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 405 REFV--NKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEK 482
Cdd:cd14880 310 KQQQvfKKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 483 LQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE-KPMGVLALLDEECLFPKANDKS-FVEKLQKTHNKHPKF 560
Cdd:cd14880 390 LQQHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCL 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 561 IVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEfagicaAEMNETAFGMRSRKG 640
Cdd:cd14880 469 GHNKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------EEKTQEEPSGQSRAP 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 641 MFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 720
Cdd:cd14880 543 VLTVVSKF-KASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERY 621
|
....*
gi 1767286957 721 EILTP 725
Cdd:cd14880 622 KLLRR 626
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
93-763 |
1.46e-120 |
|
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276860 [Multi-domain] Cd Length: 704 Bit Score: 398.17 E-value: 1.46e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHeMPPHIFAIADTAYRSM---LQE----RED 164
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYDLHKYREEMPGWTA-LPPHVFSIAEGAYRSLrrrLHEpgasKKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 165 QSILCTGESGAGKTENTKKVIQYLAHVAGATRNKSlNAAAQQNIVQKgelehQLLQANPILEAFGNSKTVKNDNSSRFGK 244
Cdd:cd14895 81 QTILVSGESGAGKTETTKFIMNYLAESSKHTTATS-SSKRRRAISGS-----ELLSANPILESFGNARTLRNDNSSRFGK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 245 FIRINF-----DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG----I 315
Cdd:cd14895 155 FVRMFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLSAQEFQYISGgqcyQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 316 TLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSD---------------QAMLQDDRVIQK 380
Cdd:cd14895 235 RNDGVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQH 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 381 ---VCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDR----------T 447
Cdd:cd14895 315 ldiVSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQrqfalnpnkaA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 448 HRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDlQPTIDLIE-KPM 526
Cdd:cd14895 395 NKDTTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPS 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 527 GVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQN 605
Cdd:cd14895 474 GIFSLLDEECVVPKGSDAGFARKLYQRLQEHSNFSASRTdQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGK 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 606 STDPFVAGIwkdaeFAGICAAEMNETAFG---MRSRKGMFRTV---SQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKS 679
Cdd:cd14895 554 TSDAHLREL-----FEFFKASESAELSLGqpkLRRRSSVLSSVgigSQF-KQQLASLLDVVQQTQTHYIRCIKPNDESAS 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 680 GKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILtpdVIPKNFIDGKESvrKMITALDIDTnlYRIGQSK 759
Cdd:cd14895 628 DQFDMAKVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLL---VAAKNASDATAS--ALIETLKVDH--AELGKTR 700
|
....
gi 1767286957 760 VFFR 763
Cdd:cd14895 701 VFLR 704
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
92-723 |
1.36e-118 |
|
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: 393.19 E-value: 1.36e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKR-HEMPPHIFAIADTAYRSMLQEREDQSILC 169
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 170 TGESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQNIVQKgelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRIN 249
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNNNSIEK-----DILTSNPILEAFGNSRTTKNHNSSRFGKFLKIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 250 FDMS-GYISGANIEFYLLEKSRVL-RQAQDERSFHIFYQILRGCSAKEKSEYLLEG-VDNYRFLVNR------------- 313
Cdd:cd14906 156 FRSSdGKIDGASIETYLLEKSRIShRPDNINLSYHIFYYLVYGASKDERSKWGLNNdPSKYRYLDARddvissfksqssn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 314 --GITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRV---IQKVCHLLGLP 388
Cdd:cd14906 236 knSNHNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVtasLESVSKLLGYI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 389 VIELQKAFLRPRIKV-GREFVNKAQNQ-EQAEFAVEAIAKASYERLFKWLVTRINKSLDR----------THRQGASFIG 456
Cdd:cd14906 316 ESVFKQALLNRNLKAgGRGSVYCRPMEvAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 457 ILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIE-KPMGVLALLDEE 535
Cdd:cd14906 396 VLDIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEkKSDGILSLLDDE 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 536 CLFPKANDKSFVEKLQKTHNKHPKFIVPDMrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIW 615
Cdd:cd14906 475 CIMPKGSEQSLLEKYNKQYHNTNQYYQRTL-AKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLF 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 616 KdaefagicAAEMNETAFGMRSRKGMfrTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNG 695
Cdd:cd14906 554 Q--------QQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVG 623
|
650 660
....*....|....*....|....*...
gi 1767286957 696 VLEGIRICRQGFPNRVPFQEFRHRYEIL 723
Cdd:cd14906 624 VLNTIKVRKMGYSYRRDFNQFFSRYKCI 651
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
92-720 |
3.23e-112 |
|
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: 374.82 E-value: 3.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIE--------EFKGKKRHEMP--PHIFAIADTAYRSMLQ 160
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRgyaydhnsQFGDRVTSTDPrePHLFAVARAAYIDIVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 161 EREDQSILCTGESGAGKTENTKKVIQYLAHVAG--ATRNKSLNAAAQQNIVQKGELEHQLLQANPILEAFGNSKTVKNDN 238
Cdd:cd14899 81 NGRSQSILISGESGAGKTEATKIIMTYFAVHCGtgNNNLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 239 SSRFGKFIRINF-DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRG---CSAKEKSEYLL--EGVDNYRfLVN 312
Cdd:cd14899 161 SSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnnCVSKEQKQVLAlsGGPQSFR-LLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 313 RGITLPNVDDVQ---EFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ--EKKSDQAMLQDDRVIQ-------- 379
Cdd:cd14899 240 QSLCSKRRDGVKdgvQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafdh 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 380 --KVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRT---------- 447
Cdd:cd14899 320 ftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgades 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 448 ----HRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLIE 523
Cdd:cd14899 400 dvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELFE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 524 -KPMGVLALLDEECLFPKANDKSFVEKLQKTHNK---HPKF-IVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNEN 598
Cdd:cd14899 479 hRPIGIFSLTDQECVFPQGTDRALVAKYYLEFEKknsHPHFrSAPLIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCES 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 599 VVGLMQNSTDPFVAGIWKDAEFAGICAAEMNETAFGMRSRKGMFRT----VSQLHKEQLTKLMTTLRNTSPHFVRCIIPN 674
Cdd:cd14899 559 AAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVRCIKPN 638
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1767286957 675 HEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRY 720
Cdd:cd14899 639 DSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
92-763 |
4.54e-102 |
|
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: 342.77 E-value: 4.54e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYsedlIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYlaHVAGatrnkslnaaaqqnIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSG--------------VKEDNEISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDVQEFHSTIN 331
Cdd:cd14937 141 EYQNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 332 SMRIMGFADDEiSSIMRVVSAVLLLGNLEFTQ-EK--KSDQAMLQDDR--VIQKVCHLLGLPVIELQKAFLRPRIKVGRE 406
Cdd:cd14937 221 SFDKMNMHDMK-DDLFLTLSGLLLLGNVEYQEiEKggKTNCSELDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 407 FVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDrTHRQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd14937 300 KIEIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLN-NNKELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDFIDFGLDlQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMR 566
Cdd:cd14937 379 YLYIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 567 SKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFAgicaaemneTAFGmrsRKGMfrtVS 646
Cdd:cd14937 458 INKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEVS---------ESLG---RKNL---IT 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 647 QLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRIcRQGFPNRVPFQEFRHRYEILTPD 726
Cdd:cd14937 523 FKYLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYS 601
|
650 660 670
....*....|....*....|....*....|....*..
gi 1767286957 727 VIPKNFIDGKESVrKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14937 602 TSKDSSLTDKEKV-SMILQNTVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
89-762 |
1.47e-99 |
|
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: 335.67 E-value: 1.47e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 89 LNEASVLHNLKDRYYSSLIYTY---SGLfcVVINPYKKLPIYSEDLIEEFK-------GKKRHEMPPHIFAIADTAYRSM 158
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 159 LQEREDQSILCTGESGAGKTEN----TKKVIQYLAHVAGATRnkslnaaaqqnivqkgeLEHQLLQANPILEAFGNSKTV 234
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESrrllLRQLLRLSSHSKKGTK-----------------LSSQISAAEFVLDSFGNAKTL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 235 KNDNSSRFGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG 314
Cdd:cd14879 142 TNPNASRFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLASYG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 315 ----ITLPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ--EKKSDQAMLQDDRVIQKVCHLLGLP 388
Cdd:cd14879 222 chplPLGPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYdhEGGEESAVVKNTDVLDIVAAFLGVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 389 VIELQKAfLRPRIK-VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHRQGASFIGILDIAGFEIFD 467
Cdd:cd14879 302 PEDLETS-LTYKTKlVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 468 ---INSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEwdfidfgLDLQPTID-------LIEKPMGVLALLDEECL 537
Cdd:cd14879 381 stgGNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-------VPATSYFDnsdcvrlLRGKPGGLLGILDDQTR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 538 -FPKANDKSFVEKLQKTHNKHPKFIV----PDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLnenvvglmqnSTDpFVA 612
Cdd:cd14879 454 rMPKKTDEQMLEALRKRFGNHSSFIAvgnfATRSGSASFTVNHYAGEVTYSVEGFLERNGDVL----------SPD-FVN 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 613 giwkdaefagicaaemnetafgmrsrkgMFRTVSQLhKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLR 692
Cdd:cd14879 523 ----------------------------LLRGATQL-NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIR 573
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 693 CNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPdvipknFIDGKESVRKMITALDIDTNLYRIGQSKVFF 762
Cdd:cd14879 574 SLGLPELAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
92-763 |
2.81e-97 |
|
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: 329.47 E-value: 2.81e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYS---EDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSIL 168
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYStmvSQLYLSSSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 169 CTGESGAGKTENTKKVIQYLAHVAGATRNKslnaaaqqnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRI 248
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASSSRTT---------------FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 249 NF-DMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLvNRGI-----TLPNVDD 322
Cdd:cd14878 146 QFcERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYL-NQTMredvsTAERSLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 323 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 402
Cdd:cd14878 225 REKLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 403 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSL---DRTHRQGASFIGILDIAGFEIFDINSFEQICINYT 479
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLqsqDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 480 NEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTID-LIEKPMGVLALLDEECLFPKANDKSFVEKLQ---KTHN 555
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQsllESSN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 556 KHPKFI--------VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAefagicaae 627
Cdd:cd14878 465 TNAVYSpmkdgngnVALKDQGTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLLFVMKTSENVVINHLFQSK--------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 628 mnetafgmrsrkgMFRTVSQLHKeQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGF 707
Cdd:cd14878 536 -------------LVTIASQLRK-SLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGY 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 708 PNRVPFQEFRHRYEILTpDVIP--KNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 763
Cdd:cd14878 602 PVRLSFSDFLSRYKPLA-DTLLgeKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
92-763 |
2.44e-95 |
|
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276852 Cd Length: 725 Bit Score: 326.22 E-value: 2.44e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYS--------SLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQERE 163
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 164 DQSILCTGESGAGKTENTKKVIQYLAHVAgaTRNKSLNAAAqqnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFG 243
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVS--DRRHGADSQG---------LEARLLQSGPVLEAFGNAHTVLNANSSRFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 244 KFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRgitlpnvddv 323
Cdd:cd14887 150 KMLLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQKSSAGEGDPESTDLRR---------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 324 qefhsTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ------------------------------EKKSDQAMLQ 373
Cdd:cd14887 220 -----ITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTdqepetskkrkltsvsvgceetaadrshssEVKCLSSGLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 374 DDRVIQK----VCHLLGLP--VIELQKAFLRPRIKVGREfVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRT 447
Cdd:cd14887 295 VTEASRKhlktVARLLGLPpgVEGEEMLRLALVSRSVRE-TRSFFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 448 HR-------------QGASFIGILDIAGFEIF---DINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREG--IEWDFI 509
Cdd:cd14887 374 AKpsesdsdedtpstTGTQTIGILDLFGFEDLrnhSKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCS 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 510 DFGLDLQPTIDLIEKPMGVLALL-------------------------DEECLFP-----KANDKSFVEKLQK--THNKH 557
Cdd:cd14887 454 AFPFSFPLASTLTSSPSSTSPFSptpsfrsssafatspslpsslsslsSSLSSSPpvwegRDNSDLFYEKLNKniINSAK 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 558 PKFIVPDM-RSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaEFAGICAAEMNEtafGMR 636
Cdd:cd14887 534 YKNITPALsRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACS-----------TYTRLVGSKKNS---GVR 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 637 SRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 716
Cdd:cd14887 600 AISSRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVEL 679
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1767286957 717 RHRYEILTPDVIpKNFIDGKESVRKMITALDIDTNLYRIGQSKVFFR 763
Cdd:cd14887 680 WRRYETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
93-725 |
1.96e-92 |
|
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: 312.99 E-value: 1.96e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKlpIYSEDLIEEFKGKKRHeMPPHIFAIADTAYRSMLQErEDQSILCTGE 172
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQDLLVH-GNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHvagatRNKSLNAaaqqnivqkgeLEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDm 252
Cdd:cd14898 78 SGSGKTENAKLVIKYLVE-----RTASTTS-----------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 sGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQIlrgCSAKE---KSEYLlegvdNYRFLVNRGITLpnVDDVQEFHST 329
Cdd:cd14898 141 -GKITGAKFETYLLEKSRVTHHEKGERNFHIFYQF---CASKRlniKNDFI-----DTSSTAGNKESI--VQLSEKYKMT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 330 INSMRIMGFADdeISSIMRVVSAVLLLGNLEFTQEkksDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVN 409
Cdd:cd14898 210 CSAMKSLGIAN--FKSIEDCLLGILYLGSIQFVND---GILKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 410 KAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRThrqGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNN 489
Cdd:cd14898 285 VFNTLKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIK 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 490 TMFILEQEEYQREGIEWDFIDFgLDLQPTIDLIEKPMGVLALLDEECLFPKANDKSFVEKLqKTHNKHpkFIVPDMRSKs 569
Cdd:cd14898 362 KMFRAKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNLLVKI-KKYLNG--FINTKARDK- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 570 hFAVVHYAGRVDYSADQWLMKNMDPLNENVVGlmqnstDPFVAgiwkdaefagicaaemnetafgmrsRKGMFRTVSQLH 649
Cdd:cd14898 437 -IKVSHYAGDVEYDLRDFLDKNREKGQLLIFK------NLLIN-------------------------DEGSKEDLVKYF 484
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 650 KEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTP 725
Cdd:cd14898 485 KDSMNKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
92-715 |
2.55e-82 |
|
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: 286.80 E-value: 2.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKGKKRHE-------MPPHIFAIADTAYRSMLQERE 163
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 164 DQSILCTGESGAGKTENTKKVIQYLAHVagatrnkslnaaaqQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 243
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYI--------------QTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 244 KFIRINFD---------MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEY-LLEGVDNYRFLVN- 312
Cdd:cd14884 147 RINLLIFEeventqknmFNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDLARRnLVRNCGVYGLLNPd 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 313 -----RGIT--------------LPNVDDVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNleftqekksdqamlq 373
Cdd:cd14884 227 eshqkRSVKgtlrlgsdsldpseEEKAKDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGN--------------- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 374 ddRVIQKVCHLLGLPVIELQKAFLRPRIKVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRIN---------KSL 444
Cdd:cd14884 292 --RAYKAAAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINrnvlkckekDES 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 445 DRTH--RQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGlDLQPTIDLI 522
Cdd:cd14884 370 DNEDiySINEAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 523 EKpmgVLALLDE-----ECLFPKANDKSFV-----EKLQKTHNKHPK-FIVPDMRS---------KSHFAVVHYAGRVDY 582
Cdd:cd14884 449 AK---IFRRLDDitklkNQGQKKTDDHFFRyllnnERQQQLEGKVSYgFVLNHDADgtakkqnikKNIFFIRHYAGLVTY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 583 SADQWLMKNMDPLNENVVGLMQNSTDPFvagiwkdaefagicaaeMNETAFGmrSRKGMFRTVSQLHKEQLTKLMTTLRN 662
Cdd:cd14884 526 RINNWIDKNSDKIETSIETLISCSSNRF-----------------LREANNG--GNKGNFLSVSKKYIKELDNLFTQLQS 586
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 663 TSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQE 715
Cdd:cd14884 587 TDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
93-763 |
4.20e-79 |
|
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: 276.97 E-value: 4.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLP-IYSEDLIEEFKgkKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAhVAGATRNKSLnaaaqqnivqkgelEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFD 251
Cdd:cd14905 80 ESGSGKSENTKIIIQYLL-TTDLSRSKYL--------------RDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 252 MSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRG-ITLPNVDDVQEFHSTI 330
Cdd:cd14905 145 LYGEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQGGsISVESIDDNRVFDRLK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 331 NSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQekKSDQAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIKVgrefVNK 410
Cdd:cd14905 225 MSFVFFDFPSEKIDLIFKTLSFIIILGNVTFFQ--KNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMP----VNE 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 411 AQNQEqaefavEAIAKASYERLFKWLVTRINKSLDRThrQGASFIGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNT 490
Cdd:cd14905 299 AVENR------DSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 491 MFILEQEEYQREGIEW-DFIDFGlDLQPTIDLIEKpmgVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFivpdMRSKS 569
Cdd:cd14905 371 VLKQEQREYQTERIPWmTPISFK-DNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLF----GKKPN 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 570 HFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGiwKDAEF-AGICAAEMNEtafgmrsrkgMFRTVSQL 648
Cdd:cd14905 443 KFGIEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFS--RDGVFnINATVAELNQ----------MFDAKNTA 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 649 HKEQLT--KLMTTLRNTSP-----------------------------------------------HFVRCIIPNHEKKS 679
Cdd:cd14905 511 KKSPLSivKVLLSCGSNNPnnvnnpnnnsgggggggnsgggsgsggstyttysstnkainnsncdfHFIRCIKPNSKKTH 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 680 GKINSNLVLEQLRCNGVLEGIRICRQGFP----NRVPFQEFRHRYEiltpdvIPKNFIDGKESVRKmiTALDIDTNL--- 752
Cdd:cd14905 591 LTFDVKSVNEQIKSLCLLETTRIQRFGYTihynNKIFFDRFSFFFQ------NQRNFQNLFEKLKE--NDINIDSILppp 662
|
730
....*....|.
gi 1767286957 753 YRIGQSKVFFR 763
Cdd:cd14905 663 IQVGNTKIFLR 673
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
93-725 |
7.69e-79 |
|
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: 275.07 E-value: 7.69e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPiysEDL-IEEFKGKKRHempPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDVG---NPLtLTSTRSSPLA---PQLLKVVQEAVRQQSETGYPQAIILSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGatrnkslnaaaqqnivqkGELE----HQLLQANPILEAFGNSKTVKNDNSSRFGKFIR 247
Cdd:cd14881 76 TSGSGKTYASMLLLRQLFDVAG------------------GGPEtdafKHLAAAFTVLRSLGSAKTATNSESSRIGHFIE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 248 INFdMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEG--VDNYRFLVNRGITLPNVDDVQE 325
Cdd:cd14881 138 VQV-TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDGysPANLRYLSHGDTRQNEAEDAAR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 326 FHSTINSMRIMG--FADdeissIMRVVSAVLLLGNLEFTQEKKSDQAMLQDDRvIQKVCHLLGLPVIELQKAFLRPRIKV 403
Cdd:cd14881 217 FQAWKACLGILGipFLD-----VVRVLAAVLLLGNVQFIDGGGLEVDVKGETE-LKSVAALLGVSGAALFRGLTTRTHNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 404 GREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINkSLDRTHRQGAS-----FIGILDIAGFEIFDINSFEQICINY 478
Cdd:cd14881 291 RGQLVKSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SLKRLGSTLGThatdgFIGILDMFGFEDPKPSQLEHLCINL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 479 TNEKLQQLFNNTMFILEQEEYQREGIEWDF-IDFgLDLQPTIDLIEK-PMGVLALLDEECLfPKANDKSFVEKLQKTHNK 556
Cdd:cd14881 370 CAETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQ 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 557 HPKFIVPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTdpfvagiwkdaefagiCaaemnetAFGmr 636
Cdd:cd14881 448 NPRLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYKQN----------------C-------NFG-- 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 637 srkgmFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEF 716
Cdd:cd14881 503 -----FATHTQDFHTRLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAF 577
|
....*....
gi 1767286957 717 RHRYEILTP 725
Cdd:cd14881 578 NARYRLLAP 586
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
93-763 |
1.84e-75 |
|
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: 265.07 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGE 172
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 173 SGAGKTENTKKVIQYLAHVAgatrnKSLNAAAQqnivqkgelehQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDM 252
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLG-----DGNRGATG-----------RVESSIKAILALVNAGTPLNADSTRCILQYQLTFGS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 253 SGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEK-SEYLLEGVDNYRFL----VNRGITLPNVDD----- 322
Cdd:cd14882 146 TGKMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRlKEYNLKAGRNYRYLrippEVPPSKLKYRRDdpegn 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 323 VQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKSdqAMLQDDRVIQKVCHLLGLPVIELQKAFLRPRIK 402
Cdd:cd14882 226 VERYKEFEEILKDLDFNEEQLETVRKVLAAILNLGEIRFRQNGGY--AELENTEIASRVAELLRLDEKKFMWALTNYCLI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 403 VGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINK--SLDRTHRQGASFIGILDIAGFEIFDINSFEQICINYTN 480
Cdd:cd14882 304 KGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMkmSFPRAVFGDKYSISIHDMFGFECFHRNRLEQLMVNTLN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 481 EKLQQLFNNTMFILEQEEYQREGIEWDFIDFgLDLQPTID-LIEKPMGVLALLDEEClfPKANDKSFVekLQKTHNKHPK 559
Cdd:cd14882 384 EQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDDAS--RSCQDQNYI--MDRIKEKHSQ 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 560 FIVPDmrSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKdaefagicaaemNETAFGMRSRK 639
Cdd:cd14882 459 FVKKH--SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFT------------NSQVRNMRTLA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 640 GMFRTVSQlhkEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHR 719
Cdd:cd14882 525 ATFRATSL---ELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRR 601
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1767286957 720 YEILTPDvIPKNFIDGKESVRKMITALDIDTnlYRIGQSKVFFR 763
Cdd:cd14882 602 YQFLAFD-FDETVEMTKDNCRLLLIRLKMEG--WAIGKTKVFLK 642
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
92-763 |
5.59e-75 |
|
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: 263.27 E-value: 5.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 92 ASVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFkgkkrhemppHIFAIADTAYRSMLQERED-QSILCT 170
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 171 GESGAGKTENTKKVIQYLAhvagaTRNKSLNAAAQQNIVQKgelehqllqanpILEAFGNSKTVKNDNSSRFGKFIRINF 250
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT-----SQPKSKVTTKHSSAIES------------VFKSFGCAKTLKNDEATRFGCSIDLLY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 251 DmSGYISGANIEFYL-LEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYrFLVNRGITLPNV-DDVQEFHS 328
Cdd:cd14874 134 K-RNVLTGLNLKYTVpLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKF-FYINQGNSTENIqSDVNHFKH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 329 TINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQEKKS----DQAMLQDDRVIQKVCHLLGLPVIELQkAFLRPRIKVG 404
Cdd:cd14874 212 LEDALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNPnveqDVVEIGNMSEVKWVAFLLEVDFDQLV-NFLLPKSEDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 405 REF-VNKAQNQEqaefavEAIAKASYERLFKWLVTRINKSLDRTHRQGAsfIGILDIAGFEIFDINSFEQICINYTNEKL 483
Cdd:cd14874 291 TTIdLNAALDNR------DSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERI 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 484 QQLFNNTMFILEQEEYQREGIEWDF-IDFGLDLQPTIDLI-EKPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFI 561
Cdd:cd14874 363 ENLFVKHSFHDQLVDYAKDGISVDYkVPNSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 562 VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKDAEFagicaaemnetafgmrSRKGM 641
Cdd:cd14874 443 KARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYSS----------------NTSDM 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 642 FRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYE 721
Cdd:cd14874 507 IVSQAQFILRGAQEIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYR 586
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1767286957 722 ILTPDVIPKnFIDGKESVRKMITALDID-TNLYRIGQSKVFFR 763
Cdd:cd14874 587 CLLPGDIAM-CQNEKEIIQDILQGQGVKyENDFKIGTEYVFLR 628
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
95-721 |
1.07e-71 |
|
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: 256.82 E-value: 1.07e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 95 LHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFKGKKR----------HEMPPHIFAIADTAYRSMLQERED 164
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 165 QSILCTGESGAGKTENTKKVIQYLAHVAGAT--RNKSLNAA-AQQNIVQkgelehQLLQANPILEAFGNSKTVKNDNSSR 241
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIGDETepRPDSEGASgVLHPIGQ------QILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 242 FGKFIRINFDMSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGC----SAKEKSEyLLEGVDNYRFLVNRGITL 317
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVqhdpTLRDSLE-MNKCVNEFVMLKQADPLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 318 PNVD-DVQEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEF---------------TQEKKSDQAMLQDDRVIQKV 381
Cdd:cd14893 237 TNFAlDARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggansTTVSDAQSCALKDPAQILLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 382 CHLLGLPVIELQKAFLRprikvgREFVNKAQNQ----------EQAEFAVEAIAKASYERLFKWLVTRINKSL----DRT 447
Cdd:cd14893 317 AKLLEVEPVVLDNYFRT------RQFFSKDGNKtvsslkvvtvHQARKARDTFVRSLYESLFNFLVETLNGILggifDRY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 448 HRQG----ASFIGILDIAGFEIFD--INSFEQICINYTNEKLQQLF-NNTMFI----LEQEEYQREGIEWD--FIDFGLD 514
Cdd:cd14893 391 EKSNivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENRLTVnsNVDITSE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 515 LQPTIDLIE-KPMGVLALLDEECLFPKANDKSFVEKLQKTHNKHPKFIVPDMRSKSH-------------FAVVHYAGRV 580
Cdd:cd14893 471 QEKCLQLFEdKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNEAVGGLSRPNMGADTTneylapskdwrllFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 581 DYSADQWLMKNMDPLNENVVGLMQNSTDPFVAGIWKdAEFAGICAAEMNETAFGMRSRKGMFRTVSQLHKE--------- 651
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNAVLHAVGA-AQMAAASSEKAAKQTEERGSTSSKFRKSASSAREsknitdsaa 629
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 652 -----QLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYE 721
Cdd:cd14893 630 tdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRYK 704
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
93-761 |
1.01e-64 |
|
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: 235.50 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 93 SVLHNLKDRYYSSLIYTYSGLFCVVINPYKKLPIYSEDLIEEFK-GKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTG 171
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKcIDCIEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 172 ESGAGKTENTKKVIQYLAHVAGATRNKSLNAAAQQ--------NIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFG 243
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYQVKGSRRLPTNLNDQEednihneeNTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 244 KFIRINFDmSGYISGANIEFYLLEKSRVLRQAQDERSFHIFYQILRGCSAKEKSEYLLEGVDNYRFLVNRGITLPNVDDV 323
Cdd:cd14938 162 KFCTIHIE-NEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 324 QEFHSTINSMRIMGFADDEISSIMRVVSAVLLLGNLEFTQ---------------------------EKKSDQAMLQDDR 376
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNTEIVKafrkksllmgknqcgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 377 VIQKVCHLLGLPVIELQKAFLRPRIkVGREFVNKAQNQEQAEFAVEAIAKASYERLFKWLVTRINKSLDRTHR--QGASF 454
Cdd:cd14938 321 NLLLACKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 455 IGILDIAGFEIFDINSFEQICINYTNEKLQQLFNNTMFILEQEEYQREGIEWDFIDFGLDLQPTID-LIEKPMGVLALLD 533
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNlLVGPTEGSLFSLL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 534 EECLFPKANDKSFVEKL-QKTHNKHPKFIVPD--MRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENVVGLMQNSTDPF 610
Cdd:cd14938 480 ENVSTKTIFDKSNLHSSiIRKFSRNSKYIKKDdiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMVKQSENEY 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 611 VAGI--WKDAEFAGICAAEMN----ETAFGMRSRKgmFRTVSQ----LHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKS- 679
Cdd:cd14938 560 MRQFcmFYNYDNSGNIVEEKRrysiQSALKLFKRR--YDTKNQmavsLLRNNLTELEKLQETTFCHFIVCMKPNESKREl 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 680 GKINSNLVLEQLRCNGVLEGIRICRQGFPNRVPFQEFRHRYEILTPDVipknfidgKESVRKMITALDIDTNLYRIGQSK 759
Cdd:cd14938 638 CSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNEDL--------KEKVEALIKSYQISNYEWMIGNNM 709
|
..
gi 1767286957 760 VF 761
Cdd:cd14938 710 IF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
114-255 |
4.77e-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: 198.34 E-value: 4.77e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 114 FCVVINPYKKLPIYSEDLIEEF-KGKKRHEMPPHIFAIADTAYRSMLQEREDQSILCTGESGAGKTENTKKVIQYLAHVA 192
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFyRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 193 GATRNKSLNAAAQQNIVQKGELEHQLLQANPILEAFGNSKTVKNDNSSRFGKFIRINFDMSGY 255
Cdd:cd01363 81 FNGINKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
98-704 |
5.10e-28 |
|
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: 123.31 E-value: 5.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 98 LKDRYYSSLIYTYSGLFCV-VINPYKKL------PIYSEDLIEEFKGKKRHE--MPPHIFAIAD---------------- 152
Cdd:cd14894 7 LTSRFDDDRIYTYINHHTMaVMNPYRLLqtarftSIYDEQVVLTYADTANAEtvLAPHPFAIAKqslvrlffdnehtmpl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 153 ----TAYRSMLQEReDQSILCTGESGAGKTENTKKVIQYLAHVA---------------GATRN---KSLNAAAQQNIVQ 210
Cdd:cd14894 87 pstiSSNRSMTEGR-GQSLFLCGESGSGKTELAKDLLKYLVLVAqpalskgseetckvsGSTRQpkiKLFTSSTKSTIQM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 211 KGE-------------------------------------------------------LEHQ------------------ 217
Cdd:cd14894 166 RTEeartialleakgvekyeivlldlhperwdemtsvsrskrlpqvhvdglffgfyekLEHLedeeqlrmyfknphaakk 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 218 ---LLQANPILEAFGNSKTVKNDNSSRFGKF--IRINFDMSGY---ISGANIEFYLLEKSRVLRQA------QDERSFHI 283
Cdd:cd14894 246 lsiVLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 284 FYQILRGCSAKE-----KSEYLLEGVD--NYRFLVNRGITLPNV--------DDVQEFHSTINSMRIMGFADDEISSIMR 348
Cdd:cd14894 326 LYAMVAGVNAFPfmrllAKELHLDGIDcsALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFK 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 349 VVSAVLLLGNLEFTQEKKSDQAMLQDDRVI---QKVCHLLGLPVIELQKAFLRPR---IKVGREFVNKAQNQEQAEFAVE 422
Cdd:cd14894 406 VLSAVLWLGNIELDYREVSGKLVMSSTGALnapQKVVELLELGSVEKLERMLMTKsvsLQSTSETFEVTLEKGQVNHVRD 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 423 AIAKASYERLFKWLVTRINK-------SLDRTHRQ---------GASFIGILDIAGFEIFDINSFEQICINYTNEKLQQL 486
Cdd:cd14894 486 TLARLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKLYAR 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 487 FNNTMFILEQEEYQREGIEWDfidfgldlQPTIDLIEKPMGVLALLDEECLFPKAND----------KSFVEKLQKTHNK 556
Cdd:cd14894 566 EEQVIAVAYSSRPHLTARDSE--------KDVLFIYEHPLGVFASLEELTILHQSENmnaqqeekrnKLFVRNIYDRNSS 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 557 H----PKFI------VPDMRSKSHFAVVHYAGRVDYSADQWLMKNMDPLNENV-VGLMQNSTDPFVAGIWKDAEFAgiCA 625
Cdd:cd14894 638 RlpepPRVLsnakrhTPVLLNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLlVGLKTSNSSHFCRMLNESSQLG--WS 715
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 626 AEMNETAFG-MRSRKGMFRTVSQLHKEQLTKLMTTLRNTSPHFVRCIIPNHEKKSGKINSNLVLEQLRCNGVLEGIRICR 704
Cdd:cd14894 716 PNTNRSMLGsAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQMEICR 795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
857-1686 |
3.92e-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: 117.85 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 857 KERLLKMEHDfRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLqtRNQELEYIVNDMRDRLSEEEQQNEKNNDE 936
Cdd:TIGR02168 175 KETERKLERT-RENLDRLEDILNELERQLKSLERQAEKAERYKELKAEL--RELELALLVLRLEELREELEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 937 RRKQMETVRDLeeqleqeeqarQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEkrlleekVEGLTTQLLDHEERAKH 1016
Cdd:TIGR02168 252 EEELEELTAEL-----------QELEEKLEELRLEVSELEEEIEELQKELYALANE-------ISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1017 GVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESA 1096
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1097 NVTLMQKQMRDMQTTIDELREdmETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIE 1176
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLED--RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1177 QIQHTMEGKIEEQKAKFSRQ--VEELHDQIEQHKKQRSQLEKQQNQ--------ADQERADMAQEIALLQASRADIDKKR 1246
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLdsLERLQENLEGFSEGVKALLKNQSGlsgilgvlSELISVDEGYEAAIEAALGGRLQAVV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1247 KIHEAHLMEIQANLAESDEHKRTLIdqlersrdELDHLNRVREEEEHAFanmqrRLATAEGQIQELNEQIQEETRLKIAN 1326
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQNELGRVTFL--------PLDSIKGTEIQGNDRE-----ILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1327 INRARQL---EDEKNALLDEKEEAEGLR-AHLEKEIHAARqgaGEARRKAEESVNQQLEelRKKNLRDVEHLQKQLEESE 1402
Cdd:TIGR02168 619 SYLLGGVlvvDDLDNALELAKKLRPGYRiVTLDGDLVRPG---GVITGGSAKTNSSILE--RRREIEELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1403 VAKERILQSKKKIQQELEDssmELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEV 1482
Cdd:TIGR02168 694 AELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1483 DIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNlqiAEDARLRLEVTNQAL 1562
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERR---IAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1563 KSESDRAISNKDV---------EAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEY 1633
Cdd:TIGR02168 848 EELSEDIESLAAEieeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1767286957 1634 NKQLKK--------NQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREAN 1686
Cdd:TIGR02168 928 ELRLEGlevridnlQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVN 988
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1112-1689 |
1.96e-25 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 115.42 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1112 IDELREDMETERNARNKAEmTRREVVAQLEKVKGDV-LDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQK 1190
Cdd:COG1196 195 LGELERQLEPLERQAEKAE-RYRELKEELKELEAELlLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1191 AKFSR---QVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHK 1267
Cdd:COG1196 274 LELEElelELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1268 RTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEA 1347
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1348 EGLRAHLEKEIHAARQGAGEARRKAEesvnqQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELE 1427
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEE-----ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1428 NVRASHRDSEKRqkkfesqmaeeRVAVQKALLDRDAMSQELRDRETRVLSLLNEVdimkehlEESDRVRRSLQQELQDSI 1507
Cdd:COG1196 509 GVKAALLLAGLR-----------GLAGAVAVLIGVEAAYEAALEAALAAALQNIV-------VEDDEVAAAAIEYLKAAK 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1508 SNKDDFgknvheLEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKR-RGLLK 1586
Cdd:COG1196 571 AGRATF------LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRaVTLAG 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1587 QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLR 1666
Cdd:COG1196 645 RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
570 580
....*....|....*....|...
gi 1767286957 1667 EADRKFRAVEAEREQLREANEGL 1689
Cdd:COG1196 725 ALEEQLEAEREELLEELLEEEEL 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
970-1904 |
3.43e-25 |
|
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: 114.77 E-value: 3.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 970 QRLRNLEERLVELQDaydkLLKEkrlLEEKVEGLTTQlldheerAKHGVKAKgRLENQLHELEQDL--NRERQYKSELEQ 1047
Cdd:TIGR02168 179 RKLERTRENLDRLED----ILNE---LERQLKSLERQ-------AEKAERYK-ELKAELRELELALlvLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1048 hKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVtlmQKQMRDMQTTIDELREDMETERNARN 1127
Cdd:TIGR02168 244 -LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL---ANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1128 KAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVnATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQH 1207
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1208 KKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRkiHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRV 1287
Cdd:TIGR02168 399 NNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1288 REEEEHAFANMQRRLATaegqIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKeihAARQGAGE 1367
Cdd:TIGR02168 477 LDAAERELAQLQARLDS----LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA---ALGGRLQA 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1368 ARRKAEESVNQQLEELRKKNLRDVEHLqkqleesevakERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQM 1447
Cdd:TIGR02168 550 VVVENLNAAKKAIAFLKQNELGRVTFL-----------PLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1448 AE--ERVAVQKALLDRDAMSQELRdRETRVLSLlnevdimkehleESDRVRRSlqqelqDSISNKDDFGKNVhELEKakr 1525
Cdd:TIGR02168 619 SYllGGVLVVDDLDNALELAKKLR-PGYRIVTL------------DGDLVRPG------GVITGGSAKTNSS-ILER--- 675
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1526 slEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSEsdraISNKDVEAEEKRR---GLLKQIRDLENELENEKRGK 1602
Cdd:TIGR02168 676 --RREIEELEEKIEELEEKIAELEKALAELRKELEELEEE----LEQLRKELEELSRqisALRKDLARLEAEVEQLEERI 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1603 SGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQL 1682
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1683 REANEGLMQARKQlelendeleelrakgggiSSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSM 1762
Cdd:TIGR02168 830 ERRIAATERRLED------------------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1763 ERTLNQKTEAEKQSLERSNRDYKAKITELESgAQSRARAQMAALEAKVQYLEDQLNVEGQekTAANRAARRLEKRLNDTT 1842
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELRE-KLAQLELRLEGLEVRIDNLQERLSEEYS--LTLEEAEALENKIEDDEE 968
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1843 QQFEDEKRANEQAKELleksnlKNRNLrrqldEAEDEMSRERTKHRNVQREADDLLDANEQL 1904
Cdd:TIGR02168 969 EARRRLKRLENKIKEL------GPVNL-----AAIEEYEELKERYDFLTAQKEDLTEAKETL 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1093-1877 |
1.97e-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: 112.07 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1093 EESANVTLMQKQMRDMQTTIDELREDM--------ETERNARN---KAEMTRR--EVVAQLEKVKGDVLdkVDEATMLQD 1159
Cdd:TIGR02168 162 EEAAGISKYKERRKETERKLERTRENLdrledilnELERQLKSlerQAEKAERykELKAELRELELALL--VLRLEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1160 LMSRKDEEVNATKRAIEQIQhtmegkieeqkakfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASR 1239
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELT---------------AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1240 ADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEE 1319
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1320 TRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAeesVNQQLEELRKknlrDVEHLQKQLE 1399
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE---LQAELEELEE----ELEELQEELE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1400 ESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALL-----------------DRD 1462
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlselisvdegYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1463 AMSQELRDRETRVL-----SLLNEVDIMKEH-------LEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAE 1530
Cdd:TIGR02168 538 AIEAALGGRLQAVVvenlnAAKKAIAFLKQNelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1531 LNDM--RVQM-EELED--NLQIAEDARLRLeVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELEnekrgksga 1605
Cdd:TIGR02168 618 LSYLlgGVLVvDDLDNalELAKKLRPGYRI-VTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE--------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1606 vshrkKIENQIGELEQQLEVANRLKEEYNKQLKKNQQI-------IKEYQIECEEARQAKEDIAALLREADRKFRAVEAE 1678
Cdd:TIGR02168 688 -----ELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1679 REQLREANEGLmqarkqlelendeleelrakgggisSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITT 1758
Cdd:TIGR02168 763 IEELEERLEEA-------------------------EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1759 DLSMERTLNQKTEAEKQSLERSNRDYKAKITELeSGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRL 1838
Cdd:TIGR02168 818 EAANLRERLESLERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
810 820 830
....*....|....*....|....*....|....*....
gi 1767286957 1839 NDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAE 1877
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1695 |
1.72e-23 |
|
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: 109.00 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 844 DEIrAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDirgrLQTRNQELEYIVndmrdrL 923
Cdd:TIGR02169 160 DEI-AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQA----LLKEKREYEGYE------L 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 924 SEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKtnvDQRLRNLEERLVELQDaydkllKEKRLLEEKVEGL 1003
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEI---EQLLEELNKKIKDLGE------EEQLRVKEKIGEL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1004 TTQLldheERAKHGVKAKGRlenqlhELEQDLNRERQYKSELEqhkrKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEE 1083
Cdd:TIGR02169 300 EAEI----ASLERSIAEKER------ELEDAEERLAKLEAEID----KLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1084 LQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSR 1163
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1164 KDEEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASR---- 1239
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLS-KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIqgvh 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1240 ---ADIDKKRKIHEAHL-----MEIQANLAESDEHKRTLIDQLER---SRDELDHLNRVREEE----------------- 1291
Cdd:TIGR02169 525 gtvAQLGSVGERYATAIevaagNRLNNVVVEDDAVAKEAIELLKRrkaGRATFLPLNKMRDERrdlsilsedgvigfavd 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1292 --------EHAFANMQR------------------RLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKE 1345
Cdd:TIGR02169 605 lvefdpkyEPAFKYVFGdtlvvedieaarrlmgkyRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLE 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1346 EAEGLRAHLEKEIHAARQGAGEARRKAEESvNQQLEELRKKnlrdvehLQKQLEESEVAKERILQSKKKIQQeledSSME 1425
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDA-SRKIGEIEKE-------IEQLEQEEEKLKERLEELEEDLSS----LEQE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1426 LENVRASHRDSEKRQKKFESQMAEERVAVQKaLLDRDAMSQ-------------ELRDRETRVLSL---LNEVDIMKEHL 1489
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALND-LEARLSHSRipeiqaelskleeEVSRIEARLREIeqkLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1490 EESdrvRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELednlqiaedarlrlevtnqalksesdra 1569
Cdd:TIGR02169 832 EKE---IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL---------------------------- 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1570 isnkdveaEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQI------ 1643
Cdd:TIGR02169 881 --------ESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIpeeels 952
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1644 ---IKEYQIECEEARQAKEDIAALlreADRKFRAVEAEREQLREANEGLMQARKQ 1695
Cdd:TIGR02169 953 ledVQAELQRVEEEIRALEPVNML---AIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
961-1635 |
2.94e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 961 LLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQ 1040
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1041 YKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDME 1120
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1121 TERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQkakfsrqvEEL 1200
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE--------EAL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1201 HDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQAsradidkkrkiheahlMEIQANLAESDEHKRTLIDQLERSRDE 1280
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLE----------------AEADYEGFLEGVKAALLLAGLRGLAGA 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1281 LDHLNRVREEEEHAFANmqrRLATAEGQIQELNEQIQEETR--LKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEI 1358
Cdd:COG1196 526 VAVLIGVEAAYEAALEA---ALAAALQNIVVEDDEVAAAAIeyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1359 HAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELEnvrASHRDSEK 1438
Cdd:COG1196 603 LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL---AALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1439 RQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEEsdrVRRSLQQELQDSISNKDDFGKNVH 1518
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA---EREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1519 ELEKAKRSLEAELNDMRVQMEELED-NLQIAEDARlrlevtnqalksesdraisnkdvEAEEKRRGLLKQIRDLENElen 1597
Cdd:COG1196 757 PEPPDLEELERELERLEREIEALGPvNLLAIEEYE-----------------------ELEERYDFLSEQREDLEEA--- 810
|
650 660 670
....*....|....*....|....*....|....*...
gi 1767286957 1598 ekrgksgavshRKKIENQIGELEQqlEVANRLKEEYNK 1635
Cdd:COG1196 811 -----------RETLEEAIEEIDR--ETRERFLETFDA 835
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1198-1839 |
3.04e-23 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 108.10 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1198 EELHDQIEQHKKQRSQLEKQQNQAdQERADMAQEIALLQASRAdidkkrkihEAHLMEIQANLAESDEHKRTLIDQLERS 1277
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEKA-ERYRELKEELKELEAELL---------LLKLRELEAELEELEAELEELEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1278 RDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKE 1357
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1358 IHAARQGAGEARRKAEESvNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEdssmELENVRASHRDSE 1437
Cdd:COG1196 339 LEELEEELEEAEEELEEA-EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA----QLEELEEAEEALL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1438 KRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDsisnkddfgknv 1517
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE------------ 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1518 helekAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLkQIRDLENELEN 1597
Cdd:COG1196 482 -----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL-AAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1598 EKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLkknqqiikeyqieceEARQAKEDIAALLREADRKFRAVEA 1677
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARG---------------AIGAAVDLVASDLREADARYYVLGD 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1678 EREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQIT 1757
Cdd:COG1196 621 TLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1758 TDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEktaanRAARRLEKR 1837
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE-----RELERLERE 775
|
..
gi 1767286957 1838 LN 1839
Cdd:COG1196 776 IE 777
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
837-1541 |
2.27e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 837 LQVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIV 916
Cdd:TIGR02168 274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 917 NDMRDRLSEEE---QQNEKNNDERRKQMETVRDleeqleqeeqARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEK 993
Cdd:TIGR02168 354 ESLEAELEELEaelEELESRLEELEEQLETLRS----------KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 994 RLLEEKVEglTTQLLDHEERAkhgvkakGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEEL 1073
Cdd:TIGR02168 424 EELLKKLE--EAELKELQAEL-------EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1074 nnqlmkrdEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRRE--VVAQLEKVKGDV--LD 1149
Cdd:TIGR02168 495 --------ERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQavVVENLNAAKKAIafLK 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1150 KVDE--ATMLQdLMSRKDEEVNATKRAIEQIQHTMEG---KIEEQKAKFSRQVEEL------HDQIEQHKKQRSQLEKQQ 1218
Cdd:TIGR02168 567 QNELgrVTFLP-LDSIKGTEIQGNDREILKNIEGFLGvakDLVKFDPKLRKALSYLlggvlvVDDLDNALELAKKLRPGY 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1219 N----QADQERAD--MAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEE 1292
Cdd:TIGR02168 646 RivtlDGDLVRPGgvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1293 HAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIhAARQGAGEARRKA 1372
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREA 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1373 EESVNQQLEELRK---KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAE 1449
Cdd:TIGR02168 805 LDELRAELTLLNEeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1450 ERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQE---LQDSISNK-----DDFGKNVHELE 1521
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnLQERLSEEysltlEEAEALENKIE 964
|
730 740
....*....|....*....|
gi 1767286957 1522 KAKRSLEAELNDMRVQMEEL 1541
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1049-1727 |
8.28e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 103.48 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1049 KRKLLAELEDSKDHLAEKMGKVEELNNQL--MKRD-------EELQHQLTRYDeesanVTLMQKQMRDMQTTIDELREDM 1119
Cdd:COG1196 174 KEEAERKLEATEENLERLEDILGELERQLepLERQaekaeryRELKEELKELE-----AELLLLKLRELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1120 ETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNatkRAIEQIQHTMEGKIEEQkakfsRQVEE 1199
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA---RLEQDIARLEERRRELE-----ERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1200 LHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRD 1279
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1280 ELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIH 1359
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1360 AARQGagEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKR 1439
Cdd:COG1196 481 ELLEE--LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1440 QKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHE 1519
Cdd:COG1196 559 AAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1520 LEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDvEAEEKRRGLLKQIRDLENELENEK 1599
Cdd:COG1196 639 AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEEL-ELEEALLAEEEEERELAEAEEERL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1600 RGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQiecEEARQAKEDIAAL----LReADRKFRAV 1675
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE---RELERLEREIEALgpvnLL-AIEEYEEL 793
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1676 EAEREQLREANEGLMQARKQlelendeleelrakgggisseekrrLEAKIAQ 1727
Cdd:COG1196 794 EERYDFLSEQREDLEEARET-------------------------LEEAIEE 820
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
993-1638 |
2.83e-20 |
|
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: 98.65 E-value: 2.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 993 KRLLEE---KVEGLTTQLLD----HEERAKHGVKAKGRLENQLHELEQDLN-------RERQYKSELEQHKRKLLAELED 1058
Cdd:pfam15921 77 ERVLEEyshQVKDLQRRLNEsnelHEKQKFYLRQSVIDLQTKLQEMQMERDamadirrRESQSQEDLRNQLQNTVHELEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1059 SK----DHLAEKMGKVEELNNQLMKRD---EELQHQLTRYDEESANVTLMQKQMRDMQTtidelredmeteRNARNKAEM 1131
Cdd:pfam15921 157 AKclkeDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHF------------RSLGSAISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1132 TRREVVAQLEKVKGDVLDKVDEatmlqdLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQR 1211
Cdd:pfam15921 225 ILRELDTEISYLKGRIFPVEDQ------LEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1212 SQLEKQQNQADQERADMAQEIALLQAS----RADIDKKRKIHEAHLMEIQANLAESDEhkrtlidQLERSRDELDHLNrv 1287
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQLSDLESTvsqlRSELREAKRMYEDKIEELEKQLVLANS-------ELTEARTERDQFS-- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1288 rEEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLeKEIHAARQGAGE 1367
Cdd:pfam15921 370 -QESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1368 ARRKAEESVNQQLEElrkknlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQM 1447
Cdd:pfam15921 448 RQMAAIQGKNESLEK--------VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1448 AEERVAVQKALLDRdamsQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSL 1527
Cdd:pfam15921 520 TKLRSRVDLKLQEL----QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQL 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1528 EAELNDMRVQMEELEdNLQIAEDARLR-LEVTNQALKSE--------SDRAISNKDVEAEekRRGLLKQIRDLENEL--- 1595
Cdd:pfam15921 596 EKEINDRRLELQEFK-ILKDKKDAKIReLEARVSDLELEkvklvnagSERLRAVKDIKQE--RDQLLNEVKTSRNELnsl 672
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 1767286957 1596 -ENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLK 1638
Cdd:pfam15921 673 sEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLK 716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
936-1687 |
2.18e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.52 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 936 ERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQ---RLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLdhee 1012
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERldlIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELL---- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1013 rakhgvKAKGRLENQLHELEQDLnrerqykSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYD 1092
Cdd:TIGR02169 230 ------KEKEALERQKEAIERQL-------ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKI 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1093 EEsanvtlMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATK 1172
Cdd:TIGR02169 297 GE------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1173 RAIEQIQHTMEGKIEEQKaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAH 1252
Cdd:TIGR02169 371 AELEEVDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1253 LMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVRE--EEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIanINRA 1330
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSklQRELAEAEAQARASEERVRGGRAVEEVLKASIQGV--HGTV 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1331 RQLEDEKNALLDEKEEAEGLRAH---LEKEIHAARQGAGEARRKAEESVNQQLEELRKKnLRDVEHLQKQ---------- 1397
Cdd:TIGR02169 528 AQLGSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDE-RRDLSILSEDgvigfavdlv 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1398 ------------------LEESEVAKERILQSKKKIQQE---LEDS-SMELENVRASHRDSEKRQKKFESQMAEERVAVQ 1455
Cdd:TIGR02169 607 efdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEgelFEKSgAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1456 KALLDRdaMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMR 1535
Cdd:TIGR02169 687 KRELSS--LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1536 VQMEELEDNLQIAEDARLRLEvtnQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQ 1615
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1616 IGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANE 1687
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE 913
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
817-1408 |
5.16e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 5.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 817 AYLKLRNWQWWRLftkvkpllQVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSA 896
Cdd:COG1196 227 AELLLLKLRELEA--------ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 897 ELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLE 976
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 977 ERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAEL 1056
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1057 EDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYdeesanvtLMQKQMRdmqttiDELREDMETERNARNKAEMTRREV 1136
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARL--------LLLLEAE------ADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1137 VAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEqiqhtmegkiEEQKAKFSRQVEELHDQIEQHKKQrsqlek 1216
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE----------YLKAAKAGRATFLPLDKIRARAAL------ 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1217 qqnQADQERADMAQEIALLQASRADIDKKRKIHEAHLME---IQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEH 1293
Cdd:COG1196 589 ---AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1294 AFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAgEARRKAE 1373
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL-LEELLEE 744
|
570 580 590
....*....|....*....|....*....|....*
gi 1767286957 1374 ESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERI 1408
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
841-1614 |
1.08e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 93.67 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 841 RTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMR 920
Cdd:PTZ00121 1188 RKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 921 DRLSEEEQqnEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKrlleekv 1000
Cdd:PTZ00121 1268 RQAAIKAE--EARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKA------- 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1001 eglttqlldhEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKllaelEDSKDHLAEKMGKVEELNNQlMKR 1080
Cdd:PTZ00121 1339 ----------EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK-----ADAAKKKAEEKKKADEAKKK-AEE 1402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1081 DEELQHQLTRYDEESANVTLMQKQMRDMQTTiDELREDMETERNA---RNKAEMTRREVVAQL---EKVKGDVLDKVDEA 1154
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKA-DEAKKKAEEAKKAdeaKKKAEEAKKAEEAKKkaeEAKKADEAKKKAEE 1481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1155 TMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERAdmAQEIAL 1234
Cdd:PTZ00121 1482 AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKK--AEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1235 LQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNE 1314
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1315 QIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESvNQQLEELRKKNLRDVEHL 1394
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKA 1718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1395 QKQLEESEVAKERILQSKKKIQQE---LEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDR 1471
Cdd:PTZ00121 1719 EELKKAEEENKIKAEEAKKEAEEDkkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1472 ETRvlSLLNEVDIMKEHLEESDRVRRSlQQELQDSISNKDDFGKNVhELEKAKRSLEAELNDMRVQMEELEDNLQIAEDA 1551
Cdd:PTZ00121 1799 KIK--DIFDNFANIIEGGKEGNLVIND-SKEMEDSAIKEVADSKNM-QLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1767286957 1552 RLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRD-LENELENEKRGKSGAVSHRKKIEN 1614
Cdd:PTZ00121 1875 DLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDiIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
977-1788 |
2.41e-18 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 92.51 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 977 ERLVELQDAyDKLLKEKRLLEEKVEGlttqllDHEERA--KHGVKAKGRLENQLHELEQDlNRERQYKSELEQHKRKLLA 1054
Cdd:PTZ00121 1030 EELTEYGNN-DDVLKEKDIIDEDIDG------NHEGKAeaKAHVGQDEGLKPSYKDFDFD-AKEDNRADEATEEAFGKAE 1101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1055 ELEDSKDHLAEKMGKVEELnnqlMKRDEELQH-QLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTR 1133
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEA----KKKAEDARKaEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKK 1177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1134 REVVAQLEKV-KGDVLDKVDEATMLQDlmSRKDEEVnatkRAIEQIQHTMEgkieEQKAKFSRQVEELHDQIEQHKKQRS 1212
Cdd:PTZ00121 1178 AEAARKAEEVrKAEELRKAEDARKAEA--ARKAEEE----RKAEEARKAED----AKKAEAVKKAEEAKKDAEEAKKAEE 1247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1213 QLEKQQNQADQErADMAQEIALLQASRADidKKRKIHEAHLMEiqaNLAESDEHKRTlidQLERSRDELdhlnRVREEEE 1292
Cdd:PTZ00121 1248 ERNNEEIRKFEE-ARMAHFARRQAAIKAE--EARKADELKKAE---EKKKADEAKKA---EEKKKADEA----KKKAEEA 1314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1293 HAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAgEARRKA 1372
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA-EEKKKA 1393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1373 EEsVNQQLEELRKKnlrdVEHLQKQLEESEVAKEriLQSKKKIQQELEDSSMELENVRAShrdSEKRQKKFESQMAEErv 1452
Cdd:PTZ00121 1394 DE-AKKKAEEDKKK----ADELKKAAAAKKKADE--AKKKAEEKKKADEAKKKAEEAKKA---DEAKKKAEEAKKAEE-- 1461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1453 AVQKALLDRDAMSQELRDRETRvlsllnEVDIMKEHLEE----SDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLE 1528
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK------KADEAKKKAEEakkkADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1529 AElNDMRVQMEELEDNLQIAEDARLRLEV--TNQALKSESDRAISNKDVE----AEEKRRGLLKQIRDLENELENEKRGK 1602
Cdd:PTZ00121 1536 AD-EAKKAEEKKKADELKKAEELKKAEEKkkAEEAKKAEEDKNMALRKAEeakkAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1603 sgAVSHRKKIEnQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYqiecEEARQAKEDIAALLREADRKFRAVEAEREQL 1682
Cdd:PTZ00121 1615 --AEEAKIKAE-ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE----EENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1683 REANEGLM----QARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNcELAIDKQRKAQVQLEQITT 1758
Cdd:PTZ00121 1688 KKAAEALKkeaeEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE-EAKKDEEEKKKIAHLKKEE 1766
|
810 820 830
....*....|....*....|....*....|
gi 1767286957 1759 DLSMERTLNQKTEAEKQSLERSNRDYKAKI 1788
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1273-1912 |
3.09e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 91.92 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1273 QLERSRDELDHLNRVREEeehafanMQRRLATAEGQ------IQELNEQIQEetRLKIANINRARQLEDEKNALLDEKEE 1346
Cdd:COG1196 180 KLEATEENLERLEDILGE-------LERQLEPLERQaekaerYRELKEELKE--LEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1347 AEGLRAHLEKEIhaarqgagEARRKAEESVNQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1426
Cdd:COG1196 251 LEAELEELEAEL--------AELEAELEELRLELEELELE----LEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1427 ENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEvdimkehLEESDRVRRSLQQELQDS 1506
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-------LAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1507 ISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISnKDVEAEEKRRGLLK 1586
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1587 QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEynkqlkknqqiikeyqieceEARQAKEDIAALLR 1666
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLL--------------------AGLRGLAGAVAVLI 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1667 EADRKFRAVEAEREQLREANEGL--MQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAID 1744
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNIVVedDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLRE 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1745 KQRKAQVQLEQIttdlsMERTLNQKTEAEKQSLERSnRDYKAKITELESGAQSRARAQMAALEAKvqyLEDQLNVEGQEK 1824
Cdd:COG1196 611 ADARYYVLGDTL-----LGRTLVAARLEAALRRAVT-LAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAEL 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1825 TAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDAN--- 1901
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppd 761
|
650
....*....|..
gi 1767286957 1902 -EQLTRELMNLR 1912
Cdd:COG1196 762 lEELERELERLE 773
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1043-1868 |
2.82e-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: 88.59 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1043 SELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQL-----------TRYDEESANVTLMQKQMRDMQTT 1111
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAEryqallkekreYEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1112 IDELREDME------TERNAR-NKAEMTRREVVAQLEKVKGDvldkvdEATMLQDLMSRKDEEVNATKRAIEQIQHTME- 1183
Cdd:TIGR02169 246 LASLEEELEklteeiSELEKRlEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLERSIAEKERELEd 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1184 -----GKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEkqqnqadQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQA 1258
Cdd:TIGR02169 320 aeerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLT-------EEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1259 NLAEsdehkrtLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIqEETRLKIANINR-----ARQL 1333
Cdd:TIGR02169 393 KLEK-------LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK-EDKALEIKKQEWkleqlAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1334 EDEKNALLDEKEEAEglraHLEKEIHAARQ--GAGEARRKA---EESVNQQLEELRKKNLRDVEHLQKQL---------- 1398
Cdd:TIGR02169 465 SKYEQELYDLKEEYD----RVEKELSKLQRelAEAEAQARAseeRVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryata 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1399 --------------EESEVAKERILQSKKKIQQELedSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALldRDAM 1464
Cdd:TIGR02169 541 ievaagnrlnnvvvEDDAVAKEAIELLKRRKAGRA--TFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKY--EPAF 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1465 SQELRDRetrvlSLLNEVDIMKEHLEESDRVrrSLQQELQD---SISNKDDFGKNvheLEKAKRSLEAELNDMRVQMEEL 1541
Cdd:TIGR02169 617 KYVFGDT-----LVVEDIEAARRLMGKYRMV--TLEGELFEksgAMTGGSRAPRG---GILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1542 EDNLQIAEDARLRLEVTNQALKSESDRA------ISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQ 1615
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDAsrkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1616 IGELEqqlEVANRLKEEYNK-QLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARK 1694
Cdd:TIGR02169 767 IEELE---EDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRI 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1695 ----QLELENDELEELRAKGGGISSEEKrRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKT 1770
Cdd:TIGR02169 844 dlkeQIKSIEKEIENLNGKKEELEEELE-ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1771 EAEKQSLERSNRDYKAKITELESgaQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKR 1850
Cdd:TIGR02169 923 KAKLEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
890
....*....|....*...
gi 1767286957 1851 ANEQAKELLEKSNLKNRN 1868
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKRE 1018
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1007-1633 |
6.09e-17 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 87.40 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1007 LLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRklLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQH 1086
Cdd:PRK02224 164 LEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDLHER--LNGLESELAELDEEIERYEEQREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1087 QLTRYDEEsanvtlmQKQMRDMQTTIDELREDM---ETERNARNKAEMTRREVVAQLEKVKGDVLDKVDeatmlqdlMSR 1163
Cdd:PRK02224 242 VLEEHEER-------REELETLEAEIEDLRETIaetEREREELAEEVRDLRERLEELEEERDDLLAEAG--------LDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1164 KDEEVnatkraieqiqhtmegkIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADID 1243
Cdd:PRK02224 307 ADAEA-----------------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1244 KKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLK 1323
Cdd:PRK02224 370 SELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1324 IANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIhaarqgagEARRKAEESVNQQLEELrkknlrdvehlqKQLEESEV 1403
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVETIEEDRERVEELEAEL--------EDLEEEVEEVEERLERA------------EDLVEAED 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1404 AKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLlnevd 1483
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL----- 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1484 imKEHLEESDRVRRSLQ--QELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIaEDARLRLEVTNQA 1561
Cdd:PRK02224 585 --KERIESLERIRTLLAaiADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARI-EEAREDKERAEEY 661
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1562 LKSesdraISNKDVEAEEKRRGLLKQIRDLENELENEKRGKsgavSHRKKIENQIGELEQQLEVANRLKEEY 1633
Cdd:PRK02224 662 LEQ-----VEEKLDELREERDDLQAEIGAVENELEELEELR----ERREALENRVEALEALYDEAEELESMY 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
959-1528 |
7.87e-17 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 87.04 E-value: 7.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 959 QKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKakgrLENQLHELEQDLNRE 1038
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1039 RQYKSELEQHKRKLLAELEDskdhLAEKMGKVEELnNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRED 1118
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEE----LEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1119 METERNARNKAEMTRREVVAQLEKVKGDVLdKVDEATMLQDLMSR-----KDEEVNATKRAIEQIQHTMEgKIEEQKAKF 1193
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELERlkkrlTGLTPEKLEKELEELEKAKE-EIEEEISKI 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1194 SRQVEELHDQIEQHKKQRSQLEKQQNQ--------ADQERADMAQ----EIALLQASRADIDKKRKIHEAHLMEIQANLA 1261
Cdd:PRK03918 411 TARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEeytaELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1262 ESDE--HKRTLIDQLERSRDELDHLNRVR-EEEEHAFANMQRRLATAEGQIQELNEQiqeetrlkianINRARQLEDEKN 1338
Cdd:PRK03918 491 KESEliKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLKGEIKSLKKE-----------LEKLEELKKKLA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1339 ALLDEKEEAEGLRAHLEKEIhaarqgaGEARRKAEESVNQQLEELRKKNLRDVEhlqkqLEESEVAKERILQSKKKIQQE 1418
Cdd:PRK03918 560 ELEKKLDELEEELAELLKEL-------EELGFESVEELEERLKELEPFYNEYLE-----LKDAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1419 LEDSSMELENVRASHRDSEKRQKKFESQMAEErvavqkalldrdamsqELRDRETRVLSLLNEVDIMKEHLEESDRVRRS 1498
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEE----------------EYEELREEYLELSRELAGLRAELEELEKRREE 691
|
570 580 590
....*....|....*....|....*....|
gi 1767286957 1499 LQQELQDSISNKDDFGKNVHELEKAKRSLE 1528
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1273-1912 |
9.42e-17 |
|
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: 87.03 E-value: 9.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1273 QLERSRDELDHLNRVREEEEHAFANMQRRLATAEgQIQELNEQIqEETRLKIAnINRARQLEDEKNALLDEKEEAEGLRA 1352
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAEL-RELELALL-VLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1353 HLEKEIHAArqgagearrkaeesvNQQLEELRKKNL---RDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELEnv 1429
Cdd:TIGR02168 257 ELTAELQEL---------------EEKLEELRLEVSeleEEIEELQKELYALANEISRLEQQKQILRERLANLERQLE-- 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1430 RASHRDSEKRQKKFESQMAEERVAVQKALLdrdamsqelrdrETRVLSLLNEVDIMKEHLEESDRVRRSLQQELqdsisn 1509
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEEL------------KEELESLEAELEELEAELEELESRLEELEEQL------ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1510 kDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNL------------------------------QIAEDARLRLEVTN 1559
Cdd:TIGR02168 382 -ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieellkkleeaelkelqaeleeleEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1560 QALKSESDR--AISNKDVEAEEK---RRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYN 1634
Cdd:TIGR02168 461 EALEELREEleEAEQALDAAERElaqLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1635 KQLKKNQQiikeyQIECEEARQAKEDIAALLREA-------------DRKFRAVEAER---------------------- 1679
Cdd:TIGR02168 541 AALGGRLQ-----AVVVENLNAAKKAIAFLKQNElgrvtflpldsikGTEIQGNDREIlkniegflgvakdlvkfdpklr 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1680 -------------EQLREANEglMQARKQLELENDELEELRAKGGGISS---------------------EEKRRLEAKI 1725
Cdd:TIGR02168 616 kalsyllggvlvvDDLDNALE--LAKKLRPGYRIVTLDGDLVRPGGVITggsaktnssilerrreieeleEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1726 AQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELE------------- 1792
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEaeieeleerleea 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1793 SGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQ 1872
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1767286957 1873 LDEAEDEMSRERTKHRNVQREADDLLDANEQLTRELMNLR 1912
Cdd:TIGR02168 854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
881-1224 |
5.63e-15 |
|
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: 81.26 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 881 RAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIV---NDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQA 957
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRkelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 958 RQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNR 1037
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1038 ERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRE 1117
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1118 DMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRK-DEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQ 1196
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEaRRRLKRLENKIKELGPVNLAAIEEYEELKERY 1002
|
330 340
....*....|....*....|....*...
gi 1767286957 1197 vEELHDQIEQHKKQRSQLEKQQNQADQE 1224
Cdd:TIGR02168 1003 -DFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1542 |
2.03e-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: 79.34 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQviVERAVIQEQLQQES--ENSAELDDIRGRLQTRNQELEYI 915
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE--LEREIEEERKRRDKltEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 916 VNDMRDRLSEEEQQNEKNNDERRkqmETVRDLEEQLEQEEQARQKLLldktNVDQRLRNLEERLVELQDAYDKLLKEKRL 995
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREIN---ELKRELDRLQEELQRLSEELA----DLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 996 LEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNR---ERQYKSELEQHKRKLLAELEDSKD---HLAEKMGK 1069
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaeaQARASEERVRGGRAVEEVLKASIQgvhGTVAQLGS 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1070 VEE-------------LNNQLMKRDEELQH--QLTRYDEESANVTLMQKQMRDMQTTIDELRED---------METERNA 1125
Cdd:TIGR02169 533 VGEryataievaagnrLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlVEFDPKY 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1126 RNKAEMTRRE--VVAQLEKVKgDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQkaKFSRQVEELHDQ 1203
Cdd:TIGR02169 613 EPAFKYVFGDtlVVEDIEAAR-RLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQ--RLRERLEGLKRE 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1204 IEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDH 1283
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1284 LNRVREEEEHAFANMQRRLatAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAArq 1363
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARL--SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL-- 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1364 gagEARRKAEEsvnQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKF 1443
Cdd:TIGR02169 846 ---KEQIKSIE---KEIENLNGK----KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1444 ESQMAEERVAVQkALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKA 1523
Cdd:TIGR02169 916 RKRLSELKAKLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEK 994
|
730
....*....|....*....
gi 1767286957 1524 KRSLEAELNDMRVQMEELE 1542
Cdd:TIGR02169 995 RAKLEEERKAILERIEEYE 1013
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1695 |
1.35e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1106 RDMQTTIDELREDMETERNARNKAEMTRR--EVVAQLEKVKGDVLDKVDEATMLQDLMSRkdeevnatkRAIEQIQhtme 1183
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREqiELLEPIRELAERYAAARERLAELEYLRAA---------LRLWFAQ---- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1184 gkieeqkakfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRkiheahLMEIQANLAES 1263
Cdd:COG4913 288 -----------RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR------LEQLEREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1264 DEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRlkiANINRARQLEDEKNALLDE 1343
Cdd:COG4913 351 ERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA---EAEAALRDLRRELRELEAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 KEEAEGLRAHLEKEIHAARqgagearrkaeESVNQQLeELRKKNLRDV-EHLQKQLEES--EVAKERILQSKKK---IQQ 1417
Cdd:COG4913 428 IASLERRKSNIPARLLALR-----------DALAEAL-GLDEAELPFVgELIEVRPEEErwRGAIERVLGGFALtllVPP 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1418 ELEDSSME-LENVRASHR-DSEK---RQKKFESQMAEERVAVQKALLDRDAMSQELRDRetrvlsLLNEVDIMK-EHLEE 1491
Cdd:COG4913 496 EHYAAALRwVNRLHLRGRlVYERvrtGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEAE------LGRRFDYVCvDSPEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1492 SDRVRRSLQQELQdsISN------KDD---------FGKN----VHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDAR 1552
Cdd:COG4913 570 LRRHPRAITRAGQ--VKGngtrheKDDrrrirsryvLGFDnrakLAALEAELAELEEELAEAEERLEALEAELDALQERR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1553 LRLEVTNQALKSESD-RAISNKDVEAEEKRRGLLK---QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANR 1628
Cdd:COG4913 648 EALQRLAEYSWDEIDvASAEREIAELEAELERLDAssdDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1629 LKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRA-VEAEREQLREANEGLMQARKQ 1695
Cdd:COG4913 728 ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEErIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1262-1841 |
1.41e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.62 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1262 ESDEHKR--TLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELN--EQIQEETRLKIAninrarQLEDEK 1337
Cdd:PRK02224 201 EKDLHERlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELEtlEAEIEDLRETIA------ETERER 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1338 NALLDEKEEAEGLRAHLEKEIHAARQGAGeARRKAEESVNQQLEEL--RKKNLRDV-----EHLQKQLEESEVAKERILQ 1410
Cdd:PRK02224 275 EELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELedRDEELRDRleecrVAAQAHNEEAESLREDADD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1411 SK---KKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAM---SQELRDRETRVLSLLNEVDI 1484
Cdd:PRK02224 354 LEeraEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAedfLEELREERDELREREAELEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1485 MKEHLEESDRVRRSLQ---------QELQDSisnkdDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARlrl 1555
Cdd:PRK02224 434 TLRTARERVEEAEALLeagkcpecgQPVEGS-----PHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLV--- 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1556 evtnqalksESDRAISNKdveaEEKRRGLLKQIRDLENELEnEKRGKsgAVSHRKKIENQIGELEQQLEVANRLKEEYNK 1635
Cdd:PRK02224 506 ---------EAEDRIERL----EERREDLEELIAERRETIE-EKRER--AEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1636 QLKKNQQIIKEYQiECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEndeleelrakgggisS 1715
Cdd:PRK02224 570 AREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEK---------------R 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1716 EEKRRLEAKIaqleeeleeEQSNCELAIDKQRKAQVQLEQITTDLsmertlnQKTEAEKQSLERSNRDYKAKITELESga 1795
Cdd:PRK02224 634 ERKRELEAEF---------DEARIEEAREDKERAEEYLEQVEEKL-------DELREERDDLQAEIGAVENELEELEE-- 695
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1767286957 1796 qsrARAQMAALEAKVQYLED-QLNVEGQEKTAA-------NRAARRLEKRLNDT 1841
Cdd:PRK02224 696 ---LRERREALENRVEALEAlYDEAEELESMYGdlraelrQRNVETLERMLNET 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1240-1913 |
1.46e-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: 76.65 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1240 ADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVRE-----------EEEHAFANMQRRLATAEGQ 1308
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAllkekreyegyELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1309 IQELNEQIQEETRL---KIANINRARQLEDEKNALLDEKEEAEGLR-----AHLEKEIHAARQGAGEARRKAEESVNQ-- 1378
Cdd:TIGR02169 246 LASLEEELEKLTEEiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRvkekiGELEAEIASLERSIAEKERELEDAEERla 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1379 QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAL 1458
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1459 LDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSisnkddfGKNVHELEKAKRSLEAELNDMRVQM 1538
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-------EWKLEQLAADLSKYEQELYDLKEEY 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1539 EELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVeAEEKRRGLLKQIRDLenelenekrGKSGAvSHRKKIENQIGE 1618
Cdd:TIGR02169 479 DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEV-LKASIQGVHGTVAQL---------GSVGE-RYATAIEVAAGN 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1619 LEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLR-----------EADRKFRAV------------ 1675
Cdd:TIGR02169 548 RLNNVVVEDDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdlvEFDPKYEPAfkyvfgdtlvve 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1676 --EAEREQL-----------------------REANEGLMQARKQleleNDELEELRAKGGGISSEEKrRLEAKIAQLEE 1730
Cdd:TIGR02169 628 diEAARRLMgkyrmvtlegelfeksgamtggsRAPRGGILFSRSE----PAELQRLRERLEGLKRELS-SLQSELRRIEN 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1731 ELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRaRAQMAALEAKV 1810
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL-EEDLHKLEEAL 781
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1811 QYLEDQLNVE-----GQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERT 1885
Cdd:TIGR02169 782 NDLEARLSHSripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
730 740
....*....|....*....|....*...
gi 1767286957 1886 KHRNVQREADDLLDANEQLTRELMNLRG 1913
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLKK 889
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
838-1563 |
1.75e-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: 76.26 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEiRAKDDELRATKERLLKME-----HDFRENEKKLDQVIVERAVIQEQLQQESEnsaELDDIRGRLQTRNQEL 912
Cdd:TIGR02169 199 QLERLRRE-REKAERYQALLKEKREYEgyellKEKEALERQKEAIERQLASLEEELEKLTE---EISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 913 EYIvNDMRDRLSEEEQ-----QNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYD 987
Cdd:TIGR02169 275 EEL-NKKIKDLGEEEQlrvkeKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 988 KLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKM 1067
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1068 GKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREV----------- 1136
Cdd:TIGR02169 434 AKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeervrggrave 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1137 -------------VAQLEKVKGD-----------------VLDKVDEATMLQDLMSRK-----------------DEEVN 1169
Cdd:TIGR02169 514 evlkasiqgvhgtVAQLGSVGERyataievaagnrlnnvvVEDDAVAKEAIELLKRRKagratflplnkmrderrDLSIL 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1170 ATKRAI----------EQIQH----------------------------TMEGKIEEQ-----------------KAKFS 1194
Cdd:TIGR02169 594 SEDGVIgfavdlvefdPKYEPafkyvfgdtlvvedieaarrlmgkyrmvTLEGELFEKsgamtggsraprggilfSRSEP 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1195 RQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQL 1274
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1275 ERSRDELDHLNRVREEEEHAFANMQRRLATAEgqiQELNEQiqeetrlkianinRARQLEDEKNALLDEKEEAEGLRAHL 1354
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLE---ARLSHS-------------RIPEIQAELSKLEEEVSRIEARLREI 817
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1355 EKEIhaarqgagearrKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHR 1434
Cdd:TIGR02169 818 EQKL------------NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1435 DSEKRQKKFESQMAEERVAVQKALLDRDamsqelrDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISnKDDFG 1514
Cdd:TIGR02169 886 DLKKERDELEAQLRELERKIEELEAQIE-------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQ 957
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1767286957 1515 KNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALK 1563
Cdd:TIGR02169 958 AELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
845-1674 |
4.91e-13 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 75.01 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 845 EIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLS 924
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 925 EEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLlldKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLT 1004
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE---EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1005 TQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEqhKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEEL 1084
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE--ESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1085 QHQLTRYDEESANVTLMQKQMRDMQttiDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRK 1164
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEE---RSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1165 DEEVNATKRAIEQIQHtmegkieeqkakfSRQVEELHDQIEQHKKQRSQLEKQQNQADQERaDMAQEIALLQASRADIDK 1244
Cdd:pfam02463 550 IVEVSATADEVEERQK-------------LVRALTELPLGARKLRLLIPKLKLPLKSIAVL-EIDPILNLAQLDKATLEA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1245 KRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEldhlnrvrEEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKI 1324
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKG--------VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAES 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1325 ANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIhaarqgAGEARRKAEESVNQQLEELRKKNLrdvehLQKQLEESEVA 1404
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEE------LLADRVQEAQDKINEELKLLKQKI-----DEEEEEEEKSR 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1405 KERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDI 1484
Cdd:pfam02463 757 LKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELE 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1485 MKEHLEESDRVRRSLQQELQdsISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKS 1564
Cdd:pfam02463 837 ELALELKEEQKLEKLAEEEL--ERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEE 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1565 ESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQII 1644
Cdd:pfam02463 915 KENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDE 994
|
810 820 830
....*....|....*....|....*....|
gi 1767286957 1645 KEYQIECEEARQAKEDIAALLREADRKFRA 1674
Cdd:pfam02463 995 LEKERLEEEKKKLIRAIIEETCQRLKEFLE 1024
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
961-1602 |
5.26e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 5.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 961 LLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLE--EKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRE 1038
Cdd:COG4913 216 YMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1039 RQykSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdeeLQHQLTRydeesanvtlmqkqmrdmqttIDELRED 1118
Cdd:COG4913 296 EL--EELRAELARLEAELERLEARLDALREELDELEAQI------RGNGGDR---------------------LEQLERE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1119 METERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKakfsRQVE 1198
Cdd:COG4913 347 IERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR----RELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1199 ELHDQIEQHKKQRSQLEKQQNQAdqeRADMAQEIAL-------------------------------------------L 1235
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLAL---RDALAEALGLdeaelpfvgelievrpeeerwrgaiervlggfaltllvppehyA 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1236 QASRA--DIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLE----RSRDELDHL-----NRVREEEEHAFANMQRRLaT 1304
Cdd:COG4913 500 AALRWvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDfkphPFRAWLEAElgrrfDYVCVDSPEELRRHPRAI-T 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1305 AEGQ-----------------------------IQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLE 1355
Cdd:COG4913 579 RAGQvkgngtrhekddrrrirsryvlgfdnrakLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1356 KEI-----HAARQGAGEARRKAEESvNQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVR 1430
Cdd:COG4913 659 DEIdvasaEREIAELEAELERLDAS-SDDLAALEEQ----LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1431 ASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNE-----VDIMKEH----------------- 1488
Cdd:COG4913 734 DRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRaeeelERAMRAFnrewpaetadldadles 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1489 LEESDRVRRSLQQElqDSISNKDDFGKNVHELEKAKRS-----LEAELNDMRVQMEELED---NLQIAEDARLRLEVT-- 1558
Cdd:COG4913 814 LPEYLALLDRLEED--GLPEYEERFKELLNENSIEFVAdllskLRRAIREIKERIDPLNDslkRIPFGPGRYLRLEARpr 891
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1559 --------NQALKSESDRAISNKDVEAEEK---RRGLLKQIRDLENELENEKRGK 1602
Cdd:COG4913 892 pdpevrefRQELRAVTSGASLFDEELSEARfaaLKRLIERLRSEEEESDRRWRAR 946
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1289-1836 |
5.86e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1289 EEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKianiNRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEA 1368
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIE----ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1369 RRKAEESVNQQLE-ELRKKNLRDVEHLQKQLEES-EVAKERILQSKKKIQ-----QELEDSSMELENVRASHRDSEKRQK 1441
Cdd:PRK03918 234 EELKEEIEELEKElESLEGSKRKLEEKIRELEERiEELKKEIEELEEKVKelkelKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1442 KFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQ----ELQDSISNKDDFGKNV 1517
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlKKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1518 HELEKAK-------RSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALkSESDRA------------ISNKDVEAE 1578
Cdd:PRK03918 394 EELEKAKeeieeeiSKITARIGELKKEIKELKKAIEELKKAKGKCPVCGREL-TEEHRKelleeytaelkrIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1579 EKRRGLLKQIRDLENELENEKRgksgaVSHRKKIENQIGELEQQLEVANrlkeeynkqLKKNQQIIKEYQIECEEARQAK 1658
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESE-----LIKLKELAEQLKELEEKLKKYN---------LEELEKKAEEYEKLKEKLIKLK 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1659 EDIAALLREADRKfravEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEaKIAQLEEELEEEQSN 1738
Cdd:PRK03918 539 GEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELE-PFYNEYLELKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1739 CELAIDKQRKAQVQLEQITTDLS-----MERTLNQKTEAEKQSLERSNRDYKAKITELESgAQSRARAQMAALEAKVQYL 1813
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAetekrLEELRKELEELEKKYSEEEYEELREEYLELSR-ELAGLRAELEELEKRREEI 692
|
570 580
....*....|....*....|...
gi 1767286957 1814 EDQLNVEGQEKTAANRAARRLEK 1836
Cdd:PRK03918 693 KKTLEKLKEELEEREKAKKELEK 715
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1024-1866 |
7.49e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 74.23 E-value: 7.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1024 LENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDhLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQK 1103
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRI-LAAKKSETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1104 QMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLdKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTme 1183
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLL-TLCTPCMPDTYHERKQVLEKELKHLREALQQT-- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1184 gkieeqkakfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIheAHLMEIQANLAES 1263
Cdd:TIGR00618 239 -----------QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKA--APLAAHIKAVTQI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1264 DEhkrtlidQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANinrarqleDEKNALLDE 1343
Cdd:TIGR00618 306 EQ-------QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAH--------EVATSIREI 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 KEEAEGLRAHLEKEihaarqgagearRKAEESVNQQLEELRKKNLRDVEHLQKQleESEVAKERILQSKK---KIQQELE 1420
Cdd:TIGR00618 371 SCQQHTLTQHIHTL------------QQQKTTLTQKLQSLCKELDILQREQATI--DTRTSAFRDLQGQLahaKKQQELQ 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1421 DSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALL-DRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDR---VR 1496
Cdd:TIGR00618 437 QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIhpnPA 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1497 RSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDraisnkdve 1576
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP--------- 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1577 aeeKRRGLLKQIRDLENELENEKRGKSGAV-SHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQ-QIIKEYQIECEEA 1654
Cdd:TIGR00618 588 ---NLQNITVRLQDLTEKLSEAEDMLACEQhALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAlQLTLTQERVREHA 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1655 RQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRlEAKIAQLEEELEE 1734
Cdd:TIGR00618 665 LSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL-GSDLAAREDALNQ 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1735 EQSNCELAIDKQRKAQVQL-EQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITEL---ESGAQSRARAQMAALEAKV 1810
Cdd:TIGR00618 744 SLKELMHQARTVLKARTEAhFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLktlEAEIGQEIPSDEDILNLQC 823
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1767286957 1811 QYL---EDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKN 1866
Cdd:TIGR00618 824 ETLvqeEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
958-1659 |
8.37e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 73.85 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 958 RQKLLLDKTNVDQRlrnleERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrLENQLHELEQDLNR 1037
Cdd:TIGR00618 165 KKELLMNLFPLDQY-----TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQV--LEKELKHLREALQQ 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1038 ERQYKSELEQhKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDE-----ELQHQLTRYDEESANVTLMQKQMRDMQTTI 1112
Cdd:TIGR00618 238 TQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEEtqeriNRARKAAPLAAHIKAVTQIEQQAQRIHTEL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1113 DELREDMETERNARNKAEMTRREVVAQ------LEKVKGDVLDKVDEATMLQDLMSRKDEEVNATkRAIEQIQHTMEGKI 1186
Cdd:TIGR00618 317 QSKMRSRAKLLMKRAAHVKQQSSIEEQrrllqtLHSQEIHIRDAHEVATSIREISCQQHTLTQHI-HTLQQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1187 EEQKAKFSRQVEELHDQIEQHKKQRSqLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDE- 1265
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQq 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1266 --HKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDE 1343
Cdd:TIGR00618 475 lqTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 KEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRkknLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSS 1423
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR---LQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1424 MELENVRASHRDSEKRQKKFESQMAEERVAvQKALLDRDAMSQELRDRE---TRVLSLLNEVDIMKEHLEESDRVRRSLQ 1500
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVR-EHALSIRVLPKELLASRQlalQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1501 QELQDSisnkddfGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEK 1580
Cdd:TIGR00618 711 THIEEY-------DREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHL 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1581 RRGLLKQIRDLENELENEKRGKSgavSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQI---IKEYQIECEEARQA 1657
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEA---EIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATlgeITHQLLKYEECSKQ 860
|
..
gi 1767286957 1658 KE 1659
Cdd:TIGR00618 861 LA 862
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
972-1646 |
1.09e-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: 73.52 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 972 LRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRK 1051
Cdd:TIGR04523 49 LKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1052 LLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRedmeterNARNKAEM 1131
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK-------NKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1132 TRREVVAQLEKVK---GDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKaKFSRQVEELHDQIEQHK 1208
Cdd:TIGR04523 202 LLSNLKKKIQKNKsleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-KIKKQLSEKQKELEQNN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1209 KQRSQLEKQQNQADQERADMAQEIA--LLQASRADIDKKRKiheaHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNR 1286
Cdd:TIGR04523 281 KKIKELEKQLNQLKSEISDLNNQKEqdWNKELKSELKNQEK----KLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1287 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETrLKIANINRARQLEDEKNALLDEK-EEAEGLRAHLEKEIHAARQGA 1365
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE-SQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1366 GEARRKAEESVNQ--QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKF 1443
Cdd:TIGR04523 436 IKNNSEIKDLTNQdsVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1444 ESQMAEERVAVQKALLDRDAMSQELRDRETRVlsllnevdimkehleesdrvrrslqqelqdsisNKDDFGKNVHELEKA 1523
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDEL---------------------------------NKDDFELKKENLEKE 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1524 KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSEsdraISNKDVEAEEkrrgllkqirdLENELENEKRGKS 1603
Cdd:TIGR04523 563 IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE----IEEKEKKISS-----------LEKELEKAKKENE 627
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1767286957 1604 GAVSHRKKIENQIGELEQQLEvanRLKEEYNKQLKKNQQIIKE 1646
Cdd:TIGR04523 628 KLSSIIKNIKSKKNKLKQEVK---QIKETIKEIRNKWPEIIKK 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
898-1482 |
1.12e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.54 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 898 LDDIRGRL--------QTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETvRDLEEQLEQEEQARQkllldktnvd 969
Cdd:PRK02224 182 LSDQRGSLdqlkaqieEKEEKDLHERLNGLESELAELDEEIERYEEQREQARET-RDEADEVLEEHEERR---------- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 970 QRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKG-------RLENQLHELEqdlNRERQYK 1042
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGlddadaeAVEARREELE---DRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1043 SELEQHkRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLtrydeESANVTLmqkqmRDMQTTIDELREDMETE 1122
Cdd:PRK02224 328 DRLEEC-RVAAQAHNEEAESLREDADDLEERAEELREEAAELESEL-----EEAREAV-----EDRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1123 RNARNKAEMTRREVVAQLEkvkgDVLDKVDEATmlQDLMSRKDEEVNATKRAIEQIQHTMEGKIEE--QKAKFSRQVEEL 1200
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLE----ELREERDELR--EREAELEATLRTARERVEEAEALLEAGKCPEcgQPVEGSPHVETI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1201 HD---QIEQHKKQRSQLEKQQNQADQ--ERADMAQE----IALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLI 1271
Cdd:PRK02224 471 EEdreRVEELEAELEDLEEEVEEVEErlERAEDLVEaedrIERLEERREDLEELIAERRETIEEKRERAEELRERAAELE 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1272 DQLERSRDEldhLNRVREEEEHAfanmQRRLATAEGQIQELNEQIQEETRL-----KIANINRARQLEDEKNALLDEKEE 1346
Cdd:PRK02224 551 AEAEEKREA---AAEAEEEAEEA----REEVAELNSKLAELKERIESLERIrtllaAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1347 aeglrahLEKEIHAARQgagEARRKAEESVNQ-QLEELRKKNLRDVEHLQK---QLEESEVAKERILQSKKKIQQELEds 1422
Cdd:PRK02224 624 -------ERRERLAEKR---ERKRELEAEFDEaRIEEAREDKERAEEYLEQveeKLDELREERDDLQAEIGAVENELE-- 691
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1767286957 1423 smELENVRASHRDSEKRQKKFESqMAEERVAVQKALLDRDAmsqELRDRETRVLS-LLNEV 1482
Cdd:PRK02224 692 --ELEELRERREALENRVEALEA-LYDEAEELESMYGDLRA---ELRQRNVETLErMLNET 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1268-1879 |
2.35e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1268 RTLIDQLERSRDELDHLNRVREEEEHAFAnmQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEA 1347
Cdd:COG4913 258 RELAERYAAARERLAELEYLRAALRLWFA--QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1348 EGLR-AHLEKEIHAARQGAGEARRKAEEsVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1426
Cdd:COG4913 336 GGDRlEQLEREIERLERELEERERRRAR-LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1427 ENVRASHRDSEKRQKKFESQmaeeRVAVQKALLD-RDAMSQELRDRETRVLSLLNEVDIMKEHLE-----EsdRVRRSLQ 1500
Cdd:COG4913 415 RDLRRELRELEAEIASLERR----KSNIPARLLAlRDALAEALGLDEAELPFVGELIEVRPEEERwrgaiE--RVLGGFA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1501 QELqdsISNKDDFgknvhelEKAKRSLEAELNDMRVQMEELEDNLQIAEDARL-------RLEVTNQALKSEsdraisnk 1573
Cdd:COG4913 489 LTL---LVPPEHY-------AAALRWVNRLHLRGRLVYERVRTGLPDPERPRLdpdslagKLDFKPHPFRAW-------- 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1574 dVEAEEKRRGLLKQIRDLEnELENEKRG-------KSGAVSHRKKI--------------ENQIGELEQQLEVANRLKEE 1632
Cdd:COG4913 551 -LEAELGRRFDYVCVDSPE-ELRRHPRAitragqvKGNGTRHEKDDrrrirsryvlgfdnRAKLAALEAELAELEEELAE 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1633 YNKQLKKNQQIIKEYQIECEEARQAKEDIAALL--READRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKG 1710
Cdd:COG4913 629 AEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1711 GGIsSEEKRRLEAKIAQLEeeleeeqsncelaiDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITE 1790
Cdd:COG4913 709 DEL-KGEIGRLEKELEQAE--------------EELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1791 LESGAQSRARAQMAALEAKV-QYLEDQlNVEGQEKTAANRAARRLEKRLNDTTQqfEDEKRANEQAKELLEKSNLKNR-N 1868
Cdd:COG4913 774 RIDALRARLNRAEEELERAMrAFNREW-PAETADLDADLESLPEYLALLDRLEE--DGLPEYEERFKELLNENSIEFVaD 850
|
650
....*....|.
gi 1767286957 1869 LRRQLDEAEDE 1879
Cdd:COG4913 851 LLSKLRRAIRE 861
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1748 |
2.66e-12 |
|
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: 72.31 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 844 DEIRAKDDELRATKERLLKMEhdfRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDmrdrl 923
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLI---EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 924 seEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKtnvdQRLRNLEERLVELQDAYDKLLKEKRLLEEKvegl 1003
Cdd:pfam02463 231 --YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV----LKENKEEEKEKKLQEEELKLLAKEEEELKS---- 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1004 ttQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKrKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEE 1083
Cdd:pfam02463 301 --ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1084 LQHQLTRYDEESANVTLMQKQMRDmqttiDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKvdeatmlqdlmsR 1163
Cdd:pfam02463 378 KKKLESERLSSAAKLKEEELELKS-----EEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESI------------E 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1164 KDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADID 1243
Cdd:pfam02463 441 LKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGV 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1244 KKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFAN-MQRRLATAEGQIQELNEQIQEETRL 1322
Cdd:pfam02463 521 GGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPlGARKLRLLIPKLKLPLKSIAVLEID 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1323 KIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEElRKKNLRDVEHLQKQLEESE 1402
Cdd:pfam02463 601 PILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAE-KSEVKASLSELTKELLEIQ 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1403 VAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAlldrdamSQELRDRETRVLSLLNEV 1482
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI-------NEELKLLKQKIDEEEEEE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1483 DIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDmrvQMEELEDNLQIAEDARLRLEVTNQAL 1562
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL---RALEEELKEEAELLEEEQLLIEQEEK 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1563 KSESDRAISNKDVEAEEKRRGLL--KQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQ-QLEVANRLKEEYNKQLKK 1639
Cdd:pfam02463 830 IKEEELEELALELKEEQKLEKLAeeELERLEEEITKEELLQELLLKEEELEEQKLKDELESkEEKEKEEKKELEEESQKL 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1640 NQQIIKEYQIECEEAR-QAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEK 1718
Cdd:pfam02463 910 NLLEEKENEIEERIKEeAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
890 900 910
....*....|....*....|....*....|
gi 1767286957 1719 RRLEAKIAQLEEELEEEQSNCELAIDKQRK 1748
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEETCQRL 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1167-1790 |
3.11e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1167 EVNATKRAIEQI---QHTMEGKIEEQKAKF---SRQVEELHDQIEQHKKQRSQLEKQQnqadQERADMAQEIALLQASRA 1240
Cdd:PRK03918 173 EIKRRIERLEKFikrTENIEELIKEKEKELeevLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1241 DIDKKRKIHEAHLMEIQANLAESDEHKRTL------IDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNE 1314
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELeekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1315 QIQEETRLKianiNRARQLEDEKNALLDEKEEAEGLRAHLEkeihaarqgagEARRKAEEsvnqqLEELRKK-NLRDVEH 1393
Cdd:PRK03918 329 RIKELEEKE----ERLEELKKKLKELEKRLEELEERHELYE-----------EAKAKKEE-----LERLKKRlTGLTPEK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1394 LQKQLEESEVAKERILQSKKKIQQELEdssmELENVRASHRDSEKRQKKfesqmAEERVAVQKALLDRDamsqelrdret 1473
Cdd:PRK03918 389 LEKELEELEKAKEEIEEEISKITARIG----ELKKEIKELKKAIEELKK-----AKGKCPVCGRELTEE----------- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1474 rvlsllNEVDIMKEHLEESDRVRRSLQQelqdsisnkddFGKNVHELEKAKRSLEAELNDMRvqmeELEDNLQIAEdarl 1553
Cdd:PRK03918 449 ------HRKELLEEYTAELKRIEKELKE-----------IEEKERKLRKELRELEKVLKKES----ELIKLKELAE---- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1554 RLEVTNQALKSESDRAISNKDVEAE---EKRRGLLKQIRDLENELENEKRGKsgavSHRKKIENQIGELEQQL-EVANRL 1629
Cdd:PRK03918 504 QLKELEEKLKKYNLEELEKKAEEYEklkEKLIKLKGEIKSLKKELEKLEELK----KKLAELEKKLDELEEELaELLKEL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1630 KE---EYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEEL 1706
Cdd:PRK03918 580 EElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1707 RAKGggiSSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQItTDLSMERTLNQKTEAEKQSLERSNRDYKA 1786
Cdd:PRK03918 660 EYEE---LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER-EKAKKELEKLEKALERVEELREKVKKYKA 735
|
....
gi 1767286957 1787 KITE 1790
Cdd:PRK03918 736 LLKE 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1469-1915 |
6.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1469 RDRETRVLSLLNEVDIMKEHLE-ESDRVRR--SLQQELQD-----SISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEE 1540
Cdd:COG1196 185 EENLERLEDILGELERQLEPLErQAEKAERyrELKEELKEleaelLLLKLRELEAELEELEAELEELEAELEELEAELAE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1541 LEDNLQIAEDARLRLEVTNQALKsESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELE 1620
Cdd:COG1196 265 LEAELEELRLELEELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1621 QQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQAR-KQLELE 1699
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLeRLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1700 NDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLER 1779
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL--LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1780 SNRDYkakitelesGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDttqqfEDEKRANEQAKELl 1859
Cdd:COG1196 502 DYEGF---------LEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVV-----EDDEVAAAAIEYL- 566
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1860 eKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTRELMNLRGNN 1915
Cdd:COG1196 567 -KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1271-1693 |
8.25e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.18 E-value: 8.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1271 IDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIqEETRLKIANINRARQLEDEKNALLDEKEEAEGL 1350
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL-EKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1351 RAHLE--KEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELEN 1428
Cdd:COG4717 152 EERLEelRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1429 VRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIM---------KEHLEESDRV---- 1495
Cdd:COG4717 232 LENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALlflllarekASLGKEAEELqalp 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1496 -RRSLQQELQDSISNKDDFGKNVHELE-KAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQAlKSESDRAISNK 1573
Cdd:COG4717 312 aLEELEEEELEELLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA-GVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1574 dVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKK--IENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQI-- 1649
Cdd:COG4717 391 -LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEdg 469
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1767286957 1650 ECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQAR 1693
Cdd:COG4717 470 ELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1027-1691 |
1.59e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 69.94 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1027 QLHELEQDLNRERQykseleqhKRKLLAELEDSKDHLAEKMGKVEELnnqlmkrdEELQHQLTRYDEESAnVTLMQKQMR 1106
Cdd:COG4913 236 DLERAHEALEDARE--------QIELLEPIRELAERYAAARERLAEL--------EYLRAALRLWFAQRR-LELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1107 DMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKvdeatmLQDLMSRKDEEVNATKRAIEQIQHTMEG-- 1184
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ------LEREIERLERELEERERRRARLEALLAAlg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1185 -KIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAEs 1263
Cdd:COG4913 373 lPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1264 dehkrtlidQLERSRDEL----DHLNrVREEEE----------HAFAnmqRRLATAEGQIQELN---EQIQEETRLKIAN 1326
Cdd:COG4913 452 ---------ALGLDEAELpfvgELIE-VRPEEErwrgaiervlGGFA---LTLLVPPEHYAAALrwvNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1327 INRARQLED----EKNALLDEKEEAEG-----LRAHLEKEIHAARQGAGEARRKAEESVNQ-----QLEELRKKNLRDVE 1392
Cdd:COG4913 519 VRTGLPDPErprlDPDSLAGKLDFKPHpfrawLEAELGRRFDYVCVDSPEELRRHPRAITRagqvkGNGTRHEKDDRRRI 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1393 HLQKQLEESEVAKERILQSK-KKIQQELEDSSMELENVRASHRDSEKRQkkfesqMAEERVA-VQKALLDRDAMSQELRD 1470
Cdd:COG4913 599 RSRYVLGFDNRAKLAALEAElAELEEELAEAEERLEALEAELDALQERR------EALQRLAeYSWDEIDVASAEREIAE 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1471 RETRvlsllnevdimKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAED 1550
Cdd:COG4913 673 LEAE-----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1551 ---ARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRgksgavSHRKKIENQIGELEQQLEVAN 1627
Cdd:COG4913 742 larLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR------AFNREWPAETADLDADLESLP 815
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1628 RLKEEYNKQ----LKKNQQIIKEYQIECEEarqakEDIAALLREADrkfRAVEAEREQLREANEGLMQ 1691
Cdd:COG4913 816 EYLALLDRLeedgLPEYEERFKELLNENSI-----EFVADLLSKLR---RAIREIKERIDPLNDSLKR 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1361-1879 |
2.25e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.30 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1361 ARQGAGEARRKAEESVNQ---QLEELRKKNLRD-VEHLQKQLEESEVAKERILQSKKKIQQELEdssmELENVRASHRDS 1436
Cdd:PRK02224 174 ARLGVERVLSDQRGSLDQlkaQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRD----EADEVLEEHEER 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1437 EKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVD--------------IMKEHLEESDRVRRSLQQE 1502
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDdllaeaglddadaeAVEARREELEDRDEELRDR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1503 LQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDraisnkdvEAEEKRR 1582
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE--------ELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1583 GLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEynKQLKKNQQIIKEYQIEC--EEARQAKED 1660
Cdd:PRK02224 402 DAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA--GKCPECGQPVEGSPHVEtiEEDRERVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1661 IAALLREADRKFRAVEAEREQLREANEglMQARKQLELENDELEELRAkgggisSEEKRRLEAKIAQLEEELEEEQSNCE 1740
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLVE--AEDRIERLEERREDLEELI------AERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1741 LAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNR--DYKAKITELESGAQSRaRAQMAALeakvqyleDQLN 1818
Cdd:PRK02224 552 EAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirTLLAAIADAEDEIERL-REKREAL--------AELN 622
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1819 VEGQEKTAANRAARR-LEKRLNDttQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDE 1879
Cdd:PRK02224 623 DERRERLAEKRERKReLEAEFDE--ARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAE 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
845-1419 |
2.87e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 845 EIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVEravIQEQLQQESENSAELDDIRGRLqtrnQELEYIvndmRDRLS 924
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLRE---INEISSELPELREELEKLEKEV----KELEEL----KEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 925 EEEQQNEKNNDERRKQMETVRDlEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLT 1004
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1005 TQLLDHEERAKHGVKAKGRLE-------------NQLHELEQDLNRERQYKSELEQHKRKL-----------LAELEDSK 1060
Cdd:PRK03918 321 EEINGIEERIKELEEKEERLEelkkklkelekrlEELEERHELYEEAKAKKEELERLKKRLtgltpeklekeLEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1061 DHLAEKMGKVEELNNQLMKRDEELQHQLT-------------RYDEESANVTLMQKQMRDMQTTIDELREDMETERNARN 1127
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1128 KAEMTRREVVAQLEKVK-GDVLDKVDEATmlQDLMSRKDEEVNATKRAIEqiqhTMEGKIEEQKAKFSRQVEELhDQIEQ 1206
Cdd:PRK03918 481 ELRELEKVLKKESELIKlKELAEQLKELE--EKLKKYNLEELEKKAEEYE----KLKEKLIKLKGEIKSLKKEL-EKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1207 HKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKR--KIHEAHLMEIQANLAESDehkrtlidqLERSRDELDHL 1284
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERlkELEPFYNEYLELKDAEKE---------LEREEKELKKL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1285 NRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIAniNRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQG 1364
Cdd:PRK03918 625 EEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELR--EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1365 AGEARRKAEESvnqqleELRKKNLRDVEHLQKQLEESEV-AKERILQSKKKIQQEL 1419
Cdd:PRK03918 703 LEEREKAKKEL------EKLEKALERVEELREKVKKYKAlLKERALSKVGEIASEI 752
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
975-1868 |
4.21e-11 |
|
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: 68.46 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 975 LEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrlENQLHELEQDLNRERQYKSELEQHKRKLLA 1054
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKE---KLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1055 ELEDSKDHLAEKMGKVEELNnqlmkrdeelqhqltryDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRR 1134
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKL-----------------AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1135 EVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQiqhtMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQL 1214
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA----EEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1215 EKQQNQADQERADMAQEIALLQaSRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHA 1294
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEAQ-LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1295 FANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE 1374
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAI 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1375 SVNQQLEELRKKnlRDVEHLQKqleeSEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAV 1454
Cdd:pfam02463 546 STAVIVEVSATA--DEVEERQK----LVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1455 QKALLDRDamsqeLRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDM 1534
Cdd:pfam02463 620 KRAKVVEG-----ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1535 RVQMEELEDNLQIAEdarLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIEN 1614
Cdd:pfam02463 695 LRRQLEIKKKEQREK---EELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSL 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1615 QIGELEQQLEVANRLKEEYNKQLKKnqqiiKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARK 1694
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKL-----KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1695 QLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEK 1774
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEE 926
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1775 QSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQ 1854
Cdd:pfam02463 927 AEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
890
....*....|....
gi 1767286957 1855 AKELLEKSNLKNRN 1868
Cdd:pfam02463 1007 LIRAIIEETCQRLK 1020
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
813-1421 |
4.27e-11 |
|
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: 68.46 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 813 RNGLAYLKLRNWQWWRLFTKVKPLLQVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQES 892
Cdd:TIGR00618 232 REALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 893 ENSaeldDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLdktnvdQRL 972
Cdd:TIGR00618 312 IHT----ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT------QHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 973 RNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQ-------DLNRERQYKSEL 1045
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELcaaaitcTAQCEKLEKIHL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1046 EQHKRKL------LAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDM 1119
Cdd:TIGR00618 462 QESAQSLkereqqLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1120 ETERNARNKAEMTRRevvaQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEE 1199
Cdd:TIGR00618 542 TSEEDVYHQLTSERK----QRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1200 LHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQ-----------ASRADIDKKRKIHEAHLMEIQANLAESDEHKR 1268
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqervrehalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1269 TLIDQLERSRDELDHL---NRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKI---------------ANINRA 1330
Cdd:TIGR00618 698 MLAQCQTLLRELETHIeeyDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLkarteahfnnneevtAALQTG 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1331 RQLEDEKNALLDEKEEAE---GLRAHLEKEIHAARQGAGEAR-------RKAEESVNQQLEELRKKnLRDVEHLQKQLEE 1400
Cdd:TIGR00618 778 AELSHLAAEIQFFNRLREedtHLLKTLEAEIGQEIPSDEDILnlqcetlVQEEEQFLSRLEEKSAT-LGEITHQLLKYEE 856
|
650 660
....*....|....*....|.
gi 1767286957 1401 SEVAKERILQSKKKIQQELED 1421
Cdd:TIGR00618 857 CSKQLAQLTQEQAKIIQLSDK 877
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1215-1908 |
6.53e-11 |
|
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: 68.07 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1215 EKQQNQADQERADMAQEiallqASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEldhlnrvREEEEHA 1294
Cdd:pfam02463 145 EIIAMMKPERRLEIEEE-----AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQ-------AKKALEY 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1295 FANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE 1374
Cdd:pfam02463 213 YQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1375 SVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASH-------RDSEKRQKKFESQm 1447
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKReaeeeeeEELEKLQEKLEQL- 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1448 aeERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKD------DFGKNVHELE 1521
Cdd:pfam02463 372 --EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEeeeesiELKQGKLTEE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1522 KAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRG 1601
Cdd:pfam02463 450 KEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1602 K---------SGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLK-KNQQIIKEYQIECEEARQAKEDIAALLREADRK 1671
Cdd:pfam02463 530 RlgdlgvaveNYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLD 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1672 FRAVEAEREQLREAN--EGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKA 1749
Cdd:pfam02463 610 KATLEADEDDKRAKVveGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1750 QVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLE---DQLNVEGQEKTA 1826
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKsrlKKEEKEEEKSEL 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1827 ANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTR 1906
Cdd:pfam02463 770 SLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE 849
|
..
gi 1767286957 1907 EL 1908
Cdd:pfam02463 850 KL 851
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
884-1400 |
7.65e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 7.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 884 IQEQLQQESENSAELDDIRGRLQTRNQEleyivndmRDRLSEEEQQNEKNNDERRKQMETvrDLEEQLEQEEQARQKLLL 963
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQ--------IELLEPIRELAERYAAARERLAEL--EYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 964 dktnVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLttqlldHEERAKHGVKAKGRLENQLHELEQDLNRERQ--- 1040
Cdd:COG4913 293 ----LEAELEELRAELARLEAELERLEARLDALREELDEL------EAQIRGNGGDRLEQLEREIERLERELEERERrra 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1041 ----------------------YKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANV 1098
Cdd:COG4913 363 rleallaalglplpasaeefaaLRAEAAALLEALEEELEALEEALAEAEAALRDLRREL----RELEAEIASLERRKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1099 TLMQKQMRDM---QTTIDE-----------LREDMETERNARNKA----------------------EMTRREVVAQLEK 1142
Cdd:COG4913 439 PARLLALRDAlaeALGLDEaelpfvgelieVRPEEERWRGAIERVlggfaltllvppehyaaalrwvNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1143 VKGDVLD----KVDEATM--------------LQDLMSRK--------DEEVNATKRAIeqiqhTMEGKIeeqKAKFSRQ 1196
Cdd:COG4913 519 VRTGLPDperpRLDPDSLagkldfkphpfrawLEAELGRRfdyvcvdsPEELRRHPRAI-----TRAGQV---KGNGTRH 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1197 VEELHDQIEQH-------KKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHlmeiqANLAESDEHKRT 1269
Cdd:COG4913 591 EKDDRRRIRSRyvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRL-----AEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1270 LIDQLERSRDELDHLnrvrEEEEHAFANMQRRLATAEGQIQELNEQI----QEETRLKiANINRARQLEDEKNALLDEKE 1345
Cdd:COG4913 666 AEREIAELEAELERL----DASSDDLAALEEQLEELEAELEELEEELdelkGEIGRLE-KELEQAEEELDELQDRLEAAE 740
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1346 EAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEE 1400
Cdd:COG4913 741 DLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1282-1893 |
1.45e-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: 66.68 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1282 DHLNRVREEEEHAFANMQRRLataeGQIQELNEQIQEETRLKIANIN-RARQLEDEKNALLD----EKEEAEGLRAHLEK 1356
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRL----NESNELHEKQKFYLRQSVIDLQtKLQEMQMERDAMADirrrESQSQEDLRNQLQN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1357 EIHAArQGAGEARRKAEESVNQQLEELRKKNLRDvEHLQKQLEESEVAKERilQSKKKIQQELEDSSMELENVRAS---- 1432
Cdd:pfam15921 150 TVHEL-EAAKCLKEDMLEDSNTQIEQLRKMMLSH-EGVLQEIRSILVDFEE--ASGKKIYEHDSMSTMHFRSLGSAiski 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1433 --HRDSEKRQKKFESQMAEERVAVQKAlLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNK 1510
Cdd:pfam15921 226 lrELDTEISYLKGRIFPVEDQLEALKS-ESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEII 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1511 DDFGKN--------VHELEKAKRSLEAELNDMRV----QMEELEDNLQIAEDARLRLEVTNQALKSESdraiSNKDVEAE 1578
Cdd:pfam15921 305 QEQARNqnsmymrqLSDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQES----GNLDDQLQ 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1579 EKRRGLLKQIRDLENELENEKR------GKSGAVSH-RKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIEC 1651
Cdd:pfam15921 381 KLLADLHKREKELSLEKEQNKRlwdrdtGNSITIDHlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESL 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1652 EEA-------RQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKgggisSEEKRRLEAK 1724
Cdd:pfam15921 461 EKVssltaqlESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSR-----VDLKLQELQH 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1725 IAQLEEELEEEQSNCE-LAIDKQRKAQV------QLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESgAQS 1797
Cdd:pfam15921 536 LKNEGDHLRNVQTECEaLKLQMAEKDKVieilrqQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI-LKD 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1798 RARAQMAALEAKVQYLEDQ---LNVEGQEKTaanRAARRLEKrlnDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLD 1874
Cdd:pfam15921 615 KKDAKIRELEARVSDLELEkvkLVNAGSERL---RAVKDIKQ---ERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSE 688
|
650
....*....|....*....
gi 1767286957 1875 EAEDEMSRERTKHRNVQRE 1893
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
845-1623 |
1.74e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.61 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 845 EIRAKDDELRATKERLLKMEHDFRENEKKLDQViveraviqeqLQQESENSAELDDIRGRlqtrnqeleyIVNDMRDRLS 924
Cdd:TIGR00606 263 KIMKLDNEIKALKSRKKQMEKDNSELELKMEKV----------FQGTDEQLNDLYHNHQR----------TVREKERELV 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 925 EEEQQNEKNNDERRkqmetVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLlkekrlleEKVEGLT 1004
Cdd:TIGR00606 323 DCQRELEKLNKERR-----LLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGF--------ERGPFSE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1005 TQLLDHEERAKHGVKAKGRLENQL-HELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQL------ 1077
Cdd:TIGR00606 390 RQIKNFHTLVIERQEDEAKTAAQLcADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELqqlegs 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1078 MKRDEELQHQLTRYD------EESANVTLMQKQMRDMQTT----------IDELREDMETERNARNKAEMTRREVVAQLE 1141
Cdd:TIGR00606 470 SDRILELDQELRKAErelskaEKNSLTETLKKEVKSLQNEkadldrklrkLDQEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1142 KVKGDVLDKVDEAT----------MLQDLMSRKDEEVNATKRAIEQIQ------HTMEGKIEEQKAKFSRQVEELHDQI- 1204
Cdd:TIGR00606 550 QIRKIKSRHSDELTsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNkelaslEQNKNHINNELESKEEQLSSYEDKLf 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1205 -----EQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRD 1279
Cdd:TIGR00606 630 dvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1280 ELDHLNRVREEEEHAFANMqrrLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALldekEEAEGLRAHLEKEIH 1359
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEM---LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDI----EEQETLLGTIMPEEE 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1360 AARQgagearRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAK--ERILQSKKKIQQELEDSSMELENVRASHRDSE 1437
Cdd:TIGR00606 783 SAKV------CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1438 KRQKKFESQMAE---ERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFG 1514
Cdd:TIGR00606 857 EQIQHLKSKTNElksEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN 936
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1515 KNVHE--------------------------LEKAKRSLEAELNDMRVQMEELEDNLQ-IAEDARLRLEVTNQALKSES- 1566
Cdd:TIGR00606 937 KKAQDkvndikekvknihgymkdienkiqdgKDDYLKQKETELNTVNAQLEECEKHQEkINEDMRLMRQDIDTQKIQERw 1016
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1567 ------DRAISNKDVEAEEKRRGLLKQI------------RDLENELENEKRGKSGAVSHRKKIENQIGELEQQL 1623
Cdd:TIGR00606 1017 lqdnltLRKRENELKEVEEELKQHLKEMgqmqvlqmkqehQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
925-1660 |
2.10e-10 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 66.22 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 925 EEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKL---LKEKRLLEEKVE 1001
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLdneIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1002 GLTTQLLDHEERAKHGVkakgrlENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRD 1081
Cdd:TIGR00606 283 KDNSELELKMEKVFQGT------DEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1082 EELQHQLTRYDEEsanvtlmqKQMRDMQTTIDELREDMETERNARNKAEMTRREvvaqlekvkgdvldKVDEATMLQDLM 1161
Cdd:TIGR00606 357 DRHQEHIRARDSL--------IQSLATRLELDGFERGPFSERQIKNFHTLVIER--------------QEDEAKTAAQLC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1162 SRKDEEVNATKRAIEQIQHTMEGK---IEEQKAKFSRQVEELhdqieqhKKQRSQLEKQQNQADQ-ERADMAQEIALLQA 1237
Cdd:TIGR00606 415 ADLQSKERLKQEQADEIRDEKKGLgrtIELKKEILEKKQEEL-------KFVIKELQQLEGSSDRiLELDQELRKAEREL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1238 SRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLErsrdELDHLNRVREEEEhafaNMQRRLATAEGQIQELNEQIQ 1317
Cdd:TIGR00606 488 SKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME----QLNHHTTTRTQME----MLTKDKMDKDEQIRKIKSRHS 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1318 EETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARrKAEESVNQQLEELRKKNLR-------- 1389
Cdd:TIGR00606 560 DELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN-NELESKEEQLSSYEDKLFDvcgsqdee 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1390 -DVEHLQKQLEESEVAK----------------------------ERILQSKKKIQQELEDSSMELENVRASHRDSEKRQ 1440
Cdd:TIGR00606 639 sDLERLKEEIEKSSKQRamlagatavysqfitqltdenqsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESEL 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1441 KKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEEsdrvrrslQQELQDSISNKDDFGKNVHEL 1520
Cdd:TIGR00606 719 KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE--------QETLLGTIMPEEESAKVCLTD 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1521 EKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQAL-KSESDRAISNKDVEAEEKRRGLLKQIRDLE---NELE 1596
Cdd:TIGR00606 791 VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQeKQHELDTVVSKIELNRKLIQDQQEQIQHLKsktNELK 870
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1767286957 1597 NEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKED 1660
Cdd:TIGR00606 871 SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET 934
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
844-1167 |
2.63e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 844 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENS-AELDDIRGRLQTRNQELEYI---VNDM 919
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkSELKELEARIEELEEDLHKLeeaLNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 920 RDRLSEEEQQNEknNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDaydkllkEKRLLEEK 999
Cdd:TIGR02169 785 EARLSHSRIPEI--QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-------QIKSIEKE 855
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1000 VEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmk 1079
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL-- 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1080 rdEELQHQLTRYDEESANVTlmqkQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQD 1159
Cdd:TIGR02169 934 --SEIEDPKGEDEEIPEEEL----SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILE 1007
|
....*...
gi 1767286957 1160 LMSRKDEE 1167
Cdd:TIGR02169 1008 RIEEYEKK 1015
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1052-1491 |
2.74e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1052 LLAELEDSKDHLAEKMGKVEELNNQLMKRDE----ELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARN 1127
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEeelkEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1128 KAEMTRRevVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQH 1207
Cdd:COG4717 127 LLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1208 KKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEL------ 1281
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1282 ------DHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLE 1355
Cdd:COG4717 285 llallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1356 KEIHAARQGAGEARRKA--EESVNQQLEELRKKN--LRDVEHLQKQLEESEVAKERILQ--SKKKIQQELEDSSMELENV 1429
Cdd:COG4717 365 LEELEQEIAALLAEAGVedEEELRAALEQAEEYQelKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEEL 444
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1767286957 1430 RASHRDSEKRQKKFESQM--AEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEE 1491
Cdd:COG4717 445 EEELEELREELAELEAELeqLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1382-1912 |
7.90e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1382 ELRKKNLRDV----EHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESqmaeerVAVQKA 1457
Cdd:PRK03918 175 KRRIERLEKFikrtENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE------LEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1458 LLDRDAMSQELRDRETRvlSLLNEVdimKEHLEESDRVRRSLQqELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQ 1537
Cdd:PRK03918 249 SLEGSKRKLEEKIRELE--ERIEEL---KKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1538 MEELEDNLQIAEDARLRLEVTNQALKS-ESDRAISNKDVEAEEKRRGLLKQIR------------DLENELENEKRGKSG 1604
Cdd:PRK03918 323 INGIEERIKELEEKEERLEELKKKLKElEKRLEELEERHELYEEAKAKKEELErlkkrltgltpeKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1605 AVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKK------------NQQIIKEYQIECEEARQAKEDIAALLREADRKF 1672
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1673 RAVEAEREQLREanegLMQARKqlelENDELEELRAKGGGISSEEkrrLEAKIAQLeeeleeeqsncELAIDKQRKAQVQ 1752
Cdd:PRK03918 483 RELEKVLKKESE----LIKLKE----LAEQLKELEEKLKKYNLEE---LEKKAEEY-----------EKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1753 LEQITTDLSMERTLNQKTEAekqsLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAanraar 1832
Cdd:PRK03918 541 IKSLKKELEKLEELKKKLAE----LEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA------ 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1833 rlEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRErtKHRNVQREADDLLDANEQLTRELMNLR 1912
Cdd:PRK03918 611 --EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEELE 686
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1074-1445 |
8.52e-10 |
|
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: 63.99 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1074 NNQLMKRDEELqHQLTRYDEESANVTLMQKQMRDMQTTIDELREdmETERNARnkaEMTRREVVAQLEKVKGDVLDKVDE 1153
Cdd:pfam17380 261 NGQTMTENEFL-NQLLHIVQHQKAVSERQQQEKFEKMEQERLRQ--EKEEKAR---EVERRRKLEEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1154 ATMLQDLMSRKDEevnatkRAIEQIQHtmegkiEEQKAKFSR-QVEELHDQIEQHKK-QRSQLEKQQ-NQADQERADMAQ 1230
Cdd:pfam17380 335 IYAEQERMAMERE------RELERIRQ------EERKRELERiRQEEIAMEISRMRElERLQMERQQkNERVRQELEAAR 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1231 EIALLQASRadidkKRKIHEaHLMEIQANLAESDEHKRTLIDQLERSRDEldHLNRVREEEEHAFANMQR-RLATAEGQI 1309
Cdd:pfam17380 403 KVKILEEER-----QRKIQQ-QKVEMEQIRAEQEEARQREVRRLEEERAR--EMERVRLEEQERQQQVERlRQQEEERKR 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1310 QELNEQIQEETRLKIANINRA---RQLEDEKNALLDEKEEaeglRAHLEKEIhaarqgagEARRKA--EESVNQQLEELR 1384
Cdd:pfam17380 475 KKLELEKEKRDRKRAEEQRRKileKELEERKQAMIEEERK----RKLLEKEM--------EERQKAiyEEERRREAEEER 542
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1767286957 1385 KKnlrdvehlQKQLEESEVAKERILQSKKKiQQELEDSSMELENVRAShRDSEKRQKKFES 1445
Cdd:pfam17380 543 RK--------QQEMEERRRIQEQMRKATEE-RSRLEAMEREREMMRQI-VESEKARAEYEA 593
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
838-1383 |
9.76e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQqesensaELDDIRGRLQTRNqeleyivN 917
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVR-------DLRERLEELEEER-------D 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 918 DMRDRLSEEEqqneknnderrkqmetvrdleeqleqeeqarqkllLDKTNVDQRLRNLEERLVELQDAydklLKEKRL-- 995
Cdd:PRK02224 297 DLLAEAGLDD-----------------------------------ADAEAVEARREELEDRDEELRDR----LEECRVaa 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 996 --LEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSkdhlAEKMGKVEEL 1073
Cdd:PRK02224 338 qaHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA----PVDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1074 NNQLMKRDEELQHQLTrydEESANVTLMQKQMRDMQTTIDELR-----------EDMETERNARNKAEMTRREvVAQLEK 1142
Cdd:PRK02224 414 LEELREERDELREREA---ELEATLRTARERVEEAEALLEAGKcpecgqpvegsPHVETIEEDRERVEELEAE-LEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1143 VKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQhTMEGKIEEQkakfSRQVEELHDQIEQHKKQRSQLEKQQNQAD 1222
Cdd:PRK02224 490 EVEEVEERLERAEDLVEAEDRIERLEERREDLEELIA-ERRETIEEK----RERAEELRERAAELEAEAEEKREAAAEAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1223 QERADMAQEIALLQASRADIDKKRkiheahlmEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEehafanmQRRL 1302
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERI--------ESLERIRTLLAAIADAEDEIERLREKREALAELNDER-------RERL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1303 ATAEGQIQELNEQIQEEtRLKIANINRAR------QLEDEKNALLDEKEEAEGLRAHLEKEIHA-----ARQGAGEARRK 1371
Cdd:PRK02224 630 AEKRERKRELEAEFDEA-RIEEAREDKERaeeyleQVEEKLDELREERDDLQAEIGAVENELEEleelrERREALENRVE 708
|
570
....*....|..
gi 1767286957 1372 AEESVNQQLEEL 1383
Cdd:PRK02224 709 ALEALYDEAEEL 720
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
869-1430 |
1.24e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.50 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 869 ENEKKLDQVIVERAVIQEQL----QQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDeRRKQMETV 944
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIkndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYND-LKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 945 RDLEEQLEQEEQARQKLLldkTNVDQRLRNLEERLVELQdaydkllkekrLLEEKVEGLTTQLLDHEERAKHGVKAKGRL 1024
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNI---DKIKNKLLKLELLLSNLK-----------KKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1025 ENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANVTLmqKQ 1104
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWN--KE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1105 MRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKvkgdvldkvdEATMLQDLMSRKDEEVNATKRAIEQIQHTMEG 1184
Cdd:TIGR04523 312 LKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKK----------ELTNSESENSEKQRELEEKQNEIEKLKKENQS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1185 KIEEQKaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKiheahlmeiqaNLAESD 1264
Cdd:TIGR04523 382 YKQEIK-NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK-----------DLTNQD 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1265 EHKRTLIDQLERSRDE----LDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETrlkianiNRARQLEDEKNAL 1340
Cdd:TIGR04523 450 SVKELIIKNLDNTRESletqLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELE-------EKVKDLTKKISSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1341 LDEKEEAEGLRAHLEKEIhaarqgagearRKAEESVNQQLEELRKKNLRDV-EHLQKQLEESEVAKERILQSKKKIQQEL 1419
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKI-----------SDLEDELNKDDFELKKENLEKEiDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
570
....*....|.
gi 1767286957 1420 EDSSMELENVR 1430
Cdd:TIGR04523 592 DQKEKEKKDLI 602
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
970-1375 |
2.00e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 970 QRLRNLEERLVELQDAYDKLLKEKRLLEEKVE--GLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQ 1047
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1048 HKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEEsanvtlMQKQMRDMQTTIDELREDMETERNARN 1127
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE------LEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1128 KAEMTRREVVAQLEKVKGDVLDKVDE-----------ATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSR- 1195
Cdd:COG4717 249 RLLLLIAAALLALLGLGGSLLSLILTiagvlflvlglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAl 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1196 ---------QVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLmEIQANLAESDEH 1266
Cdd:COG4717 329 glppdlspeELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEEL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1267 KRTLIDQLERSRDELDHLNRVREEEEHafANMQRRLATAEGQIQELNEQIQeETRLKIANINRARQLEDeknaLLDEKEE 1346
Cdd:COG4717 408 EEQLEELLGELEELLEALDEEELEEEL--EELEEELEELEEELEELREELA-ELEAELEQLEEDGELAE----LLQELEE 480
|
410 420 430
....*....|....*....|....*....|..
gi 1767286957 1347 AEGLRAHLEKEIHAARQGA---GEARRKAEES 1375
Cdd:COG4717 481 LKAELRELAEEWAALKLALellEEAREEYREE 512
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
916-1685 |
2.05e-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: 62.93 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 916 VNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEkrl 995
Cdd:pfam12128 211 VVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE--- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 996 LEEKVEGLTTQLLDHEERAKHGVKA-KGRLENQLHELEQDLNRERQYKSElEQHKRKLLAELEDSkdhlaekmgkveeLN 1074
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAaDAAVAKDRSELEALEDQHGAFLDA-DIETAAADQEQLPS-------------WQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1075 NQLMKRDEELQHQLTRY-DEESANVTLMQKQMRDMQTTIDELREDMETERNARNKaemtrrevvaQLEKVKGDvldkvde 1153
Cdd:pfam12128 354 SELENLEERLKALTGKHqDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDR----------QLAVAEDD------- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1154 atmLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQV--EELHDQIEQHKKQRSQLEKQQNQADQERADMAQE 1231
Cdd:pfam12128 417 ---LQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATatPELLLQLENFDERIERAREEQEAANAEVERLQSE 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1232 IALLQASRADIDKKRKIHEAHLMEIQANLAEsdehkrtLIDQLERSRDELDHLnrVREEEEHAFANMQRRLATAEGQIQE 1311
Cdd:pfam12128 494 LRQARKRRDQASEALRQASRRLEERQSALDE-------LELQLFPQAGTLLHF--LRKEAPDWEQSIGKVISPELLHRTD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1312 LNEQIQEEtrlkianinrarQLEDEKNALldekeeaeGLRAHLEkeihaarqgageaRRKAEESV--NQQLEELR---KK 1386
Cdd:pfam12128 565 LDPEVWDG------------SVGGELNLY--------GVKLDLK-------------RIDVPEWAasEEELRERLdkaEE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1387 NLRDVEHLQKQLEESEVAkerilqskkkIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDR-DAMS 1465
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQ----------ANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkDSAN 681
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1466 QELRDRETRVLSLLNEVDIMKEHLeesdrvrrslqqelqdsisnKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNL 1545
Cdd:pfam12128 682 ERLNSLEAQLKQLDKKHQAWLEEQ--------------------KEQKREARTEKQAYWQVVEGALDAQLALLKAAIAAR 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1546 QIAEDARLRlevtnqALKSESDRAISNKDVEaEEKRRGLLKQIRDLENELENEKRGKSGAVS------HRKKIENQigEL 1619
Cdd:pfam12128 742 RSGAKAELK------ALETWYKRDLASLGVD-PDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqETWLQRRP--RL 812
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1620 EQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREA 1685
Cdd:pfam12128 813 ATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED 878
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1194-1412 |
2.09e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1194 SRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQ 1273
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1274 LERSRDELDHLNRVREEEEHA-----------FANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLD 1342
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1343 EKEEAEGLRAHLEKEIhAARQGAGEARRKAEESVNQQLEELrKKNLRDVEHLQKQLEESEVAKERILQSK 1412
Cdd:COG4942 179 LLAELEEERAALEALK-AERQKLLARLEKELAELAAELAEL-QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1166-1386 |
2.40e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1166 EEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKK 1245
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA-ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1246 RKIHEAHLMEIQANLAESDEHKRTLI-------DQLERSRDELDHLNRVREEEehaFANMQRRLATAEGQIQELNEQIQE 1318
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllspedfLDAVRRLQYLKYLAPARREQ---AEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1319 ETRLKianinraRQLEDEKNALLDEKEEAEGLRAHLEKEIhAARQGAGEARRKAEESVNQQLEELRKK 1386
Cdd:COG4942 176 LEALL-------AELEEERAALEALKAERQKLLARLEKEL-AELAAELAELQQEAEELEALIARLEAE 235
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1010-1884 |
2.43e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1010 HEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLaekmgkveelnnQLMKRDEELQHQLT 1089
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHL------------NLVQTALRQQEKIE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1090 RYDEEsanvtlmqkqmrdmqttIDELREDMETERNARNKAemtrREVVAQLEKVKGDVLDKVDE-ATMLQDLMSRKDEev 1168
Cdd:PRK04863 352 RYQAD-----------------LEELEERLEEQNEVVEEA----DEQQEENEARAEAAEEEVDElKSQLADYQQALDV-- 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1169 nATKRAIeQIQHTMEGKieeQKAKFSRQVEELHdqIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKI 1248
Cdd:PRK04863 409 -QQTRAI-QYQQAVQAL---ERAKQLCGLPDLT--ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQL 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1249 HEAHLMEIQANlaESDEHKRTLIDQLERSRDELDHLNRvreeeehafanMQRRLATAEgqiQELNEQIQEETRLKIANIN 1328
Cdd:PRK04863 482 VRKIAGEVSRS--EAWDVARELLRRLREQRHLAEQLQQ-----------LRMRLSELE---QRLRQQQRAERLLAEFCKR 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1329 RARQLEDEknalldekEEAEGLRAHLEKEIHAARQGAGEARRKAEEsVNQQLEELRkknlRDVEHLQKQLEESEVAKERI 1408
Cdd:PRK04863 546 LGKNLDDE--------DELEQLQEELEARLESLSESVSEARERRMA-LRQQLEQLQ----ARIQRLAARAPAWLAAQDAL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1409 LQSKKKIQQELEDSSMeLENVRASHRDSEKrqkkfESQMAEERVAVQKALLDR------------DAMSQELRDRETRVl 1476
Cdd:PRK04863 613 ARLREQSGEEFEDSQD-VTEYMQQLLERER-----ELTVERDELAARKQALDEeierlsqpggseDPRLNALAERFGGV- 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1477 sLLNEV--DIMkehLEES-------------------DRVRRSLQQE---------LQDSISNKDDFGKNVHELEKA--- 1523
Cdd:PRK04863 686 -LLSEIydDVS---LEDApyfsalygparhaivvpdlSDAAEQLAGLedcpedlylIEGDPDSFDDSVFSVEELEKAvvv 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1524 -------------------KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNK-DVEAEEKRRG 1583
Cdd:PRK04863 762 kiadrqwrysrfpevplfgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAfEADPEAELRQ 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1584 LLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEynkqlkknqQIIKEYQiECEEARQAKEDIAA 1663
Cdd:PRK04863 842 LNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADE---------TLADRVE-EIREQLDEAEEAKR 911
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1664 LLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAI 1743
Cdd:PRK04863 912 FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLNEKLR 991
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1744 DKQRKAQVQLEQITTDLSMERtlNQKTEAEK--QSLERSNRDYKAKITELE-----------SGAQSRARAQMAALEA-- 1808
Cdd:PRK04863 992 QRLEQAEQERTRAREQLRQAQ--AQLAQYNQvlASLKSSYDAKRQMLQELKqelqdlgvpadSGAEERARARRDELHArl 1069
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1809 -----KVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRE 1883
Cdd:PRK04863 1070 sanrsRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAYLSADELRS 1149
|
.
gi 1767286957 1884 R 1884
Cdd:PRK04863 1150 M 1150
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
26-69 |
3.84e-09 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 53.97 E-value: 3.84e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1767286957 26 RKLCWVPDQNEGFLIGSIKRETNDEVLVELvDTSRQVTISRDDV 69
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1025-1699 |
5.11e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 61.66 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1025 ENQLHELEQDLNRERQYKSEL----EQHKRKLLAELEDSKDHLAEKMGKVEELN--NQLMKRDEELQHQLTRYDEESANV 1098
Cdd:pfam05483 105 ENKLQENRKIIEAQRKAIQELqfenEKVSLKLEEEIQENKDLIKENNATRHLCNllKETCARSAEKTKKYEYEREETRQV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1099 TL-MQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEK-VKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIE 1176
Cdd:pfam05483 185 YMdLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEeYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1177 QIQHtmegKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEK-----QQNQADQERADMAQEIALL---------QASRADI 1242
Cdd:pfam05483 265 ESRD----KANQLEEKTKLQDENLKELIEKKDHLTKELEDikmslQRSMSTQKALEEDLQIATKticqlteekEAQMEEL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1243 DKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRL 1322
Cdd:pfam05483 341 NKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1323 kianINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAgEARRKAEESVNQQLEELRKknlrDVEHLQKQLEESE 1402
Cdd:pfam05483 421 ----LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQL-TAIKTSEEHYLKEVEDLKT----ELEKEKLKNIELT 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1403 VAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKfesqmaeervavqkalldrdaMSQELRDRETRVLSLLNEV 1482
Cdd:pfam05483 492 AHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER---------------------MLKQIENLEEKEMNLRDEL 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1483 DIMKEHLEESdrvRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQiaedarlRLEVTNQAL 1562
Cdd:pfam05483 551 ESVREEFIQK---GDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE-------ELHQENKAL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1563 KSESdrAISNKDVEAEEKRrgllkqIRDLENELENEKRGKSGAV-SHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQ 1641
Cdd:pfam05483 621 KKKG--SAENKQLNAYEIK------VNKLELELASAKQKFEEIIdNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1642 QIIKEYQIECEEA----RQAKEDIAALLREADRK---FRAVEAEREQLREANE--------GLMQARKQLELE 1699
Cdd:pfam05483 693 EIDKRCQHKIAEMvalmEKHKHQYDKIIEERDSElglYKNKEQEQSSAKAALEielsnikaELLSLKKQLEIE 765
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1120 |
7.04e-09 |
|
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: 61.23 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVN 917
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 918 DMRDRLSEEEQQNEKNNDERRKQMETV-------RDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLL 990
Cdd:TIGR02168 828 SLERRIAATERRLEDLEEQIEELSEDIeslaaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 991 KEKRLLEEKVEGLTTQLLDHEERakhgvkaKGRLENQLHELEQDLNRErqYKSELE---QHKRKLLAELEDSKDHLAEKM 1067
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELR-------LEGLEVRIDNLQERLSEE--YSLTLEeaeALENKIEDDEEEARRRLKRLE 978
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1068 GKVEELNNQLMKRDEELQHQLTRYDEesanvtlMQKQMRDMQTTIDELREDME 1120
Cdd:TIGR02168 979 NKIKELGPVNLAAIEEYEELKERYDF-------LTAQKEDLTEAKETLEEAIE 1024
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1186-1582 |
7.58e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.91 E-value: 7.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1186 IEEQKAKFSRQVEELHDQIEQhkkQRSQLEKQQNQADQERADMAQEIAllQASRADIDKKRKIHEAHlmeiqANLAESDE 1265
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAE--KARQAEMDRQAAIYAEQ-----ERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1266 HKRTLIDQLERSRDeldhLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEEtrlkianinrarqLEDEKNALLDEKE 1345
Cdd:pfam17380 348 RELERIRQEERKRE----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQE-------------LEAARKVKILEEE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1346 eaeglrahlekeihaaRQGAGEARRKAEESVNQQLEELRKKNLRDVEhlqkqlEESEVAKERILQSKKKIQQELEdssme 1425
Cdd:pfam17380 411 ----------------RQRKIQQQKVEMEQIRAEQEEARQREVRRLE------EERAREMERVRLEEQERQQQVE----- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1426 lenvRASHRDSEKRQKKFESQmAEERVAVQKALLDRDAMSQELRDRETRVLsllnevdimkehleESDRVRRSLQQELQD 1505
Cdd:pfam17380 464 ----RLRQQEEERKRKKLELE-KEKRDRKRAEEQRRKILEKELEERKQAMI--------------EEERKRKLLEKEMEE 524
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767286957 1506 SisnkddfgKNVHELEKAKRSLEAElndmRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRR 1582
Cdd:pfam17380 525 R--------QKAIYEEERRREAEEE----RRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1328-1907 |
8.16e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1328 NRARQLEDEKNALLDEKEEAEGLRAHLEKEihaarqgAGEARRKAEESvnQQLEELRK-KNLRDVEHLQKQLEESEVAKE 1406
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARK-------AEEAKKKAEDA--RKAEEARKaEDARKAEEARKAEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1407 RILQSKKKIQQEledssmelenvrashRDSEKRQKKFESQMAEErvaVQKALLDRDAmsQELRDRETRVLSllnevdimk 1486
Cdd:PTZ00121 1158 RKAEDARKAEEA---------------RKAEDAKKAEAARKAEE---VRKAEELRKA--EDARKAEAARKA--------- 1208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1487 EHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAE----LNDMRVQMEELEDNLQIAEDARLRLEVTNQAL 1562
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEeirkFEEARMAHFARRQAAIKAEEARKADELKKAEE 1288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1563 KSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIEnqigELEQQLEVANRLKEEYNKQLKKNQQ 1642
Cdd:PTZ00121 1289 KKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE----EAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1643 IIKEYQIECEEARQAKEDI---AALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKR 1719
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAkkkAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1720 RLEAkiAQLEEELEEEQSNCELAIDKQRKAQvqleqittdlSMERTLNQKTEAEKqsLERSNRDYKAKITELESGAQSRA 1799
Cdd:PTZ00121 1445 KADE--AKKKAEEAKKAEEAKKKAEEAKKAD----------EAKKKAEEAKKADE--AKKKAEEAKKKADEAKKAAEAKK 1510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1800 RAQMAALEAKVQYLEDQLNVEgqEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDE 1879
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAE--EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580
....*....|....*....|....*...
gi 1767286957 1880 MSRERTKHRNVQREADDLLDAnEQLTRE 1907
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKA-EEAKKA 1615
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1298-1649 |
1.38e-08 |
|
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: 60.14 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1298 MQRRLATAEGQIQELNEQIQEEtRLKIANINRARQLEDEKNalLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVN 1377
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQE-RLRQEKEEKAREVERRRK--LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1378 QqleELRKKNLRDVEHLQKQLEESEVAKERILQSKKkiQQELEDSSMELENVRASHRDSEKRQKKFESQMAE-ERVAVQK 1456
Cdd:pfam17380 355 Q---EERKRELERIRQEEIAMEISRMRELERLQMER--QQKNERVRQELEAARKVKILEEERQRKIQQQKVEmEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1457 alldrdamsQELRDRETRVLSLLNEVDIMKEHLEESDRvrrslQQELQDSISNKDDFGKNVHELEKAKRS-LEAELNDMR 1535
Cdd:pfam17380 430 ---------EEARQREVRRLEEERAREMERVRLEEQER-----QQQVERLRQQEEERKRKKLELEKEKRDrKRAEEQRRK 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1536 VQMEELEDNLQ-IAEDARLRLEVTNQAlkSESDRAIsnkdveAEEKRRGLLKQIRDLENELEnekrgksgavsHRKKIEN 1614
Cdd:pfam17380 496 ILEKELEERKQaMIEEERKRKLLEKEM--EERQKAI------YEEERRREAEEERRKQQEME-----------ERRRIQE 556
|
330 340 350
....*....|....*....|....*....|....*...
gi 1767286957 1615 QI---GELEQQLEVANRlKEEYNKQLKKNQQIIKEYQI 1649
Cdd:pfam17380 557 QMrkaTEERSRLEAMER-EREMMRQIVESEKARAEYEA 593
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1306-1910 |
2.12e-08 |
|
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: 59.60 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1306 EGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELrk 1385
Cdd:TIGR00618 151 QGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKEL-- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1386 KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQ-----MAEERVAVQKALLD 1460
Cdd:TIGR00618 229 KHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaapLAAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1461 RDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKR--SLEAELNDMRVQM 1538
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQqhTLTQHIHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1539 EELEDNLQI--AEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEkrgksgavshrkkIENQI 1616
Cdd:TIGR00618 389 TTLTQKLQSlcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCT-------------AQCEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1617 GELEQQLEVANRLKEEyNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQL--REANEGLMQARK 1694
Cdd:TIGR00618 456 LEKIHLQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnPGPLTRRMQRGE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1695 QLELENDELEELrAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEK 1774
Cdd:TIGR00618 535 QTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1775 QSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYledQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDE----KR 1850
Cdd:TIGR00618 614 QHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQKmqseKE 690
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1851 ANEQAKELLEKSNLknrnLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTRELMN 1910
Cdd:TIGR00618 691 QLTYWKEMLAQCQT----LLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1502-1863 |
2.41e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1502 ELQDSISNKDDFGKnvhELEKAKRSLE-AELNDMRVQ--MEELEDNLQIAEDARLRLEvTNQALKSESdraisnKDVEAE 1578
Cdd:TIGR02169 157 KIIDEIAGVAEFDR---KKEKALEELEeVEENIERLDliIDEKRQQLERLRREREKAE-RYQALLKEK------REYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1579 EkrrgLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKN--------QQIIKEYQIE 1650
Cdd:TIGR02169 227 E----LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1651 CEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLmqarkqlELENDELEELRAKGGGISSEEKRRLEAKIAQLEE 1730
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEEL-------EREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1731 ELEEEQSncelAIDKQRKAQVQLEQITTDL-SMERTLNQKTEAEKQSLERSNR------DYKAKITELESGAQSrARAQM 1803
Cdd:TIGR02169 376 VDKEFAE----TRDELKDYREKLEKLKREInELKRELDRLQEELQRLSEELADlnaaiaGIEAKINELEEEKED-KALEI 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1804 AALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLND----------TTQQFEDEKRANEQAKELLEKSN 1863
Cdd:TIGR02169 451 KKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKlqrelaeaeaQARASEERVRGGRAVEEVLKASI 520
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
837-1399 |
3.52e-08 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 59.08 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 837 LQVTRTDDEIRAKDDELR----ATKERLLKMEH--DFRENEKK--LDQVIVERAVIQEQL---QQESEN-SAELDDIRGR 904
Cdd:pfam12128 290 QLLRTLDDQWKEKRDELNgelsAADAAVAKDRSelEALEDQHGafLDADIETAAADQEQLpswQSELENlEERLKALTGK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 905 LQTRNQELEY----IVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEqaRQKLLLDKTNVDQRLRNLEERLV 980
Cdd:pfam12128 370 HQDVTAKYNRrrskIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESEL--REQLEAGKLEFNEEEYRLKSRLG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 981 ELQDAYDKLLKEKRLLEEKV----------EGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKR 1050
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLEnfderierarEEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELEL 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1051 K-------LLAELEDSKDHLAEKMGKVeeLNNQLMKR--------DEELQHQLTRYdeeSANVTLMQKQMRDMQTTIDEL 1115
Cdd:pfam12128 528 QlfpqagtLLHFLRKEAPDWEQSIGKV--ISPELLHRtdldpevwDGSVGGELNLY---GVKLDLKRIDVPEWAASEEEL 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1116 REdmetERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSR 1195
Cdd:pfam12128 603 RE----RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1196 QVEELHDQIEQHKKQ-----RSQLEKQQNQADQERADMAQEIALLQASR--------ADIDKKRKIHEAHLMEIQA---- 1258
Cdd:pfam12128 679 SANERLNSLEAQLKQldkkhQAWLEEQKEQKREARTEKQAYWQVVEGALdaqlallkAAIAARRSGAKAELKALETwykr 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1259 ----------NLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFA----NMQRRLATAEGQIQELNEQ---IQEETR 1321
Cdd:pfam12128 759 dlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLqrrpRLATQLSNIERAISELQQQlarLIADTK 838
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1322 LKIANINRARQLEDEKNALLDEkeEAEGLRAHLEK--EIHAArQGAGEARRKAEESvNQQLEELRKKNLRDVEHLQKQLE 1399
Cdd:pfam12128 839 LRRAKLEMERKASEKQQVRLSE--NLRGLRCEMSKlaTLKED-ANSEQAQGSIGER-LAQLEDLKLKRDYLSESVKKYVE 914
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1270-1792 |
3.98e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 58.76 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1270 LIDQLERSRDELDHLNRVREEEEhafanmqRRLATAEGQIQELNEQIQEETRLKI---ANINRARQLEDEKNALLDEKEE 1346
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDE-------KSHSITLKEIERLSIEYNNAMDDYNnlkSALNELSSLEDMKNRYESEIKT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1347 AEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRkknlrDVEHLQKQLEEsevaKERILQSKKKIQQELEDSSMEL 1426
Cdd:PRK01156 261 AESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYIN-----DYFKYKNDIEN----KKQILSNIDAEINKYHAIIKKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1427 ENVRASHRDSEKRQKKFEsqmaeervavqkallDRDAMSQELRDRETRVLSLLNEVDIMKEHLEE--------SDRVRRS 1498
Cdd:PRK01156 332 SVLQKDYNDYIKKKSRYD---------------DLNNQILELEGYEMDYNSYLKSIESLKKKIEEyskniermSAFISEI 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1499 LQ-QELQDSISNK--DDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAE----------------DARLRLEVTN 1559
Cdd:PRK01156 397 LKiQEIDPDAIKKelNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqsvcpvcgttlgeekSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1560 QALKSESD-RAISNKDVEAEEKRRGLLKQIRDLE----NELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYN 1634
Cdd:PRK01156 477 KKSRLEEKiREIEIEVKDIDEKIVDLKKRKEYLEseeiNKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1635 ---------KQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEE 1705
Cdd:PRK01156 557 slkledldsKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYN 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1706 LrakgggisSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYK 1785
Cdd:PRK01156 637 E--------IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILR 708
|
....*..
gi 1767286957 1786 AKITELE 1792
Cdd:PRK01156 709 TRINELS 715
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1569-1805 |
4.50e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1569 AISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQ 1648
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1649 iecEEARQAKEDIAALLREAdrkFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGIsSEEKRRLEAKIAQL 1728
Cdd:COG4942 97 ---AELEAQKEELAELLRAL---YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767286957 1729 EEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAA 1805
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1213 |
4.97e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 919 MRDRLSEEEQQNEKNNDERRKQ-------METVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDA------ 985
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIenrldelSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEienvks 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 986 -YDKLLKEKRLLEEKVEGLTTQLLDHEER-AKHGVKAKG-----------RLENQLHELEQDLNRERQYKSELEQHKRKL 1052
Cdd:TIGR02169 759 eLKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQaelskleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1053 LAELEDSKDHLAEKMGKVEELNNQLMKRDEEL-QHQLTRYDEESANVTL------MQKQMRDMQTTIDELREDMETERNA 1125
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIENLNGKKEELEEELeELEAALRDLESRLGDLkkerdeLEAQLRELERKIEELEAQIEKKRKR 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1126 RNKAEMTRREV---VAQLEKVKGDVLDKVDEATMLQDLMSRKD---------EEVNAtkRAIEQIQHTME--GKIEEQKA 1191
Cdd:TIGR02169 919 LSELKAKLEALeeeLSEIEDPKGEDEEIPEEELSLEDVQAELQrveeeiralEPVNM--LAIQEYEEVLKrlDELKEKRA 996
|
330 340
....*....|....*....|..
gi 1767286957 1192 KFSRQVEELHDQIEQHKKQRSQ 1213
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKRE 1018
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1365-1691 |
6.02e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 6.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1365 AGEARRKAEESVNQQLEELRKKNLRDVEhlQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQK--- 1441
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAE--QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERyqa 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1442 ---KFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQ-----DSISNKDDF 1513
Cdd:PRK04863 356 dleELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQaleraKQLCGLPDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1514 gkNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDrAISNKDveAEEKRRGLLKQIRDLEN 1593
Cdd:PRK04863 436 --TADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAG-EVSRSE--AWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1594 ELENEKrgksgavshrkKIENQIGELEQQLEV---ANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADR 1670
Cdd:PRK04863 511 LAEQLQ-----------QLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
330 340
....*....|....*....|.
gi 1767286957 1671 KFRAVEAEREQLREANEGLMQ 1691
Cdd:PRK04863 580 RRMALRQQLEQLQARIQRLAA 600
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
844-1314 |
8.92e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 844 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAE-LDDIRGR---LQTRNQELEYIVNDM 919
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREdADDLEERaeeLREEAAELESELEEA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 920 RDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEerlVELQDAYDKLLKEKRLLEEK 999
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELE---ATLRTARERVEEAEALLEAG 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1000 VEGLTTQLLDHEERakhgVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKL--LAELEDSKDHLAEKMGKVEELNNQL 1077
Cdd:PRK02224 453 KCPECGQPVEGSPH----VETIEEDRERVEELEAELEDLEEEVEEVEERLERAedLVEAEDRIERLEERREDLEELIAER 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1078 MKRDEELQHQLTRYDEESanvtlmqkqmrdmqttiDELREDMETERNARNKAEM---TRREVVAQLEKVKGDVLDKVDEA 1154
Cdd:PRK02224 529 RETIEEKRERAEELRERA-----------------AELEAEAEEKREAAAEAEEeaeEAREEVAELNSKLAELKERIESL 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1155 TMLQDLMSRKDEevnatkrAIEQIqhtmeGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEkqqNQADQERADMAQEial 1234
Cdd:PRK02224 592 ERIRTLLAAIAD-------AEDEI-----ERLREKREALAELNDERRERLAEKRERKRELE---AEFDEARIEEARE--- 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1235 lqasradidkKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEhAFANMQRRLATAEGQIQELNE 1314
Cdd:PRK02224 654 ----------DKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERRE-ALENRVEALEALYDEAEELES 722
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
850-1301 |
9.77e-08 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 57.15 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 850 DDELRATKErlLKM----EHDFRENEKKLDQVIVER-AVIQEQLQQESENSA---------ELDDIRGRLQtrnqELEYI 915
Cdd:PRK04778 47 NDELEKVKK--LNLtgqsEEKFEEWRQKWDEIVTNSlPDIEEQLFEAEELNDkfrfrkakhEINEIESLLD----LIEED 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 916 VNDMRDRLSEEEQQNEKNnderRKQMETVRDLEEQleqeeqARQKLLLDKTNVDQRLRNLEERLVELQDAYdkllkekrl 995
Cdd:PRK04778 121 IEQILEELQELLESEEKN----REEVEQLKDLYRE------LRKSLLANRFSFGPALDELEKQLENLEEEF--------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 996 leEKVEGLTTQLlDHEERAKHGVKakgrLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNn 1075
Cdd:PRK04778 182 --SQFVELTESG-DYVEAREILDQ----LEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLD- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1076 qLMKRDEELQHQLTRYDEESANVTL--MQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDE 1153
Cdd:PRK04778 254 -IEKEIQDLKEQIDENLALLEELDLdeAEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1154 ATMLQD---LMSRKDEEVNATKRAIEQIQHTME---GKIEEQKAKFS----------RQVEELHDQIEQHKKQRSQLEKQ 1217
Cdd:PRK04778 333 IDRVKQsytLNESELESVRQLEKQLESLEKQYDeitERIAEQEIAYSelqeeleeilKQLEEIEKEQEKLSEMLQGLRKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1218 QNQADQERADMAQEIALLqasradidkKRKIHEAHL----MEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEH 1293
Cdd:PRK04778 413 ELEAREKLERYRNKLHEI---------KRYLEKSNLpglpEDYLEMFFEVSDEIEALAEELEEKPINMEAVNRLLEEATE 483
|
....*...
gi 1767286957 1294 AFANMQRR 1301
Cdd:PRK04778 484 DVETLEEE 491
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
916-1318 |
1.03e-07 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 56.79 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 916 VNDMRDRLSEEEQQNEKNnderRKQMETVRDLEEQleqeeqARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLlkekrl 995
Cdd:pfam06160 102 IKQILEELDELLESEEKN----REEVEELKDKYRE------LRKTLLANRFSYGPAIDELEKQLAEIEEEFSQF------ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 996 leekvEGLTTQLlDHEERAKHGVKakgrLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNn 1075
Cdd:pfam06160 166 -----EELTESG-DYLEAREVLEK----LEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGYALEHLN- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1076 qLMKRDEELQHQLTRYDEESANVTL--MQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvldkvDE 1153
Cdd:pfam06160 235 -VDKEIQQLEEQLEENLALLENLELdeAEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAE-------EQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1154 ATMLQDLMSRKDEEVNATKRAIEQIQhtmegKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIA 1233
Cdd:pfam06160 307 NKELKEELERVQQSYTLNENELERVR-----GLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQE 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1234 LLQASRADIDKKRKiheahlmEIQANLAESDEHKRTLIDQLERSR------DELDHLNRVREEEEHAFA-------NM-- 1298
Cdd:pfam06160 382 EFKESLQSLRKDEL-------EAREKLDEFKLELREIKRLVEKSNlpglpeSYLDYFFDVSDEIEDLADelnevplNMde 454
|
410 420
....*....|....*....|.
gi 1767286957 1299 -QRRLATAEGQIQELNEQIQE 1318
Cdd:pfam06160 455 vNRLLDEAQDDVDTLYEKTEE 475
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1102-1325 |
1.71e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1102 QKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQht 1181
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1182 meGKIEEQKAKFSRQVEELHDQIEQHKKQ-------------RSQLEKQQNQADQERAD-MAQEIALLQASRADIDKKRK 1247
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEeLRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1248 iheahlmEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIA 1325
Cdd:COG4942 175 -------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
844-1250 |
1.73e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 844 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVI------QEQLQQESENSAELDDIRGRLQTRNQELEYIVN 917
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekllqlLPLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 918 DMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLE 997
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 998 EK------------------VEGLTTQLLDHEER---------------AKHGVKAKGRLENQLHELEQDLNRERQYKSE 1044
Cdd:COG4717 241 LEerlkearlllliaaallaLLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1045 LEQHKRKLLAELEDSKDHLAEKMGKVEELnNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERN 1124
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEEL-QELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1125 ARNKaemtRREVVAQLEKVKGDVLDKVDEATmlqdlmsrkDEEVNAtkrAIEQIQHTMEgKIEEQKAKFSRQVEELHDQI 1204
Cdd:COG4717 400 LKEE----LEELEEQLEELLGELEELLEALD---------EEELEE---ELEELEEELE-ELEEELEELREELAELEAEL 462
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1767286957 1205 EQHKKQR--SQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHE 1250
Cdd:COG4717 463 EQLEEDGelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1202-1459 |
3.06e-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: 54.77 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1202 DQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEhkrtlidQLERSRDEL 1281
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA-------ELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1282 DHLNRVREEEEHAFANMQRRLataegqiQELNEQIQEETRLKIANINRA-RQLEDEKNALLDEKEEAEGLRAHLEkEIHA 1360
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL-------YRLGRQPPLALLLSPEDFLDAvRRLQYLKYLAPARREQAEELRADLA-ELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1361 ARQGAGEARRKAEESVNQQLEELRKknlrdvehLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQ 1440
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAA--------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|....*....
gi 1767286957 1441 KKFESQMAEERVAVQKALL 1459
Cdd:COG4942 237 AAAAERTPAAGFAALKGKL 255
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
770-1401 |
3.21e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 55.89 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 770 LEEERDlKLTALIMNFQAQCRGFLSRRLYTRRQQQS--SAIRIIQRNGlaylKLRNWQWWRLFTKVKPLLQVTRTddeir 847
Cdd:pfam15921 262 LQQHQD-RIEQLISEHEVEITGLTEKASSARSQANSiqSQLEIIQEQA----RNQNSMYMRQLSDLESTVSQLRS----- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 848 akddELRATKErllKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDirgrlqtrnqELEYIVNDMRDR---LS 924
Cdd:pfam15921 332 ----ELREAKR---MYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD----------QLQKLLADLHKRekeLS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 925 EEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKL-LLDKTNVDQRLRNLEERLVELQDAYDKLlkekrlleEKVEGL 1003
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLeALLKAMKSECQGQMERQMAAIQGKNESL--------EKVSSL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1004 TTQLLDHEErakhgvkakgrlenQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEE 1083
Cdd:pfam15921 467 TAQLESTKE--------------MLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1084 LQHQLTRYDE---ESANVTLMQKQMRDMQTTIDELREDMETE-----RNARNKAEMTRREvvAQLEKVKGDVLDKVDEAT 1155
Cdd:pfam15921 533 LQHLKNEGDHlrnVQTECEALKLQMAEKDKVIEILRQQIENMtqlvgQHGRTAGAMQVEK--AQLEKEINDRRLELQEFK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1156 MLQDlmsRKDEEVNATKRAIEQiqhtmegkIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALL 1235
Cdd:pfam15921 611 ILKD---KKDAKIRELEARVSD--------LELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1236 qasradidKKRKIHEAHLMEIQANlaESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQ 1315
Cdd:pfam15921 680 --------KRNFRNKSEEMETTTN--KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSK 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1316 IQ--EETrlkIANINRARQ-LEDEKNALLDEKEEAEGLRAHLEKEIHAARQgagEARRKAEESVNQQLeELRKKNLRDVE 1392
Cdd:pfam15921 750 IQflEEA---MTNANKEKHfLKEEKNKLSQELSTVATEKNKMAGELEVLRS---QERRLKEKVANMEV-ALDKASLQFAE 822
|
650
....*....|..
gi 1767286957 1393 H---LQKQLEES 1401
Cdd:pfam15921 823 CqdiIQRQEQES 834
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1185-1375 |
4.79e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1185 KIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQAsraDIDKKRKIHEAHLMEIQAN----- 1259
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA---EIEERREELGERARALYRSggsvs 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1260 ----LAESDE-----HKRTLIDQL-ERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINR 1329
Cdd:COG3883 104 yldvLLGSESfsdflDRLSALSKIaDADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1767286957 1330 ARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEES 1375
Cdd:COG3883 184 LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1188-1792 |
5.29e-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: 54.73 E-value: 5.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1188 EQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQEradmaqeiallqasradIDKKRKIHEAHLMEIQANLAESDEHK 1267
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENK-----------------LQENRKIIEAQRKAIQELQFENEKVS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1268 RTLIDQLERSRDELDHLNRVREeeehaFANMQRRLATAEGQIQELNEQIQEETRLKIANINRarQLEDEKNALLDEKEEA 1347
Cdd:pfam05483 134 LKLEEEIQENKDLIKENNATRH-----LCNLLKETCARSAEKTKKYEYEREETRQVYMDLNN--NIEKMILAFEELRVQA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1348 EGLRAHLEKEIhaarqgagearrKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERIL--------QSKKKIQQEL 1419
Cdd:pfam05483 207 ENARLEMHFKL------------KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMkdltflleESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1420 EDSSMELENVRashrDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSL 1499
Cdd:pfam05483 275 EKTKLQDENLK----ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1500 QQELQDSISNKDDFGKNVHE-LEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVE-- 1576
Cdd:pfam05483 351 VTEFEATTCSLEELLRTEQQrLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEki 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1577 ------AEEKRRGLL----KQIRDLENELENEKRGKSgavSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKE 1646
Cdd:pfam05483 431 aeelkgKEQELIFLLqareKEIHDLEIQLTAIKTSEE---HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1647 YQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKgggiSSEEKRRLEAKIA 1726
Cdd:pfam05483 508 ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK----SEENARSIEYEVL 583
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1727 QLEEELEEEQSNCELAIDKQRKAQVQLEQITTDlsmERTLNQKTEAEKQSLERsnrdYKAKITELE 1792
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIENKNKNIEELHQE---NKALKKKGSAENKQLNA----YEIKVNKLE 642
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
618-673 |
5.36e-07 |
|
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: 51.58 E-value: 5.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 618 AEFAGICAAEMNETAfgmrSRKG-MFRTV-----SQLHKEQLTKLMTTLRNTSPHFVRCIIP 673
Cdd:cd01363 113 LEAFGNAKTTRNENS----SRFGkFIEILldiagFEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
844-1192 |
5.45e-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: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 844 DEIRAKDDELRATKERLLKMEHDFRENEKKLDQvivERAVIQEQLQQESENSAELDDIRgrLQTRNQELEYIvndmrdRL 923
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDR---QAAIYAEQERMAMERERELERIR--QEERKRELERI------RQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 924 SEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKtnvdQRLRNLEERLVELQDAydkllkekRLLEEKVEGL 1003
Cdd:pfam17380 368 EEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQI--------RAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1004 TTQLLDhEERAKHGVKAKgrlenqLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEkmgkveELNNQLMkrDEE 1083
Cdd:pfam17380 436 EVRRLE-EERAREMERVR------LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE------EQRRKIL--EKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1084 LQHQLTRYDEESANVTLMQKQMRDMQTTIDELREdmeternaRNKAEMTRREVVaqlekvkgdvldKVDEATMLQDLMsR 1163
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--------RREAEEERRKQQ------------EMEERRRIQEQM-R 559
|
330 340
....*....|....*....|....*....
gi 1767286957 1164 KDEEVNATKRAIEQIQHTMEGKIEEQKAK 1192
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
968-1174 |
6.33e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 6.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 968 VDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSEL-- 1045
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1046 ------EQHKRKLLAELEDSKDhLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDM 1119
Cdd:COG4942 112 alyrlgRQPPLALLLSPEDFLD-AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1120 ETERNARNKaemTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRA 1174
Cdd:COG4942 191 EALKAERQK---LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1394-1911 |
6.65e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1394 LQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAE----------ERVAVQKALLDRDA 1463
Cdd:TIGR04523 129 LEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNiqknidkiknKLLKLELLLSNLKK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1464 MSQELRDRETRVLSLLNEVDIMKEHLEES-----------DRVRRSLQQELQDSISNKDDFGKNVHELEKAKR---SLEA 1529
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKqqeinektteiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKkikELEK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1530 ELNDMRVQMEELEDNLQiaedarlrlEVTNQALKSESDRaISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHR 1609
Cdd:TIGR04523 289 QLNQLKSEISDLNNQKE---------QDWNKELKSELKN-QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1610 KKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGL 1689
Cdd:TIGR04523 359 SEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1690 MQARKQLElendeleelrakgggissEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQK 1769
Cdd:TIGR04523 439 NSEIKDLT------------------NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1770 TEAEKQSLERSNRDYKAKITELESgAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAAN--RAARRLEKRLNDTTQQFED 1847
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKE-KIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKS 579
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1767286957 1848 EKRANEQAKELLEKSNLKNRNLRRQLDEAEdemsrerTKHRNVQREADDLLDANEQLTRELMNL 1911
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKE-------KKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1055-1281 |
8.98e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1055 ELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMEternaRNKAEMTRR 1134
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE-----ERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1135 EVVAQLEKVKGDVLDKVDEATMLQDLMSRkdeeVNATKRAIEQIQhtmegkieeqkakfsrqveelhDQIEQHKKQRSQL 1214
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSESFSDFLDR----LSALSKIADADA----------------------DLLEELKADKAEL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1767286957 1215 EKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDEL 1281
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1032-1340 |
1.29e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.49 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1032 EQDLNRERQYKSELEQHKRKLLA----ELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTR-YDEESANVTLMQKQMR 1106
Cdd:pfam05667 196 AQPSSRASVVPSLLERNAAELAAaqewEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSaALAGTEATSGASRSAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1107 DMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKI 1186
Cdd:pfam05667 276 DLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQ-EL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1187 EEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQadqeradMAQEIALLQASRADIDKKRKIHEAhLMEIQANLA-ESDE 1265
Cdd:pfam05667 355 EKEIKKLESSIKQVEEELEELKEQNEELEKQYKV-------KKKTLDLLPDAEENIAKLQALVDA-SAQRLVELAgQWEK 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1266 HKRTLIDQLERSRDELDHlnrvREEEEhafanmQRRLAtaegQIQELNEQIQ---EETRLKIANInraRQLEDEKNAL 1340
Cdd:pfam05667 427 HRVPLIEEYRALKEAKSN----KEDES------QRKLE----EIKELREKIKevaEEAKQKEELY---KQLVAEYERL 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1019-1296 |
1.48e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1019 KAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLmkrdeelqhqltrydeesanv 1098
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1099 TLMQKQMRDMQTTIDELREDMEternaRNKAEMTRREVVAQlekvkgdvldKVDEATMLQDLMSRKDeeVNATKRAIEQI 1178
Cdd:COG4942 79 AALEAELAELEKEIAELRAELE-----AQKEELAELLRALY----------RLGRQPPLALLLSPED--FLDAVRRLQYL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1179 QHTMEgkieeqkakfsrqveELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQA 1258
Cdd:COG4942 142 KYLAP---------------ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEK 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 1767286957 1259 NLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFA 1296
Cdd:COG4942 207 ELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1130-1552 |
1.60e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.98 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1130 EMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKA---KFSRQVEELHDQIEQ 1206
Cdd:pfam07888 5 ELVTLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRdreQWERQRRELESRVAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1207 HKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNR 1286
Cdd:pfam07888 85 LKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1287 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEkeihAARQGAG 1366
Cdd:pfam07888 165 QRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE----ALLEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1367 EARRKAEESvnQQLEELRKKNLRDVEHLQKQlEESEVAKERILQSKKKIQqeLEDSSMELENVRAshRDSEKRQKKFES- 1445
Cdd:pfam07888 241 SLQERLNAS--ERKVEGLGEELSSMAAQRDR-TQAELHQARLQAAQLTLQ--LADASLALREGRA--RWAQERETLQQSa 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1446 QMAEERVAVQKA-LLDRDAMSQELR-DRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnkddfgknvhELEKA 1523
Cdd:pfam07888 314 EADKDRIEKLSAeLQRLEERLQEERmEREKLEVELGREKDCNRVQLSESRRELQELKASLR--------------VAQKE 379
|
410 420
....*....|....*....|....*....
gi 1767286957 1524 KRSLEAELNDMRVQMEELEDNLQIAEDAR 1552
Cdd:pfam07888 380 KEQLQAEKQELLEYIRQLEQRLETVADAK 408
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
863-1267 |
1.84e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 863 MEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQME 942
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 943 ----------TVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEE 1012
Cdd:pfam05483 441 lifllqarekEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1013 RAKHGVKAKGRLENQLHELEQdlnRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYD 1092
Cdd:pfam05483 521 DIINCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1093 EESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVK---GDVLD---------KVDEATMLQDL 1160
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKqkfEEIIDnyqkeiedkKISEEKLLEEV 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1161 MSRK---DEEVNATKRAIEQIQHT---MEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIAL 1234
Cdd:pfam05483 678 EKAKaiaDEAVKLQKEIDKRCQHKiaeMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLS 757
|
410 420 430
....*....|....*....|....*....|...
gi 1767286957 1235 LQaSRADIDKKRKihEAHLMEIQANLAESDEHK 1267
Cdd:pfam05483 758 LK-KQLEIEKEEK--EKLKMEAKENTAILKDKK 787
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
970-1408 |
2.10e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 970 QRLRNLEERLVELQD---AYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrlenQLHELEQDLNRERQYKSELE 1046
Cdd:COG4717 71 KELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1047 QHKRKLLAELEDskdhLAEKMGKVEELNNQLMKRDEELQHQLTRYDEEsanvtlMQKQMRDMQTTIDELREDMETERNAR 1126
Cdd:COG4717 146 ERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLA------TEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1127 NKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKdeeVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQ 1206
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1207 HKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAEsdehkrtlIDQLERSRDELDHLNR 1286
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEE--------LQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1287 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKianiNRARQLEDEKNALLDEKEEAegLRAHLEKEIHAARQGAG 1366
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELK----EELEELEEQLEELLGELEEL--LEALDEEELEEELEELE 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1767286957 1367 EARRKAEESVNQQLEELRK-----KNLRDVEHLQKQLEESEVAKERI 1408
Cdd:COG4717 439 EELEELEEELEELREELAEleaelEQLEEDGELAELLQELEELKAEL 485
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1347-1861 |
2.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1347 AEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKnLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1426
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEE-LKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1427 ENVRA--SHRDSEKRQKKFESQMAEERVAVQKALLDRdamsQELRDRETRVLSLLNEVDIMKEHLEES-DRVRRSLQQEL 1503
Cdd:COG4717 119 EKLEKllQLLPLYQELEALEAELAELPERLEELEERL----EELRELEEELEELEAELAELQEELEELlEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1504 QDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARlRLEVTNQALKSESDRAISNKDVEAEEKRRG 1583
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLLLLIAAALLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1584 LLKQIRDLENELenekrgKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLkknQQIIKEYQIECEEARQAKEDIAA 1663
Cdd:COG4717 274 TIAGVLFLVLGL------LALLFLLLAREKASLGKEAEELQALPALEELEEEEL---EELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1664 LLREADRKFRAVEAEREQLREanEGLMQARKQLELEndeleelrakgGGISSEEKRRLEAKIAQLEEELEEEQSNCELAI 1743
Cdd:COG4717 345 RIEELQELLREAEELEEELQL--EELEQEIAALLAE-----------AGVEDEEELRAALEQAEEYQELKEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1744 DKQRKAQVQLEQITTDLSMERTLNQkTEAEKQSLERSNRDYKAKITELESG-AQSRARAQMAALEAKVQYLEDQLNvEGQ 1822
Cdd:COG4717 412 EELLGELEELLEALDEEELEEELEE-LEEELEELEEELEELREELAELEAElEQLEEDGELAELLQELEELKAELR-ELA 489
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1767286957 1823 EKTAANRAARRLekrLNDTTQQFEDEKRA--NEQAKELLEK 1861
Cdd:COG4717 490 EEWAALKLALEL---LEEAREEYREERLPpvLERASEYFSR 527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1365-1684 |
2.69e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1365 AGEARRKAEESVNQQLEELRKKNLRDVEH-----LQKQLEESEvAKERILQskkkiqQELEDSSMELENVRASHRDSEK- 1438
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQyrlveMARELEELS-ARESDLE------QDYQAASDHLNLVQTALRQQEKi 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1439 --RQKKFESqmAEERVAVQKALldRDAMSQELRDRETRVLSLLNEVDIMKEHLEEsdrvrrsLQQELQDSISNKDDFGKN 1516
Cdd:COG3096 350 erYQEDLEE--LTERLEEQEEV--VEEAAEQLAEAEARLEAAEEEVDSLKSQLAD-------YQQALDVQQTRAIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1517 VHELEKAKR----------SLEAELNDMRVQME-------ELEDNLQIAEDARLRLEVTNQALKS---ESDRAisnkdvE 1576
Cdd:COG3096 419 VQALEKARAlcglpdltpeNAEDYLAAFRAKEQqateevlELEQKLSVADAARRQFEKAYELVCKiagEVERS------Q 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1577 AEEKRRGLLKQIRDLENELENEKrgksgavshrkKIENQIGELEQQLEV---ANRLKEEYNKQLKKNQQIIKEYQIECEE 1653
Cdd:COG3096 493 AWQTARELLRRYRSQQALAQRLQ-----------QLRAQLAELEQRLRQqqnAERLLEEFCQRIGQQLDAAEELEELLAE 561
|
330 340 350
....*....|....*....|....*....|.
gi 1767286957 1654 ARQAKEDIAALLREADRKFRAVEAEREQLRE 1684
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
962-1505 |
3.64e-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: 52.06 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 962 LLDKTNVDQRLRnLEERLVELqdayDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRlenqlhELEQDLNRERQY 1041
Cdd:pfam07111 84 LLRETSLQQKMR-LEAQAMEL----DALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQR------ELEEIQRLHQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1042 KSELEQHKRKLLAELEDSKDHL--------AEKMGKVEELNnQLMKRDEELQHQLTRYDEE-SANVTLMQKQMRdmqtti 1112
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLekslnsleTKRAGEAKQLA-EAQKEAELLRKQLSKTQEElEAQVTLVESLRK------ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1113 dELREDMETERNaRNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQ-------DLMSRKDEEVNATKRAIEQIQHTMEGK 1185
Cdd:pfam07111 226 -YVGEQVPPEVH-SQTWELERQELLDTMQHLQEDRADLQATVELLQvrvqsltHMLALQEEELTRKIQPSDSLEPEFPKK 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1186 IEEQKAKFSRQVEELHDQIE----QHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLA 1261
Cdd:pfam07111 304 CRSLLNRWREKVFALMVQLKaqdlEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELS 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1262 ESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETR------------LKIANIN- 1328
Cdd:pfam07111 384 RAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRkvhtikglmarkVALAQLRq 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1329 ------------------RARQLEDEKNALLDEKEeaegLRAHL-EKEIHAARQgAGEARRKAEESVNQQLEELRKKNLR 1389
Cdd:pfam07111 464 escpppppappvdadlslELEQLREERNRLDAELQ----LSAHLiQQEVGRARE-QGEAERQQLSEVAQQLEQELQRAQE 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1390 DVEHLQKQL-----------EESEVAKERILQSKKKIQQELEDSSMELEN-VRASHRDSEKRQKKFESQMAEERVAVQKa 1457
Cdd:pfam07111 539 SLASVGQQLevarqgqqestEEAASLRQELTQQQEIYGQALQEKVAEVETrLREQLSDTKRRLNEARREQAKAVVSLRQ- 617
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1767286957 1458 lLDRDAMSQELRDRETRVLSllnevdiMKEHLEESDRVRRSLQQELQD 1505
Cdd:pfam07111 618 -IQHRATQEKERNQELRRLQ-------DEARKEEGQRLARRVQELERD 657
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
972-1368 |
3.68e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.26 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 972 LRNLEERLVELQDAydkLLKEKRLLEEKvegltTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELE---QH 1048
Cdd:COG3096 274 MRHANERRELSERA---LELRRELFGAR-----RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQtalRQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1049 KRKL---LAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEesanvtlMQKQMRDMQTTIDEL-------RED 1118
Cdd:COG3096 346 QEKIeryQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS-------LKSQLADYQQALDVQqtraiqyQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1119 METERNARN----------KAEMTRREVVAQLEKVKGDVLDkvdeatmLQDLMSRKDEEVNATKRAIEQIQhTMEGKIEE 1188
Cdd:COG3096 419 VQALEKARAlcglpdltpeNAEDYLAAFRAKEQQATEEVLE-------LEQKLSVADAARRQFEKAYELVC-KIAGEVER 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1189 QKAkFSRQVEELHD------------QIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIdkkrkihEAHLMEI 1256
Cdd:COG3096 491 SQA-WQTARELLRRyrsqqalaqrlqQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL-------EELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1257 QANLAESDEHKRTLIDQLERSRDELDHLNRVREEeehafanmQRRLATAEGQIQELNEQIQEETRLKIANIN-----RAR 1331
Cdd:COG3096 563 EAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE--------LAARAPAWLAAQDALERLREQSGEALADSQevtaaMQQ 634
|
410 420 430
....*....|....*....|....*....|....*..
gi 1767286957 1332 QLEDEKNALLdEKEEAEGLRAHLEKEIHAARQGAGEA 1368
Cdd:COG3096 635 LLEREREATV-ERDELAARKQALESQIERLSQPGGAE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
848-1057 |
4.24e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 848 AKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQeseNSAELDDIRGRLQTRNQELEYIVNDMRdRLSEEE 927
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA---LERRIAALARRIRALEQELAALEAELA-ELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 928 QQNEKNNDERRKQMETVrdLEEQLEQEEQARQKLLLDKTNVDQRLRNLE----------ERLVELQDAYDKLLKEKRLLE 997
Cdd:COG4942 93 AELRAELEAQKEELAEL--LRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 998 EKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELE 1057
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1231-1689 |
4.74e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.67 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1231 EIALLQASRadiDKKRKIHEaHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLataegqiq 1310
Cdd:pfam05557 8 KARLSQLQN---EKKQMELE-HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1311 elneqiqEETRLKIANINRARQLEDEKNALLdekEEAEGLRAHLEKEIHAARQGAG------EARRKAEESVNQQLEELR 1384
Cdd:pfam05557 76 -------ELNRLKKKYLEALNKKLNEKESQL---ADAREVISCLKNELSELRRQIQraelelQSTNSELEELQERLDLLK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1385 KK--NLRDV-EHLQKQLEESEVAKERILQSKKKIQQElEDSSMELENVR---ASHRDSEKRQKKFESQMA---------- 1448
Cdd:pfam05557 146 AKasEAEQLrQNLEKQQSSLAEAEQRIKELEFEIQSQ-EQDSEIVKNSKselARIPELEKELERLREHNKhlnenienkl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1449 --EERVAVQKALLDRDAMSQE----LRDRETRVLSLLNE-VDIMKEH---LEESDRVRRSLQQELQDSISNKD---DFGK 1515
Cdd:pfam05557 225 llKEEVEDLKRKLEREEKYREeaatLELEKEKLEQELQSwVKLAQDTglnLRSPEDLSRRIEQLQQREIVLKEensSLTS 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1516 NVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESD--RAI---SNKDVEAEEKRRGLLKQIRD 1590
Cdd:pfam05557 305 SARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDgyRAIlesYDKELTMSNYSPQLLERIEE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1591 LENELEnekrgksgavshrkKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIK--EYQIECEEARQAKEDIAALLREA 1668
Cdd:pfam05557 385 AEDMTQ--------------KMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQalRQQESLADPSYSKEEVDSLRRKL 450
|
490 500
....*....|....*....|.
gi 1767286957 1669 DRkfraVEAEREQLREANEGL 1689
Cdd:pfam05557 451 ET----LELERQRLREQKNEL 467
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1082-1422 |
5.75e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 51.59 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1082 EELQHQLTRYDEESANvtlmQKQMRDMQTTID-------ELREDMETERN--ARNKAEMTRREVVAQLEKVKGDVLDKV- 1151
Cdd:PRK10929 48 EALQSALNWLEERKGS----LERAKQYQQVIDnfpklsaELRQQLNNERDepRSVPPNMSTDALEQEILQVSSQLLEKSr 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1152 ------DEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGK-----IEEQKAKFSRQVEELhdqieQHKKQRSQLEKQQNQ 1220
Cdd:PRK10929 124 qaqqeqDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLgtpntPLAQAQLTALQAESA-----ALKALVDELELAQLS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1221 AD--QERADMAQEI---------ALLQASRADIDKKRKiHEAHL-MEIQANLAE-SDEHKRTLIDQLERSRDELDHLNRv 1287
Cdd:PRK10929 199 ANnrQELARLRSELakkrsqqldAYLQALRNQLNSQRQ-REAERaLESTELLAEqSGDLPKSIVAQFKINRELSQALNQ- 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1288 reeeehafaNMQRRLATAEGQIQELNEQIQeeTRLKIANINRARQLEDEKNALldekeeAEGLRAHLEkeihaarqgage 1367
Cdd:PRK10929 277 ---------QAQRMDLIASQQRQAASQTLQ--VRQALNTLREQSQWLGVSNAL------GEALRAQVA------------ 327
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767286957 1368 arRKAEESVNQQLE----ELRKKNLRDVEHLQKQLEESEV----------AKERILQSKKKIQQELEDS 1422
Cdd:PRK10929 328 --RLPEMPKPQQLDtemaQLRVQRLRYEDLLNKQPQLRQIrqadgqpltaEQNRILDAQLRTQRELLNS 394
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
850-1277 |
1.02e-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: 50.82 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 850 DDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESEnsaELDDIRGRLQTRNQELEYIVNDmrdrLSEEEQQ 929
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEK---EIPELRNKLQKVNRDIQRLKND----IEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 930 NEKNNDERRKQMETVRD--------LEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKE----KRLLE 997
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTDvtimerfqMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 998 EKVEGL------TTQLLDHEERAKHGVKAKGRLENQLHELE---QDLNRE----RQYKSELEQHKRKLLAELEDSKdHLA 1064
Cdd:TIGR00606 854 DQQEQIqhlkskTNELKSEKLQIGTNLQRRQQFEEQLVELStevQSLIREikdaKEQDSPLETFLEKDQQEKEELI-SSK 932
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1065 EKMGKVEELNNQLMKRDEELQH----QLTRYDEESANVTLMQK---------QMRDMQTTIDELREDMETERNARNKAEM 1131
Cdd:TIGR00606 933 ETSNKKAQDKVNDIKEKVKNIHgymkDIENKIQDGKDDYLKQKetelntvnaQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1132 TRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQR 1211
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID-LIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1212 SqlEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQanlAESDEHKRTLIDQLERS 1277
Cdd:TIGR00606 1092 R--EPQFRDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAIMKFH---SMKMEEINKIIRDLWRS 1152
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1463-1710 |
1.32e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1463 AMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELE 1542
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1543 DNLQIAEDARLRLEVTNQALKSESDRAI--SNKDVEAEEKRRGLLKQIRDLENELENEkrgksgavshrkkIENQIGELE 1620
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPARREQAEE-------------LRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1621 QQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEN 1700
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|
gi 1767286957 1701 DELEELRAKG 1710
Cdd:COG4942 244 PAAGFAALKG 253
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
923-1427 |
1.44e-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: 50.12 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 923 LSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDktnvdqRLRNLEERLVELQDAYDKLLKEKRLLEEKVEG 1002
Cdd:pfam05557 14 LQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQK------RIRLLEKREAEAEEALREQAELNRLKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1003 LTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDE 1082
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1083 ------ELQHQLTRYDEESANVTLMQK---QMRDMQTTIDELREDMETERNARNKAEMTRREVvAQLEKVKGDVLDKVDE 1153
Cdd:pfam05557 168 aeqrikELEFEIQSQEQDSEIVKNSKSelaRIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYREE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1154 ATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEeqkakFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIA 1233
Cdd:pfam05557 247 AATLELEKEKLEQELQSWVKLAQDTGLNLRSPED-----LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1234 LLQASRADIDKKRKIHEAHLMEIQ--------------ANLAESD------EHKRTLIDQLERSRDELDHLNRVREEEEH 1293
Cdd:pfam05557 322 QYLKKIEDLNKKLKRHKALVRRLQrrvllltkerdgyrAILESYDkeltmsNYSPQLLERIEEAEDMTQKMQAHNEEMEA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1294 AFANMQR-------RLATAEGQIQELNEQIQ-----------EETRLKIANINRARQ-LEDEKNALLDEKEEAEgLRAHL 1354
Cdd:pfam05557 402 QLSVAEEelggykqQAQTLERELQALRQQESladpsyskeevDSLRRKLETLELERQrLREQKNELEMELERRC-LQGDY 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1355 EKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELE 1427
Cdd:pfam05557 481 DPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
872-1666 |
1.58e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.34 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 872 KKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQ------------QNEKNNDERRK 939
Cdd:PRK04863 348 EKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQaldvqqtraiqyQQAVQALERAK 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 940 QMETVRDLEEQLEQEEQARQKLLLDKtnVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLT--------TQLLDHE 1011
Cdd:PRK04863 428 QLCGLPDLTADNAEDWLEEFQAKEQE--ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawdvaRELLRRL 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1012 ERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDhlaekmgkVEELNNQLMKRDEELQHQLTRY 1091
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE--------LEQLQEELEARLESLSESVSEA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1092 DEESanvTLMQKQMRDMQTTIDELRedmeternARNKAEMTRREVVAQLEKVKGdvlDKVDEATMLQDLMSRKDEEVNAT 1171
Cdd:PRK04863 578 RERR---MALRQQLEQLQARIQRLA--------ARAPAWLAAQDALARLREQSG---EEFEDSQDVTEYMQQLLEREREL 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1172 KRAIEQiqhtmegkIEEQKAKFSRQVEELHdqieqhkkQR--SQLEKQQNQADQERADMAQEI-------------ALLQ 1236
Cdd:PRK04863 644 TVERDE--------LAARKQALDEEIERLS--------QPggSEDPRLNALAERFGGVLLSEIyddvsledapyfsALYG 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1237 ASRADI------DKKRK------------IHEAHLMEIQANLAESDEHKRTLIDQL-----------------ERSRDE- 1280
Cdd:PRK04863 708 PARHAIvvpdlsDAAEQlagledcpedlyLIEGDPDSFDDSVFSVEELEKAVVVKIadrqwrysrfpevplfgRAAREKr 787
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1281 LDHLNRVREEEehafanmQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEknallDEKEEAEGLRAHLEKEIHA 1360
Cdd:PRK04863 788 IEQLRAEREEL-------AERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPE-----AELRQLNRRRVELERALAD 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1361 ARQGAGEARRKAEESVN--QQLEELRKK-NLRDVEHLQKQLEESEVAKERILQSKKKIQQElEDSSMELENVRASHRDSe 1437
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEglSALNRLLPRlNLLADETLADRVEEIREQLDEAEEAKRFVQQH-GNALAQLEPIVSVLQSD- 933
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1438 krqkkfESQMAEERVAVQKALLDRDAMSQELRDretrvlslLNEVDIMKEHLEESDRVRR-SLQQELQDSISNKddfgkn 1516
Cdd:PRK04863 934 ------PEQFEQLKQDYQQAQQTQRDAKQQAFA--------LTEVVQRRAHFSYEDAAEMlAKNSDLNEKLRQR------ 993
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1517 vheLEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKsESDRAISNKDVEAEEkrrGLLKQIRDLENELE 1596
Cdd:PRK04863 994 ---LEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQ-ELKQELQDLGVPADS---GAEERARARRDELH 1066
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1597 NEKRgksgavSHRKKIEnqigELEQQLEVANRLKEEYNKQLKKNQqiiKEYQIECEEARQAKEDIAALLR 1666
Cdd:PRK04863 1067 ARLS------ANRSRRN----QLEKQLTFCEAEMDNLTKKLRKLE---RDYHEMREQVVNAKAGWCAVLR 1123
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1360-1585 |
1.68e-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: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1360 AARQGAGEARRKAEESVNQQLEELRK---KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDS 1436
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKelaALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1437 EKRQKKFESQMAEERVAVQKA--------LLDRDAMSQELRDRE---TRVLSLLNEVDIMKEHLEESDRVRRSLQQELQD 1505
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplalLLSPEDFLDAVRRLQylkYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1506 SISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLL 1585
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1344-1572 |
1.77e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.22 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 KEEAEGLRAHLEKEihAARQGAGEARRKAEESvNQQLEELRKKNLRDVEHLQKQLEES---------EVAKERILQSKKK 1414
Cdd:NF012221 1541 SQQADAVSKHAKQD--DAAQNALADKERAEAD-RQRLEQEKQQQLAAISGSQSQLESTdqnaletngQAQRDAILEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1415 IQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVA-VQKALLDRDAMSQE-LRDRETRVLSLLNEVdimKEHLEES 1492
Cdd:NF012221 1618 VTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGGLLDrVQEQLDDAKKISGKqLADAKQRHVDNQQKV---KDAVAKS 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1493 DR-VRRS--LQQELQDSISNKddfgknvhELEKAKRSLEAELNDMRVQMEELEDNLqIAEDARLRLEVTNQALKSESDRA 1569
Cdd:NF012221 1695 EAgVAQGeqNQANAEQDIDDA--------KADAEKRKDDALAKQNEAQQAESDANA-AANDAQSRGEQDASAAENKANQA 1765
|
...
gi 1767286957 1570 ISN 1572
Cdd:NF012221 1766 QAD 1768
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1186-1430 |
1.78e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1186 IEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQER--ADMAQEIALLQASRADIDKKrkiheahLMEIQANLAES 1263
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNglVDLSEEAKLLLQQLSELESQ-------LAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1264 DEHKRTLIDQLERSRDELDHLNrvreeEEHAFANMQRRLATAEGQIQELNEQIQEETRlkianinRARQLEDEKNALLDE 1343
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELL-----QSPVIQQLRAQLAELEAELAELSARYTPNHP-------DVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 -KEEAEGLRAHLEKEIHAARQgagearrkAEESVNQQLEELRKKNLRDVEHLQKQLE---ESEVAKERILQSKKKIQQEL 1419
Cdd:COG3206 307 lQQEAQRILASLEAELEALQA--------REASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEAR 378
|
250
....*....|.
gi 1767286957 1420 EDSSMELENVR 1430
Cdd:COG3206 379 LAEALTVGNVR 389
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1472-1715 |
1.83e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1472 ETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLqiaeDA 1551
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----GE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1552 RLRLEVTNQALKSESDRAISNKDVEA-----------EEKRRGLLKQIRDLENELENEKrgksgavshrKKIENQIGELE 1620
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSESFSDfldrlsalskiADADADLLEELKADKAELEAKK----------AELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1621 QQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELEN 1700
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
250
....*....|....*
gi 1767286957 1701 DELEELRAKGGGISS 1715
Cdd:COG3883 241 AAAASAAGAGAAGAA 255
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
885-1219 |
2.17e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.52 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 885 QEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQAR-----Q 959
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQQTNskdgeQ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 960 KLLLDKTNVDQRLRNLEE--------RLVELQDAyDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGR-------L 1024
Cdd:PLN02939 125 LSDFQLEDLVGMIQNAEKnilllnqaRLQALEDL-EKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHveileeqL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1025 ENQLHELEQDLNRERQYKSELEQHKRKLLAE---LEDSKDHLAEKMGKVEELNNQLMKRDEELqhqltrydeesanvTLM 1101
Cdd:PLN02939 204 EKLRNELLIRGATEGLCVHSLSKELDVLKEEnmlLKDDIQFLKAELIEVAETEERVFKLEKER--------------SLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1102 QKQMRDMQTTIDELREDMETERNARNKAEMtrrEVVAQLEKVKGDVLDKVDEATML----QDLMSRKD------EEVNAT 1171
Cdd:PLN02939 270 DASLRELESKFIVAQEDVSKLSPLQYDCWW---EKVENLQDLLDRATNQVEKAALVldqnQDLRDKVDkleaslKEANVS 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1767286957 1172 KRAIEQIQhTMEGKIEEQKAKFSRQVEELHDQIEQHkkQRSQLEKQQN 1219
Cdd:PLN02939 347 KFSSYKVE-LLQQKLKLLEERLQASDHEIHSYIQLY--QESIKEFQDT 391
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
857-1282 |
2.71e-05 |
|
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: 49.25 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 857 KERLLKMEHDFRENEKKLDQVIVERAVIQEQL---QQESE-NSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEK 932
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEqNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 933 NNDERRKQMET-VRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHE 1011
Cdd:TIGR04523 318 NQEKKLEEIQNqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1012 ERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRY 1091
Cdd:TIGR04523 398 SKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1092 DEESANVTLMQKQMRDMQTTIDELREdmeternarNKAEMtrREVVAQLEKVKGDVLDKVDEatmLQDLMSRKDEEVNAT 1171
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKELKKLNE---------EKKEL--EEKVKDLTKKISSLKEKIEK---LESEKKEKESKISDL 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1172 KRAIEQIQHTME-GKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHE 1250
Cdd:TIGR04523 544 EDELNKDDFELKkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
410 420 430
....*....|....*....|....*....|..
gi 1767286957 1251 AHLMEIQANLAESDEHKRTLIDQLERSRDELD 1282
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1466-1884 |
2.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1466 QELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNL 1545
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELE-----KLEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1546 QI---AEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQ 1622
Cdd:COG4717 156 EElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENE 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1623 LEVANRlkeeyNKQLKKNQQIIK---------EYQIECEEARQAKEDIAALL----------READRKFRAVEAEREQLR 1683
Cdd:COG4717 236 LEAAAL-----EERLKEARLLLLiaaallallGLGGSLLSLILTIAGVLFLVlgllallfllLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1684 EANEGLMQAR----KQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTD 1759
Cdd:COG4717 311 PALEELEEEEleelLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1760 LSMERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEK--R 1837
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1767286957 1838 LNDTTQQFEDEKRANEQakelLEKSNLKNRNLRRQLDEAEDEMSRER 1884
Cdd:COG4717 471 LAELLQELEELKAELRE----LAEEWAALKLALELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
838-1024 |
2.83e-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: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAEL------------------- 898
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplalllsp 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 899 DDIrGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEER 978
Cdd:COG4942 129 EDF-LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1767286957 979 LVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHG--VKAKGRL 1024
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAgfAALKGKL 255
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1196-1387 |
3.00e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1196 QVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQAnlaesdehkrtlidQLE 1275
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA--------------RIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1276 RSRDELDHLNRVREEE--EHAFANMQRRLATAEGQIQELNEQIqEETRLKIANINraRQLEDEKNALLDEKEEAEGLRAH 1353
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalQKEIESLKRRISDLEDEILELMERI-EELEEELAELE--AELAELEAELEEKKAELDEELAE 153
|
170 180 190
....*....|....*....|....*....|....
gi 1767286957 1354 LEKEIHAARQGAGEARRKAEESVNQQLEELRKKN 1387
Cdd:COG1579 154 LEAELEELEAEREELAAKIPPELLALYERIRKRK 187
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1406-1915 |
3.00e-05 |
|
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: 49.25 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1406 ERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMaEERVAVQKALLDRDAMSQELRDRETRVLSLLN-EVDI 1484
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKI-KILEQQIKDLNDKLKKNKDKINKLNSDLSKINsEIKN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1485 MKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKS 1564
Cdd:TIGR04523 115 DKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1565 EsdRAISNKD----VEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKN 1640
Cdd:TIGR04523 195 K--LLKLELLlsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1641 QQIIkeyqieceearqakEDIAALLREADRKFRAVEAEREQLR-EANEGLMQARKQLELENDeleelrakgggissEEKR 1719
Cdd:TIGR04523 273 QKEL--------------EQNNKKIKELEKQLNQLKSEISDLNnQKEQDWNKELKSELKNQE--------------KKLE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1720 RLEAKIAQLEEELeeeqSNCELAIDKQRKAQVQLEqiTTDLSMERTLNQKtEAEKQSLERSNRDYKAKITELESGAQSrA 1799
Cdd:TIGR04523 325 EIQNQISQNNKII----SQLNEQISQLKKELTNSE--SENSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQIND-L 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1800 RAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDE 1879
Cdd:TIGR04523 397 ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
|
490 500 510
....*....|....*....|....*....|....*.
gi 1767286957 1880 MSRERTKHRNVQREADDLLDANEQLTRELMNLRGNN 1915
Cdd:TIGR04523 477 INKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1053-1542 |
4.39e-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: 48.53 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1053 LAELEDSKDHLAEK-------MGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNA 1125
Cdd:pfam05622 2 LSEAQEEKDELAQRcheldqqVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1126 RNKAEMTrrevVAQLEKVKGDVLDKVDEATMLQdlmsrkdEEVNATKRAIEQIQHTME--GKIEEQKAKFSRQVEELHDQ 1203
Cdd:pfam05622 82 RDDYRIK----CEELEKEVLELQHRNEELTSLA-------EEAQALKDEMDILRESSDkvKKLEATVETYKKKLEDLGDL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1204 ieqhKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDK-KRKIHEAHLM----------------EIQANLAESDEH 1266
Cdd:pfam05622 151 ----RRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETyKRQVQELHGKlseeskkadklefeykKLEEKLEALQKE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1267 KRTLI---DQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNalldE 1343
Cdd:pfam05622 227 KERLIierDTLRETNEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGS----Y 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 KEEAEGLRAHLEkEIHAARQGAGEARRKAeesvNQQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDsS 1423
Cdd:pfam05622 303 RERLTELQQLLE-DANRRKNELETQNRLA----NQRILELQQQ----VEELQKALQEQGSKAEDSSLLKQKLEEHLEK-L 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1424 MELENVRASHRDS-EKRQKKFESQMAEERVAVQKALLDRDamsQELRDRETRvlsllnevdiMKEHLEESDRVRRSLQQE 1502
Cdd:pfam05622 373 HEAQSELQKKKEQiEELEPKQDSNLAQKIDELQEALRKKD---EDMKAMEER----------YKKYVEKAKSVIKTLDPK 439
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1767286957 1503 LQDSISNKDDFGKN-VHELEKAKRSLEAELNDMRVQMEELE 1542
Cdd:pfam05622 440 QNPASPPEIQALKNqLLEKDKKIEHLERDFEKSKLQREQEE 480
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1523-1692 |
5.82e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1523 AKRSLEAELNDMRVQMEelednlQIAEDARLRLEVT-----------NQALKSESDRAISNKDVEAEEKRRGLLKQIRDL 1591
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAK------RILEEAKKEAEAIkkealleakeeIHKLRNEFEKELRERRNELQKLEKRLLQKEENL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1592 ENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKeyqiecEEARQ---------AKEDIA 1662
Cdd:PRK12704 99 DRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA------EEAKEillekveeeARHEAA 172
|
170 180 190
....*....|....*....|....*....|
gi 1767286957 1663 ALLREADRkfravEAEREQLREANEGLMQA 1692
Cdd:PRK12704 173 VLIKEIEE-----EAKEEADKKAKEILAQA 197
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
872-1298 |
7.36e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 872 KKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKnnDERRKQMETVRDLEEQL 951
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 952 EQEEQARQKLLLDKTNVDQRLRNLEERLVELQDaYDKLLKEKRL--LEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLH 1029
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLE-QLSLATEEELqdLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1030 ELEQDLNRERQYKsELEQHKRKLLA-------------------------------------ELEDSKDHLAEKMGKVEE 1072
Cdd:COG4717 231 QLENELEAAALEE-RLKEARLLLLIaaallallglggsllsliltiagvlflvlgllallflLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1073 LNNQLMKRDEELQHQLTRYD-EESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvldkv 1151
Cdd:COG4717 310 LPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE------- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1152 DEATMLQDLMsrKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQV-EELHDQIEQHKKQRSQLEKQQNQADQERADMAQ 1230
Cdd:COG4717 383 DEEELRAALE--QAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELREELAELEA 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1231 EIALLQASRAdIDKKRKIHEAHLMEIQaNLAESDEHKRTLIDQLERSRDEL--DHLNRVREEEEHAFANM 1298
Cdd:COG4717 461 ELEQLEEDGE-LAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYreERLPPVLERASEYFSRL 528
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1038-1845 |
7.63e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1038 ERQYKSELEQHKRKLLAELEDSKDHLAekMGKVEELNNQLMKRDEELQHQL---------TRYDEESANVTLMQKQMRDM 1108
Cdd:TIGR01612 961 EKSYKDKFDNTLIDKINELDKAFKDAS--LNDYEAKNNELIKYFNDLKANLgknkenmlyHQFDEKEKATNDIEQKIEDA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1109 QTTIDELreDMETERNARNKAEMTRREVVAQLEKVKGDVLDKV-------------------------------DEATML 1157
Cdd:TIGR01612 1039 NKNIPNI--EIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAeinitnfneikeklkhynfddfgkeenikyaDEINKI 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1158 QDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRqVEELHDQI-------EQHKKQR---SQLEKQQNQADqERAD 1227
Cdd:TIGR01612 1117 KDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQIND-LEDVADKAisnddpeEIEKKIEnivTKIDKKKNIYD-EIKK 1194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1228 MAQEIALLQASRADIDKKRKIHEAHLMEIQANLAES-DEHKRT---LIDQLERSRDELDHLNRVREEEEhafaNMQRRLA 1303
Cdd:TIGR01612 1195 LLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKiDEEKKKsehMIKAMEAYIEDLDEIKEKSPEIE----NEMGIEM 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1304 TAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLD------EKEEAEGLRAHLEKEIHAARqgagearrKAEESVN 1377
Cdd:TIGR01612 1271 DIKAEMETFNISHDDDKDHHIISKKHDENISDIREKSLKiiedfsEESDINDIKKELQKNLLDAQ--------KHNSDIN 1342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1378 QQLEELRK-KNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRaSHRDSEKRQKKFESQMAEErvavqk 1456
Cdd:TIGR01612 1343 LYLNEIANiYNILKLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIK-DDINLEECKSKIESTLDDK------ 1415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1457 allDRDAMSQELRDRETRVLSllnevdimkehlEESDrvrrslqqeLQDSISNKDDFGKNVHELEKakrSLEAELNDMRV 1536
Cdd:TIGR01612 1416 ---DIDECIKKIKELKNHILS------------EESN---------IDTYFKNADENNENVLLLFK---NIEMADNKSQH 1468
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1537 QMEELEDNLQIAEDARLRlEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENE------KRGKSGAVSHRK 1610
Cdd:TIGR01612 1469 ILKIKKDNATNDHDFNIN-ELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKysalaiKNKFAKTKKDSE 1547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1611 KIENQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLM 1690
Cdd:TIGR01612 1548 IIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETE 1627
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1691 QARKQlelendeleelrakgggISSEEKRRLEAKIAQLEEELEEEQSNCElAIDKQRKaqvQLEQITTDLSmerTLNQKT 1770
Cdd:TIGR01612 1628 SIEKK-----------------ISSFSIDSQDTELKENGDNLNSLQEFLE-SLKDQKK---NIEDKKKELD---ELDSEI 1683
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1767286957 1771 EAEKQSLERSNRDYK----AKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQF 1845
Cdd:TIGR01612 1684 EKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIGDIYEEF 1762
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
964-1659 |
8.58e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 964 DKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTtqllDHEERAKHGVKAKGRLENQ---LHEL--------- 1031
Cdd:TIGR01612 573 DSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNIS----DKNEYIKKAIDLKKIIENNnayIDELakispyqvp 648
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1032 EQDLNRERQY---KSELEQHKR----KLLAEL-----EDSKDHLAEKmGKVEELNNQLMKRDEELQHQLTRYDEesANVT 1099
Cdd:TIGR01612 649 EHLKNKDKIYstiKSELSKIYEddidALYNELssivkENAIDNTEDK-AKLDDLKSKIDKEYDKIQNMETATVE--LHLS 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1100 LMQKQMRDMQTTIDELREDMETERNArnkaemtrrevvaQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQ 1179
Cdd:TIGR01612 726 NIENKKNELLDIIVEIKKHIHGEINK-------------DLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIK 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1180 HTMEGKIEEQKAKfSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIAllqaSRADI------DKKRKIHEAH- 1252
Cdd:TIGR01612 793 NHYNDQINIDNIK-DEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFL----NKVDKfinfenNCKEKIDSEHe 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1253 -----LMEIQANLaeSDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQR---RLATAEGQIQELNEQIQEETRLK- 1323
Cdd:TIGR01612 868 qfaelTNKIKAEI--SDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKvdeYIKICENTKESIEKFHNKQNILKe 945
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1324 IANINrarqLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEEL---RKKNLRDVEH--LQKQL 1398
Cdd:TIGR01612 946 ILNKN----IDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYfndLKANLGKNKEnmLYHQF 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1399 EESEVAKERILQSKKKIQQELEDSSMelenvrASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSL 1478
Cdd:TIGR01612 1022 DEKEKATNDIEQKIEDANKNIPNIEI------AIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLKH 1095
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1479 LNEVDIMKE-HLEESDRVRRslqqeLQDSISNKDD-FGKNVHELEKAKRSLEAELNDMRVQMEELEDnlqiaedarlrle 1556
Cdd:TIGR01612 1096 YNFDDFGKEeNIKYADEINK-----IKDDIKNLDQkIDHHIKALEEIKKKSENYIDEIKAQINDLED------------- 1157
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1557 vtnqalksESDRAISNKDVEA-EEKRRGLLKQIRDLENELENekrgksgavshRKKIENQIGELEQ---QLEVANRLKEE 1632
Cdd:TIGR01612 1158 --------VADKAISNDDPEEiEKKIENIVTKIDKKKNIYDE-----------IKKLLNEIAEIEKdktSLEEVKGINLS 1218
|
730 740 750
....*....|....*....|....*....|....*....
gi 1767286957 1633 YNKQL------------KKNQQIIKEYQIECEEARQAKE 1659
Cdd:TIGR01612 1219 YGKNLgklflekideekKKSEHMIKAMEAYIEDLDEIKE 1257
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1609-1689 |
8.65e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1609 RKKIENQIGELEQQLEVANRLKEEYNKQLKKNQQII--------KEYQIECEEARQAKEDIAALLRE------ADRKFRA 1674
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEdklleeaeKEAQQAIKEAKKEADEIIKELRQlqkggyASVKAHE 608
|
90
....*....|....*
gi 1767286957 1675 VEAEREQLREANEGL 1689
Cdd:PRK00409 609 LIEARKRLNKANEKK 623
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1237-1680 |
9.19e-05 |
|
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: 47.33 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1237 ASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEgQIQELNEQI 1316
Cdd:pfam05701 28 AHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAK-QDSELAKLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1317 QEETRLKIANINRA---RQLEDEKN---ALLDE----KEEAEGLRahleKEIHAARQGAGEARRKAEESVNQQleelrkk 1386
Cdd:pfam05701 107 VEEMEQGIADEASVaakAQLEVAKArhaAAVAElksvKEELESLR----KEYASLVSERDIAIKRAEEAVSAS------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1387 nlRDVEhlqKQLEESEVakerilqskkkiqqELEDSSMELENVRASHRDSEkrQKKFESQMAEERvavqkallDRDAMSQ 1466
Cdd:pfam05701 176 --KEIE---KTVEELTI--------------ELIATKESLESAHAAHLEAE--EHRIGAALAREQ--------DKLNWEK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1467 ELRDRETRVLSLLNEVDIMKEH---LEESDRVRRSLQQELQDSISNK-DDFGKNVHELEKAKRSLEAELNDMRVQMEELE 1542
Cdd:pfam05701 227 ELKQAEEELQRLNQQLLSAKDLkskLETASALLLDLKAELAAYMESKlKEEADGEGNEKKTSTSIQAALASAKKELEEVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1543 DNLQIAEDARLRLEVTNQALKSESDRaisNKDVEAEEKRRGLLKQIR--DLENELENEKRGKSGAVSHRKKIENQIGELE 1620
Cdd:pfam05701 307 ANIEKAKDEVNCLRVAAASLRSELEK---EKAELASLRQREGMASIAvsSLEAELNRTKSEIALVQAKEKEAREKMVELP 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1621 QQLEVANRLKEEYNKQLKKNQQIIKEYQiecEEARQAKEDIAAL---LREADRKFRAVEAERE 1680
Cdd:pfam05701 384 KQLQQAAQEAEEAKSLAQAAREELRKAK---EEAEQAKAAASTVesrLEAVLKEIEAAKASEK 443
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1047-1403 |
1.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1047 QHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQhQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNAR 1126
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1127 nkaemtrrevvAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQ 1206
Cdd:COG4913 692 -----------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1207 HKKQRSQLEKQQNQADQERADMAQEIALLqasradidkkRKIHEAHLMEIQANLAESDehkrtliDQLERSRDELDHLNR 1286
Cdd:COG4913 761 DAVERELRENLEERIDALRARLNRAEEEL----------ERAMRAFNREWPAETADLD-------ADLESLPEYLALLDR 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1287 VREEEEHAF-ANMQRRLATAEGQ-IQELNEQIQEEtrlkianINRARQLEDEKNALLDEKEEAEGLRAHLE--------- 1355
Cdd:COG4913 824 LEEDGLPEYeERFKELLNENSIEfVADLLSKLRRA-------IREIKERIDPLNDSLKRIPFGPGRYLRLEarprpdpev 896
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1356 ----KEIHAARQGAGEARRKAEESVNQQLEELRKKnLRDVEHLQKQLEESEV 1403
Cdd:COG4913 897 refrQELRAVTSGASLFDEELSEARFAALKRLIER-LRSEEEESDRRWRARV 947
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1198-1383 |
1.08e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.99 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1198 EELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDK---------------KR-----KIHEAhLMEIQ 1257
Cdd:COG0497 154 EELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEAaalqpgeeeeleeerRRlsnaeKLREA-LQEAL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1258 ANLAESDEhkrTLIDQLERSRDELDHLnrvrEEEEHAFANMQRRLATAEGQIQELNEQIQE---------------ETRL 1322
Cdd:COG0497 233 EALSGGEG---GALDLLGQALRALERL----AEYDPSLAELAERLESALIELEEAASELRRyldslefdperleevEERL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1323 KIAN-------------INRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAG---EARRKA----EESVNQQLEE 1382
Cdd:COG0497 306 ALLRrlarkygvtveelLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEklsAARKKAakklEKAVTAELAD 385
|
.
gi 1767286957 1383 L 1383
Cdd:COG0497 386 L 386
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1185-1549 |
1.11e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.02 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1185 KIEEQKAKFSRqveeLHDQIEQHKKQRSQLEKQQNQADQEraDMAQEIALLQASRADIDKKRK---IHEAHLMEIQANLA 1261
Cdd:pfam03528 12 ELEKENAEFYR----LKQQLEAEFNQKRAKFKELYLAKEE--DLKRQNAVLQEAQVELDALQNqlaLARAEMENIKAVAT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1262 ESDEHKRTLIDQLERS-RDELDHLNRVREEE----EHAFanmQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDE 1336
Cdd:pfam03528 86 VSENTKQEAIDEVKSQwQEEVASLQAIMKETvreyEVQF---HRRLEQERAQWNQYRESAEREIADLRRRLSEGQEEENL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1337 KNALLDEKEEAEGLRA---HLEKEIHAARQGAGEARRKAEESVNQQLEELR-----KKNLRdvEHLQKQLEESEVAKERI 1408
Cdd:pfam03528 163 EDEMKKAQEDAEKLRSvvmPMEKEIAALKAKLTEAEDKIKELEASKMKELNhyleaEKSCR--TDLEMYVAVLNTQKSVL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1409 LQSKKKIQQELEDSSMELENVRASHrdsekRQKKFESQMAEERVAVQKALLDRDAMSQE--LRDRETRVLSLLNEVDIMK 1486
Cdd:pfam03528 241 QEDAEKLRKELHEVCHLLEQERQQH-----NQLKHTWQKANDQFLESQRLLMRDMQRMEsvLTSEQLRQVEEIKKKDQEE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1487 EHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAE 1549
Cdd:pfam03528 316 HKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQINSAHGSVHSLDTDVVLGA 378
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
973-1149 |
1.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 973 RNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHeeRAKHGV----KAKGRLENQLHELEQDLNRERQYKSELEQH 1048
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEF--RQKNGLvdlsEEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1049 KRKLLAELEDSKDHLAEKMGK--VEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTID-ELREDMETERNA 1125
Cdd:COG3206 242 LAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqEAQRILASLEAE 321
|
170 180
....*....|....*....|....
gi 1767286957 1126 RNKAEMTRREVVAQLEKVKGDVLD 1149
Cdd:COG3206 322 LEALQAREASLQAQLAQLEARLAE 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
969-1410 |
1.19e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 969 DQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDH---------EERAKHGVKAKGRLENQLHELEQDlnrER 1039
Cdd:PRK04863 785 EKRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHlavafeadpEAELRQLNRRRVELERALADHESQ---EQ 861
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1040 QYKSELEQHKRKL--LAELEDSKDHLAEkmgkveelnNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELRE 1117
Cdd:PRK04863 862 QQRSQLEQAKEGLsaLNRLLPRLNLLAD---------ETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQS 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1118 DMEternarnkaemtrrevvaQLEKVKGDVLDkvdeatmLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQV 1197
Cdd:PRK04863 933 DPE------------------QFEQLKQDYQQ-------AQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNSDLN 987
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1198 EELHDQIEQHKKQRSQLEKQQNQADqerADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEhkrTLIDQLERS 1277
Cdd:PRK04863 988 EKLRQRLEQAEQERTRAREQLRQAQ---AQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADS---GAEERARAR 1061
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1278 RDELDHlnrvreeeehafanmqrRLATAEGQIQELNEQIQ-EETRLKIANiNRARQLEDEknaLLDEKEEAEGLRAHLEK 1356
Cdd:PRK04863 1062 RDELHA-----------------RLSANRSRRNQLEKQLTfCEAEMDNLT-KKLRKLERD---YHEMREQVVNAKAGWCA 1120
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1357 EIHAARQGAGEARRKAEESVNQQLEELRKKN------LR----DVEHLQKQLEESEVAK--ERILQ 1410
Cdd:PRK04863 1121 VLRLVKDNGVERRLHRRELAYLSADELRSMSdkalgaLRlavaDNEHLRDVLRLSEDPKrpERKVQ 1186
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
851-1501 |
1.24e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 851 DELRATKERL-LKMEHDFRENEKKLDQVivERAVIQEQLQQESENSAELDDIRGRlQTRNQELEYIVNDMRDRLSEEEQQ 929
Cdd:pfam05483 200 EELRVQAENArLEMHFKLKEDHEKIQHL--EEEYKKEINDKEKQVSLLLIQITEK-ENKMKDLTFLLEESRDKANQLEEK 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 930 NeKNNDERRKQMETVRDleeqleqeeqarqkllldktnvdqrlrNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLD 1009
Cdd:pfam05483 277 T-KLQDENLKELIEKKD---------------------------HLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQ 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1010 HEERAkhgvkakgrlENQLHELEQDLNRERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLT 1089
Cdd:pfam05483 329 LTEEK----------EAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1090 RYDEESANVTLMQKQMRDMQTTIDELRedmeternarnkaemtrrevvaQLEKVKGDVLDKVDEATMlqdLMSRKDEEVN 1169
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKK----------------------QFEKIAEELKGKEQELIF---LLQAREKEIH 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1170 ATkraieQIQHTMEGKIEEQkakFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIA----LLQASRADIDKK 1245
Cdd:pfam05483 454 DL-----EIQLTAIKTSEEH---YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlELKKHQEDIINC 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1246 RKIHEAHLMEIQaNLAESDEHKRtliDQLERSRDEL----DHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQeETR 1321
Cdd:pfam05483 526 KKQEERMLKQIE-NLEEKEMNLR---DELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCN-NLK 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1322 LKIANINRARQLEDEKNALLDEKEEAEGLRAHL-EKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDvEHLQKQLEE 1400
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKKGSAENKQLNAyEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISE-EKLLEEVEK 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1401 SEVAKERILQSKKKIQQELEDSSMELENVRASHRDS-EKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLL 1479
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQyDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
650 660
....*....|....*....|..
gi 1767286957 1480 NEVDIMKehlEESDRVRRSLQQ 1501
Cdd:pfam05483 760 KQLEIEK---EEKEKLKMEAKE 778
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1081-1263 |
1.48e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1081 DEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDME--TERNARNKAEM---------TRREVVAQLEKVK----- 1144
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelQAELEALQAEIdklqaeiaeAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1145 -------GDVLDKVDEATMLQDLMSR---KDEEVNATKRAIEQIQHTMEgKIEEQKAKFSRQVEELHDQIEQHKKQRSQL 1214
Cdd:COG3883 95 lyrsggsVSYLDVLLGSESFSDFLDRlsaLSKIADADADLLEELKADKA-ELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1767286957 1215 EKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAES 1263
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
957-1201 |
1.50e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 957 ARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEErakhgvkakgrlenQLHELEQDLN 1036
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVM--------------DIEDPSAALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1037 RERQY----KSELEQHKRKLlaeledskdHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEesanvtlMQKQMRDMQTTI 1112
Cdd:PHA02562 259 KLNTAaakiKSKIEQFQKVI---------KMYEKGGVCPTCTQQISEGPDRITKIKDKLKE-------LQHSLEKLDTAI 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1113 DELREDMeterNARNKAEMTRREVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKIEEQKAK 1192
Cdd:PHA02562 323 DELEEIM----DEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELD-KIVKTKSE 397
|
....*....
gi 1767286957 1193 FSRQVEELH 1201
Cdd:PHA02562 398 LVKEKYHRG 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1250-1912 |
1.69e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1250 EAHLMEIQANLAESDEHKRTLIDQLERSRDELDHLNRVrEEEEHAFANMQRRLATAEGQIQEL--------NEQIQEETR 1321
Cdd:pfam12128 199 KSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGI-MKIRPEFTKLQQEFNTLESAELRLshlhfgykSDETLIASR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1322 LKianinRARQLEDEKNALLDEKE-EAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLE------ELRKKNLRDVEHL 1394
Cdd:pfam12128 278 QE-----ERQETSAELNQLLRTLDdQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAfldadiETAAADQEQLPSW 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1395 QKQLEESEVAKERILQSKKKIQQELE--DSSMELENVRASHRDSEKRQKKFES---QMAEERVAVQkalldrdAMSQELR 1469
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNrrRSKIKEQNNRDIAGIKDKLAKIREArdrQLAVAEDDLQ-------ALESELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1470 DRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVH----ELEKAKRSLEA---ELNDMRVQMEELE 1542
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIErareEQEAANAEVERlqsELRQARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1543 DNLQIAEDA----RLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIR-------DLENELENEKRGKS----GAVS 1607
Cdd:pfam12128 506 EALRQASRRleerQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISpellhrtDLDPEVWDGSVGGElnlyGVKL 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1608 HRKKIE-NQIGELEQQLEvanrlkeeynkqlKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREAN 1686
Cdd:pfam12128 586 DLKRIDvPEWAASEEELR-------------ERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNAR 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1687 EGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEeeleeeqsncelaidkqRKAQVQLEQITTDLSMERTL 1766
Cdd:pfam12128 653 LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLD-----------------KKHQAWLEEQKEQKREARTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1767 NQkteAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFE 1846
Cdd:pfam12128 716 KQ---AYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQ 792
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1767286957 1847 DEKRANE--QAKELLEKSNLKNR--NLRRQLDEAEDEMSRE----RTKHRNVQREADDLLDANEQLTRELMNLR 1912
Cdd:pfam12128 793 EVLRYFDwyQETWLQRRPRLATQlsNIERAISELQQQLARLiadtKLRRAKLEMERKASEKQQVRLSENLRGLR 866
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1392-1638 |
1.78e-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: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1392 EHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHR--DSEKRQKKFESQMAEervaVQKALLDRDAMSQELR 1469
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSE----LESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1470 DRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnkddfgknvhelekakrsLEAELNDMRVQMeeLEDNLQIAE 1549
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE----------------------LEAELAELSARY--TPNHPDVIA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1550 dARLRLEVTNQALKSESDRAIsnkdVEAEEKRRGLLKQIRDLENELENEKRgksgAVSHRKKIENQIGELEQQLEVANRL 1629
Cdd:COG3206 296 -LRAQIAALRAQLQQEAQRIL----ASLEAELEALQAREASLQAQLAQLEA----RLAELPELEAELRRLEREVEVAREL 366
|
....*....
gi 1767286957 1630 KEEYNKQLK 1638
Cdd:COG3206 367 YESLLQRLE 375
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1367-1667 |
2.17e-04 |
|
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: 46.17 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1367 EARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEvakerilQSKKKIQQELEDSSMELENVrashrDSEKRQKKFESQ 1446
Cdd:pfam05667 313 PAATSSPPTKVETEEELQQQREEELEELQEQLEDLE-------SSIQELEKEIKKLESSIKQV-----EEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1447 MAEERVAVQKALLDrdamsqELRDRETRVLSLLNEVDIMKEHL----EESDRVRRSLQQE---LQDSISNKDDfgknvhe 1519
Cdd:pfam05667 381 ELEKQYKVKKKTLD------LLPDAEENIAKLQALVDASAQRLvelaGQWEKHRVPLIEEyraLKEAKSNKED------- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1520 leKAKRSLEaELNDMRVQMEElednlqIAEDARLRLEVTNQaLKSESDRAisNKDVEAEEKRRGLL-------KQIRDLE 1592
Cdd:pfam05667 448 --ESQRKLE-EIKELREKIKE------VAEEAKQKEELYKQ-LVAEYERL--PKDVSRSAYTRRILeivknikKQKEEIT 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1593 NELENEKrgksgavSHRKKIENQIGELEQQLEVAnrlKEEYNKQLKKNQQIIKEYQI------ECEEARQAKEDIAALLR 1666
Cdd:pfam05667 516 KILSDTK-------SLQKEINSLTGKLDRTFTVT---DELVFKDAKKDESVRKAYKYlaalheNCEQLIQTVEETGTIMR 585
|
.
gi 1767286957 1667 E 1667
Cdd:pfam05667 586 E 586
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1185-1594 |
2.38e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1185 KIEEQKAKFsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALL--QASRADIDKKRKIHEAHLMEIQANLAE 1262
Cdd:COG4717 72 ELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1263 SDEHK---RTLIDQLERSRDELDHLNRVREEE--------EHAFANMQRRLATAEGQIQELNE---QIQEEtrlkianIN 1328
Cdd:COG4717 151 LEERLeelRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEeleEAQEE-------LE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1329 RARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERI 1408
Cdd:COG4717 224 ELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1409 LQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELR--DRETRVLSLLNEVDIMK 1486
Cdd:COG4717 304 AEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAALLAEAGVED 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1487 E----HLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKA--KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQ 1560
Cdd:COG4717 384 EeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
410 420 430
....*....|....*....|....*....|....
gi 1767286957 1561 ALksESDRAISnkdvEAEEKRRGLLKQIRDLENE 1594
Cdd:COG4717 464 QL--EEDGELA----ELLQELEELKAELRELAEE 491
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1367-1572 |
2.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1367 EARRKAEESVNQQLEELRKknlrdvehlqkQLEESEVAKERILQSK---------KKIQQELEDSSMELENVRASHRDSE 1437
Cdd:COG3206 171 EEARKALEFLEEQLPELRK-----------ELEEAEAALEEFRQKNglvdlseeaKLLLQQLSELESQLAEARAELAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1438 KRQKKFESQMAEERVAV----------------QKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHL-EESDRVRRSLQ 1500
Cdd:COG3206 240 ARLAALRAQLGSGPDALpellqspviqqlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1501 QELQDSISNKDdfgknvhELEKAKRSLEAELNDM---RVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISN 1572
Cdd:COG3206 320 AELEALQAREA-------SLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1325-1573 |
2.70e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1325 ANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQgageARRKAEESVNQQLEELRKKNlRDVEHLQKQLEESEVA 1404
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK----QLAALERRIAALARRIRALE-QELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1405 KERILQSKKKIQQELEdssmelENVRASHRDSEKRQKKF------ESQMAEERVAVQKALLDRDAMSQELRDRETRVLSL 1478
Cdd:COG4942 92 IAELRAELEAQKEELA------ELLRALYRLGRQPPLALllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1479 LNEVDIMKEHLEESDRVRRSLQQELQDSISNKDdfgKNVHELEKAKRSLEAELNDMRVQMEELEDNLqiaedARLRLEVT 1558
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALI-----ARLEAEAA 237
|
250
....*....|....*
gi 1767286957 1559 NQALKSESDRAISNK 1573
Cdd:COG4942 238 AAAERTPAAGFAALK 252
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1132-1434 |
3.09e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1132 TRREVVAQLEKVKGDVLDKVDEATMLQDLmsrkdeevnatkraiEQIQhtmegkieeqkakfsrqveELHDQIEQHKKQR 1211
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEAEDKLVQQDL---------------EQTL-------------------ALLDKIDRQKEET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1212 SQLEKQQNQADQERADMAQEIALLQASRADIDKKRkIHEAHLMEIQANLAEsdehkrtLIDQLERSRDELDHLN------ 1285
Cdd:PRK11281 83 EQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET-LSTLSLRQLESRLAQ-------TLDQLQNAQNDLAEYNsqlvsl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1286 RVREEeehafaNMQRRLATAEGQIQELNeqiqeeTRLKIANINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAAR--Q 1363
Cdd:PRK11281 155 QTQPE------RAQAALYANSQRLQQIR------NLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTqlQ 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1364 GAGEARRkAEESVNQQLEELRKKNLRDVEHlQKQLEESE-VAKEriLQSKKKIQQELEDS--SMELE-NVRASHR 1434
Cdd:PRK11281 223 DLLQKQR-DYLTARIQRLEHQLQLLQEAIN-SKRLTLSEkTVQE--AQSQDEAARIQANPlvAQELEiNLQLSQR 293
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1187-1505 |
3.11e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.10 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1187 EEQKAKFSRQVEELHdqiEQHKKQRSQLEKQQNQADQERADMAQEIALlqASRADIDKKRKIHEAHLMEIQANLAESDEH 1266
Cdd:COG3096 784 EKRLEELRAERDELA---EQYAKASFDVQKLQRLHQAFSQFVGGHLAV--AFAPDPEAELAALRQRRSELERELAQHRAQ 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1267 KRTLIDQLERSRDELDHLNRVR------EEEEHAfanmqRRLATAEGQIQELNEQIQEETRlkiaNINRARQLEDEKNAL 1340
Cdd:COG3096 859 EQQLRQQLDQLKEQLQLLNKLLpqanllADETLA-----DRLEELREELDAAQEAQAFIQQ----HGKALAQLEPLVAVL 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1341 LDEKEEAEGLRAHLEK---EIHAARQGAGE-----ARRKA---EESVnQQLEELRKKNlrdvEHLQKQLEESEVAKERIL 1409
Cdd:COG3096 930 QSDPEQFEQLQADYLQakeQQRRLKQQIFAlsevvQRRPHfsyEDAV-GLLGENSDLN----EKLRARLEQAEEARREAR 1004
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1410 QSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERV-----AVQKALLDRDAMSQELRDRETRVLSLLNEVDI 1484
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTR 1084
|
330 340
....*....|....*....|.
gi 1767286957 1485 MKEHLEESDRVRRSLQQELQD 1505
Cdd:COG3096 1085 CEAEMDSLQKRLRKAERDYKQ 1105
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1199-1896 |
3.14e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.95 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1199 ELHDQI-----EQHKKQRSQLEKQQNQadqeradmAQEIALLQasradidkkrkihEAHLMEIQANL-AESDEHKRTLID 1272
Cdd:PRK10246 180 EIYGQIsamvfEQHKSARTELEKLQAQ--------ASGVALLT-------------PEQVQSLTASLqVLTDEEKQLLTA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1273 QLERSRD-----ELDHLNRVREEEEHAFANMQRRLATAEGQIQELN------------EQIQEETrlkiANINRARQLED 1335
Cdd:PRK10246 239 QQQQQQSlnwltRLDELQQEASRRQQALQQALAAEEKAQPQLAALSlaqparqlrphwERIQEQS----AALAHTRQQIE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1336 EKNALLdekEEAEGLRAhlekeihaarqgagEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERIL---QSK 1412
Cdd:PRK10246 315 EVNTRL---QSTMALRA--------------RIRHHAAKQSAELQAQQQSLNTWLAEHDRFRQWNNELAGWRAQfsqQTS 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1413 KKIQ-QELEDSSMELENVRASHRDSekrqkkfESQMAEERVAVQKALLDRdamSQELRDRETRvlsllnevdimkehLEE 1491
Cdd:PRK10246 378 DREQlRQWQQQLTHAEQKLNALPAI-------TLTLTADEVAAALAQHAE---QRPLRQRLVA--------------LHG 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1492 SDRVRRSLQQELQDSISNkddfgknvHELEKAKRslEAELNDMRVQMEELEDNLQIAEdARLRLEVTNQALKSESDR--- 1568
Cdd:PRK10246 434 QIVPQQKRLAQLQVAIQN--------VTQEQTQR--NAALNEMRQRYKEKTQQLADVK-TICEQEARIKDLEAQRAQlqa 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1569 --------AISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVshrkkIENQIGELEQQLEvanRLKEEYNKQLKKN 1640
Cdd:PRK10246 503 gqpcplcgSTSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEEGAA-----LRGQLDALTKQLQ---RDESEAQSLRQEE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1641 QQIIKEYQIECEEA---RQAKEDIAALLREADRKFR-------------AVEAEREQLREANEGLMQARKQLELENDE-- 1702
Cdd:PRK10246 575 QALTQQWQAVCASLnitLQPQDDIQPWLDAQEEHERqlrllsqrhelqgQIAAHNQQIIQYQQQIEQRQQQLLTALAGya 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1703 --------------LEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQLEQITTD-LSME---R 1764
Cdd:PRK10246 655 ltlpqedeeaswlaTRQQEAQSWQQRQNELTALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQcLSLHsqlQ 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1765 TLNQKTEAEKQSLERSNRDYKAKiteLESGAQSRARAQMAA---------LEAKVQYLEDQLNvegQEKTAANRAARRLE 1835
Cdd:PRK10246 735 TLQQQDVLEAQRLQKAQAQFDTA---LQASVFDDQQAFLAAlldeetltqLEQLKQNLENQRQ---QAQTLVTQTAQALA 808
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1836 KRLNDTTQQFEDEKRANEQAKEL------LEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQ---READD 1896
Cdd:PRK10246 809 QHQQHRPDGLDLTVTVEQIQQELaqlaqqLRENTTRQGEIRQQLKQDADNRQQQQALMQQIAqatQQVED 878
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1158-1475 |
3.23e-04 |
|
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: 45.72 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1158 QDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSrqveelhdqIEQHKKQRSQLEKQQNQADQER---ADMAQEIAL 1234
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKA---------TESLEEQLAAAEAEQELEESKReteTGIQNLTAE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1235 LQASRADIDKKRKIHEAHLMEIQA--NLAESDEHKRTLIDQLERSRDELDHLNR-VREEEEHAFANMQRRLATAEGQIQE 1311
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIENIVGevELSKSSEELDSFKDTIESTKESLDEIPQnQRGYAQEILATLEDTLKAADRQIEE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1312 LNEQIQEETRLKIANINRARQLEDEKNAlLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEE--SVNQQLEELRKKNLR 1389
Cdd:COG5185 425 LQRQIEQATSSNEEVSKLLNELISELNK-VMREADEESQSRLEEAYDEINRSVRSKKEDLNEEltQIESRVSTLKATLEK 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1390 DVEHLQKQLEESEVAKERILQSKKKIQQELEDSS-MELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQEL 1468
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHiLALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQ 583
|
....*..
gi 1767286957 1469 RDRETRV 1475
Cdd:COG5185 584 QAREDPI 590
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1300-1427 |
3.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1300 RRLATAE-GQIQELNEQIQEETRLKIANInrarqledEKNALLDEKEEAEGLRAHLEKEIHAARQGAgearRKAEESVNQ 1378
Cdd:PRK12704 26 KKIAEAKiKEAEEEAKRILEEAKKEAEAI--------KKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLLQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1767286957 1379 QLEELRKKnLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELE 1427
Cdd:PRK12704 94 KEENLDRK-LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
976-1594 |
3.72e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 45.58 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 976 EERLVELQDAYDKLLKEKRLLEEKVEGLTTQLldheERAKHGVKAKGRLENQLHELEQdlNRERQYKSELEQHKRKllAE 1055
Cdd:pfam10174 115 EENFRRLQSEHERQAKELFLLRKTLEEMELRI----ETQKQTLGARDESIKKLLEMLQ--SKGLPKKSGEEDWERT--RR 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1056 LEDSKDHLAEKMGKVEELNNQLMKRDEELqHQLTRYDEESANVTLMQK--QMRD-----MQTTIDELREDMETERNARNK 1128
Cdd:pfam10174 187 IAEAEMQLGHLEVLLDQKEKENIHLREEL-HRRNQLQPDPAKTKALQTviEMKDtkissLERNIRDLEDEVQMLKTNGLL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1129 AEMTRREVVAQLEKVKGD---VLDKVDEATmlQDLmSRKDEEVNA--------------TKRAIEQIQHTMEGKiEEQKA 1191
Cdd:pfam10174 266 HTEDREEEIKQMEVYKSHskfMKNKIDQLK--QEL-SKKESELLAlqtkletltnqnsdCKQHIEVLKESLTAK-EQRAA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1192 KFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQaSRADIdKKRKIheahlMEIQANLAESDEHKRTLI 1271
Cdd:pfam10174 342 ILQTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK-DMLDV-KERKI-----NVLQKKIENLQEQLRDKD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1272 DQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRlkianiNRARQLEDEKNALLDEKEEAEGLR 1351
Cdd:pfam10174 415 KQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDR------ERLEELESLKKENKDLKEKVSALQ 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1352 AHL-EKEI-------HAARQGAGEARRkaeESVNQQLEELRKKNLRDVEHLQKQLEESEVAKErilqsKKKIQQELEDSS 1423
Cdd:pfam10174 489 PELtEKESslidlkeHASSLASSGLKK---DSKLKSLEIAVEQKKEECSKLENQLKKAHNAEE-----AVRTNPEINDRI 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1424 MELENVRASHRD-SEKRQKKFESQMAEERvAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSlqQE 1502
Cdd:pfam10174 561 RLLEQEVARYKEeSGKAQAEVERLLGILR-EVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGA--QL 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1503 LQDSISNKDDFGKNVHELEkakrsleaelndMRVQMEELEDNLQIAEDARLRLEVTNQALkSESDRAISNKDVEaeekRR 1582
Cdd:pfam10174 638 LEEARRREDNLADNSQQLQ------------LEELMGALEKTRQELDATKARLSSTQQSL-AEKDGHLTNLRAE----RR 700
|
650
....*....|..
gi 1767286957 1583 GLLKQIRDLENE 1594
Cdd:pfam10174 701 KQLEEILEMKQE 712
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1181-1463 |
3.74e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1181 TMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANL 1260
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1261 AESDEHKRTLIDQLERSRDELDHLNRVREEEEhafaNMQRRLATAEGQIQELNEQIQEETRLkianINRARQLEDEKNAL 1340
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSID----KLRKEIERLEWRQQTEVLSPEEEKEL----VEKIKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1341 LDEKEEAEGLRAhLEKEIHAARQGAGEARRKAEESVN--QQLEELRKKNLRDVEHLQKQLEEsevAKERILQSKKKIQQE 1418
Cdd:COG1340 153 KKALEKNEKLKE-LRAELKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRKEADE---LHKEIVEAQEKADEL 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1767286957 1419 LEdssmELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDA 1463
Cdd:COG1340 229 HE----EIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1104-1414 |
3.87e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1104 QMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvldkvdeatmlqdlmSRKDEEVNATKRAIEQIQhtme 1183
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELA-----------------EKRDELNAQVKELREEAQ---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1184 gkieeqkaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQaNLAES 1263
Cdd:COG1340 61 --------ELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQ-TEVLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1264 DEHKRTLIDQLERSRDELDHLNRVREEEEHaFANMQRRLATAEGQIQELNEQIQEetrlkianinRARQLEDEKNALLDE 1343
Cdd:COG1340 132 PEEEKELVEKIKELEKELEKAKKALEKNEK-LKELRAELKELRKEAEEIHKKIKE----------LAEEAQELHEEMIEL 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1767286957 1344 KEEAEGLRAHLEkEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKK 1414
Cdd:COG1340 201 YKEADELRKEAD-ELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1281-1534 |
4.40e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 4.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1281 LDHLNRVREEEEhafaNMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEkeeaeglrahlekeiha 1360
Cdd:PLN02939 155 LEDLEKILTEKE----ALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRNELLIR----------------- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1361 arqgaGEARRKAEESVNQQLEELRKKNL---RDVEHLQKQLEESEVAKERILQSKKkiQQELEDSSM-ELE-NVRASHRD 1435
Cdd:PLN02939 214 -----GATEGLCVHSLSKELDVLKEENMllkDDIQFLKAELIEVAETEERVFKLEK--ERSLLDASLrELEsKFIVAQED 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1436 SEK-RQKKFESQMaeERVAVQKALLDRDA-----------MSQELRDRETRVLSLLNE----------VDIM-------K 1486
Cdd:PLN02939 287 VSKlSPLQYDCWW--EKVENLQDLLDRATnqvekaalvldQNQDLRDKVDKLEASLKEanvskfssykVELLqqklkllE 364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1767286957 1487 EHLEESDRVRRSLQQELQDSISNKDDFGKNVHElEKAKRSLEAELNDM 1534
Cdd:PLN02939 365 ERLQASDHEIHSYIQLYQESIKEFQDTLSKLKE-ESKKRSLEHPADDM 411
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1191-1896 |
5.52e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1191 AKFSRQVEELHDQIEQHKKQRSQLEKQQNQ--ADQER-ADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDehk 1267
Cdd:COG3096 271 ADYMRHANERRELSERALELRRELFGARRQlaEEQYRlVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQE--- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1268 rtlidQLERSRDELDHLNRVREEEEHAFANMQRRLATAEgqiqELNEQIQEEtrlkianINRAR-QLEDEKNAL------ 1340
Cdd:COG3096 348 -----KIERYQEDLEELTERLEEQEEVVEEAAEQLAEAE----ARLEAAEEE-------VDSLKsQLADYQQALdvqqtr 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1341 -------LDEKEEAEGLRAHLEKEIHAARQGAGEARRKaEESVNQQLEELRKKnLRDVEHLQKQLEE---------SEVA 1404
Cdd:COG3096 412 aiqyqqaVQALEKARALCGLPDLTPENAEDYLAAFRAK-EQQATEEVLELEQK-LSVADAARRQFEKayelvckiaGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1405 KERILQSKKKIQQELEDSSMELENV---RASHRDSEKR---QKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSL 1478
Cdd:COG3096 490 RSQAWQTARELLRRYRSQQALAQRLqqlRAQLAELEQRlrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEEL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1479 LnevdimkEHLEESDRVRRSLQQELqdsisnkDDFGKNVHELEK---AKRSLEAELNDMRVQMEELEDNLQIAEDARLRL 1555
Cdd:COG3096 570 E-------EQAAEAVEQRSELRQQL-------EQLRARIKELAArapAWLAAQDALERLREQSGEALADSQEVTAAMQQL 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1556 EVTNQALKSESDraisnkdvEAEEKRRGLLKQIRDL-------ENELENEKRGKSG----------AVSHRKKIENQIGE 1618
Cdd:COG3096 636 LEREREATVERD--------ELAARKQALESQIERLsqpggaeDPRLLALAERLGGvllseiyddvTLEDAPYFSALYGP 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1619 LEQQLEVANrlKEEYNKQLKKNQQIIKE-YQIECEE------ARQAKE-DIAALLREADRKFR-------------AVEA 1677
Cdd:COG3096 708 ARHAIVVPD--LSAVKEQLAGLEDCPEDlYLIEGDPdsfddsVFDAEElEDAVVVKLSDRQWRysrfpevplfgraAREK 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1678 EREQLREANEGLMQ-----ARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDKQRKAQVQ 1752
Cdd:COG3096 786 RLEELRAERDELAEqyakaSFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQ 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1753 LEQITTDLSM-ERTLNQKTEAEKQSLERSNRDYKAKITELESGAQSRAR--AQMAALEAKVQYL------EDQLNVEGQE 1823
Cdd:COG3096 866 LDQLKEQLQLlNKLLPQANLLADETLADRLEELREELDAAQEAQAFIQQhgKALAQLEPLVAVLqsdpeqFEQLQADYLQ 945
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1824 KTAANRAARRLEKRLNDTTQQfeDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADD 1896
Cdd:COG3096 946 AKEQQRRLKQQIFALSEVVQR--RPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1304-1693 |
6.45e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 44.75 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1304 TAEGQIQELNEQIQEETRLKI---ANINRAR-QLEDEKNALLDEKE-EAEGLRAHLEKEIHAARQGAGEARRKAEESVNQ 1378
Cdd:pfam09731 49 YALGEDPPLAPKPKTFRPLQPsvvSAVTGESkEPKEEKKQVKIPRQsGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1379 QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIqqeLEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAL 1458
Cdd:pfam09731 129 ALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDS---LKEASDTAEISREKATDSALQKAEALAEKLKEVINLAKQS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1459 LDRDAMSQELRDRETrVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFgknVHELEKAKRSLEAELNDMRVQM 1538
Cdd:pfam09731 206 EEEAAPPLLDAAPET-PPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVF---QQELVSIFPDIIPVLKEDNLLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1539 EElEDNLQIAeDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENekrgksgavsHRKKIENQIgE 1618
Cdd:pfam09731 282 ND-DLNSLIA-HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEE----------VRAADEAQL-R 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1619 LEQQLEVAnRLKEEYNKQLKKnqqiikeyqieceEARQAKEDIAALLREADRKfRAVEAEREQLREANEGLMQAR 1693
Cdd:pfam09731 349 LEFERERE-EIRESYEEKLRT-------------ELERQAEAHEEHLKDVLVE-QEIELQREFLQDIKEKVEEER 408
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
878-1286 |
6.71e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 878 IVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIvnDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQA 957
Cdd:PRK11281 35 LPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALL--DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 958 RQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLeekvEGLTTQLldheERAKHGVKAKgrlENQLHELEQDLNR 1037
Cdd:PRK11281 113 ETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQL----VSLQTQP----ERAQAALYAN---SQRLQQIRNLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1038 ERQYKSELEQHKRKLL-AELedskDHLAEKMgkveELNNQLMKRDEELQHQLT-RYDEESANVTLMQKQMRDMQTTIDEL 1115
Cdd:PRK11281 182 GKVGGKALRPSQRVLLqAEQ----ALLNAQN----DLQRKSLEGNTQLQDLLQkQRDYLTARIQRLEHQLQLLQEAINSK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1116 RedmeternaRNKAEMTRREVVAQLEKVKGD----VLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKA 1191
Cdd:PRK11281 254 R---------LTLSEKTVQEAQSQDEAARIQanplVAQELEINLQLSQRLLKATEKLNTLTQQNLRVKNWLDRLTQSERN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1192 kfsrqveeLHDQIE--QHKKQRSQLEKQQNQA---DQERADMAQEIALLQASRADIDKKRK---IHEAHLMEIQANLAE- 1262
Cdd:PRK11281 325 --------IKEQISvlKGSLLLSRILYQQQQAlpsADLIEGLADRIADLRLEQFEINQQRDalfQPDAYIDKLEAGHKSe 396
|
410 420
....*....|....*....|....*
gi 1767286957 1263 -SDEHKRTLIDQLERSRDELDHLNR 1286
Cdd:PRK11281 397 vTDEVRDALLQLLDERRELLDQLNK 421
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1506-1695 |
6.84e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1506 SISNKDDFGKNvHELEKakRSLEAELNDMRVQMEELEDNLQIAEDARLRLEV------------TNQALKSESDRAISNK 1573
Cdd:COG4913 205 PIGDLDDFVRE-YMLEE--PDTFEAADALVEHFDDLERAHEALEDAREQIELlepirelaeryaAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1574 DVEAEEKRRGLLKQ-IRDLENELENEKRGKSGAVSHRKKIENQIGELEQQ--------LEVANRLKEEYNKQLKKNQQII 1644
Cdd:COG4913 282 RLWFAQRRLELLEAeLEELRAELARLEAELERLEARLDALREELDELEAQirgnggdrLEQLEREIERLERELEERERRR 361
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1645 KEYQIECEEARQA----KEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQ 1695
Cdd:COG4913 362 ARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD 416
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1038-1873 |
7.87e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.56 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1038 ERQYKSELEQHKRKllaELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVTLMQKQMRdMQTTIDELRE 1117
Cdd:COG3096 279 ERRELSERALELRR---ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALR-QQEKIERYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1118 DMEternarnkaemtrrEVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATK-------RAIEqIQHTMEGKIEE-- 1188
Cdd:COG3096 355 DLE--------------ELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKsqladyqQALD-VQQTRAIQYQQav 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1189 ---QKAKFSRQVEELHdqIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIheahLMEIQANLAESDE 1265
Cdd:COG3096 420 qalEKARALCGLPDLT--PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYEL----VCKIAGEVERSQA 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1266 HKrTLIDQLERSRDELDHLNRVreeeehafANMQRRLATAEgqiQELNEQIQEETRLKIANINRARQLEDEKNaLLDEKE 1345
Cdd:COG3096 494 WQ-TARELLRRYRSQQALAQRL--------QQLRAQLAELE---QRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1346 EAEGLRAHLEKEIHAARQGAGEARRKaEESVNQQLEELRKK-----NLRDV-EHLQKQLEESevakeriLQSKKKIQQEL 1419
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQ-LEQLRARIKELAARapawlAAQDAlERLREQSGEA-------LADSQEVTAAM 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1420 EdssMELENVRashrdsekrqkkfESQMAEERVAVQKALLDRDA--MSQELRDRETRVLS--------LLNEV--DIMKE 1487
Cdd:COG3096 633 Q---QLLERER-------------EATVERDELAARKQALESQIerLSQPGGAEDPRLLAlaerlggvLLSEIydDVTLE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1488 H----------------LEESDRVRRSLQQeLQDSIS-------NKDDFGKNVH---ELEKA------------------ 1523
Cdd:COG3096 697 DapyfsalygparhaivVPDLSAVKEQLAG-LEDCPEdlyliegDPDSFDDSVFdaeELEDAvvvklsdrqwrysrfpev 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1524 ----KRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALkseSDRAISNKDVEAEEKRRGLLKQIRDLENELENEK 1599
Cdd:COG3096 776 plfgRAAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAF---SQFVGGHLAVAFAPDPEAELAALRQRRSELEREL 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1600 RGKSGAVSHRKKienQIGELEQQLEVANRLKEEYNkqLKKNQQIIKEYQiECEEARQAKEDIAALLREADRKFRAVEAER 1679
Cdd:COG3096 853 AQHRAQEQQLRQ---QLDQLKEQLQLLNKLLPQAN--LLADETLADRLE-ELREELDAAQEAQAFIQQHGKALAQLEPLV 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1680 EQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRL-------EAKIAQLEEELEEEQSNCELAIDKQRKAQVQ 1752
Cdd:COG3096 927 AVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedaVGLLGENSDLNEKLRARLEQAEEARREAREQ 1006
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1753 LEQIT---TDLSMERT-LNQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKV-------QYLEDQLNVEG 1821
Cdd:COG3096 1007 LRQAQaqySQYNQVLAsLKSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEELsqnrsrrSQLEKQLTRCE 1086
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1822 QEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQL 1873
Cdd:COG3096 1087 AEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLARDNDVERRLHRREL 1138
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1632-1896 |
8.49e-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: 8.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1632 EYNKQLKKNQQIIKEYQIECEEARQAKEDiaaLLREADRKFRAVEAEREQLREAN-EGLMQARKQLELENDELEELRakg 1710
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEE---KAREVERRRKLEEAEKARQAEMDrQAAIYAEQERMAMERERELER--- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1711 ggISSEEKRRLEAKIAQLeeeleeeqsncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQSLERSNRDYKAKITE 1790
Cdd:pfam17380 353 --IRQEERKRELERIRQE-----------EIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQK 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1791 LES----GAQSRARA-QMAALEAKVQYLEDQLNVEGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSnlk 1865
Cdd:pfam17380 420 VEMeqirAEQEEARQrEVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKI--- 496
|
250 260 270
....*....|....*....|....*....|.
gi 1767286957 1866 nrnLRRQLDEAEDEMSRERTKHRNVQREADD 1896
Cdd:pfam17380 497 ---LEKELEERKQAMIEEERKRKLLEKEMEE 524
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1310-1420 |
8.67e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1310 QELNEQI----QEETRLKIANINrARQLEDEKNALLDE-KEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELR 1384
Cdd:PRK00409 516 EKLNELIasleELERELEQKAEE-AEALLKEAEKLKEElEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELR 594
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1767286957 1385 KK--------NLRDVEHLQKQLEESEVAKERILQSKKKIQQELE 1420
Cdd:PRK00409 595 QLqkggyasvKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
847-1090 |
9.50e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 847 RAKDDELRATKERLLKmehdfRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVN--------- 917
Cdd:COG4913 590 HEKDDRRRIRSRYVLG-----FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeidva 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 918 ---DMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLK--- 991
Cdd:COG4913 665 saeREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDlar 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 992 -------EKRLLEEKVEGLTTQLLDHEERAKHGVKAK-GRLENQLHELEQDLNRErqYKSELEQHK---------RKLLA 1054
Cdd:COG4913 745 lelrallEERFAAALGDAVERELRENLEERIDALRARlNRAEEELERAMRAFNRE--WPAETADLDadleslpeyLALLD 822
|
250 260 270
....*....|....*....|....*....|....*..
gi 1767286957 1055 ELEDskDHLAEKMGKVEELNNQLMKRD-EELQHQLTR 1090
Cdd:COG4913 823 RLEE--DGLPEYEERFKELLNENSIEFvADLLSKLRR 857
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1214-1882 |
9.92e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1214 LEKQQNQADQERADMAQEialLQASRADIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQ--LERSRDELDHLN------ 1285
Cdd:NF041483 78 LRNAQIQADQLRADAERE---LRDARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLDQelAERRQTVESHVNenvawa 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1286 ---RVREEE------EHAFANMQRRLATAEGQIQELNEQIQE-------------ETRLKIANINRARQLEDEKNALLDE 1343
Cdd:NF041483 155 eqlRARTESqarrllDESRAEAEQALAAARAEAERLAEEARQrlgseaesaraeaEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1344 KEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRD-------VEHLQKQLEESEVAKE-RILQSKKKI 1415
Cdd:NF041483 235 TDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAekvvaeaKEAAAKQLASAESANEqRTRTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1416 QQELEDSSMELENVRAshrdsEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEV---------DIMK 1486
Cdd:NF041483 315 ARLVGEATKEAEALKA-----EAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEVltkasedakATTR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1487 EHLEESDRVRRSLQQElqdsisnKDDFGKNVHEL-EKAKRSLEAELNDMRVQMEELEDnlqiaEDARLRLEVtnQALKSE 1565
Cdd:NF041483 390 AAAEEAERIRREAEAE-------ADRLRGEAADQaEQLKGAAKDDTKEYRAKTVELQE-----EARRLRGEA--EQLRAE 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1566 sdrAISNKDVEAEEKRRGLLKQIRDLENELE----------NEKRGKSGAVSHRKKIEnqigeleqQLEVANRLKEEYNK 1635
Cdd:NF041483 456 ---AVAEGERIRGEARREAVQQIEEAARTAEelltkakadaDELRSTATAESERVRTE--------AIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1636 QLKKNQQIIKEYQIECEE----ARQAKEDIAALLREADRkfRAVEAEREqlrEANEGLmqARKQLELENDELEELRAKGG 1711
Cdd:NF041483 525 TLERTRAEAERLRAEAEEqaeeVRAAAERAARELREETE--RAIAARQA---EAAEEL--TRLHTEAEERLTAAEEALAD 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1712 GISSEEKRRLEAkiAQLEEELEEEqsncelAIDKQRKAQVQLEQITTDLSMERTLN-QKTEAEKQSLE-RSNRDYKAKIT 1789
Cdd:NF041483 598 ARAEAERIRREA--AEETERLRTE------AAERIRTLQAQAEQEAERLRTEAAADaSAARAEGENVAvRLRSEAAAEAE 669
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1790 ELESGAQS---RARAQMAALEAKVQYLEDQLNVEGQEKtaANRAARRLEKRLNDTTQQFEDEK-RANEQAKELLEKSnlk 1865
Cdd:NF041483 670 RLKSEAQEsadRVRAEAAAAAERVGTEAAEALAAAQEE--AARRRREAEETLGSARAEADQEReRAREQSEELLASA--- 744
|
730
....*....|....*..
gi 1767286957 1866 nrnlRRQLDEAEDEMSR 1882
Cdd:NF041483 745 ----RKRVEEAQAEAQR 757
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1379-1711 |
1.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1379 QLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEERVAVQKAL 1458
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1459 LDRDAMSQELRDREtrvlsllNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQM 1538
Cdd:COG4372 94 AELAQAQEELESLQ-------EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1539 EELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGE 1618
Cdd:COG4372 167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1619 LEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLEL 1698
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330
....*....|...
gi 1767286957 1699 ENDELEELRAKGG 1711
Cdd:COG4372 327 KLELALAILLAEL 339
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
897-1216 |
1.19e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.86 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 897 ELDDIRGRLQTRNQ---ELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLR 973
Cdd:TIGR04523 322 KLEEIQNQISQNNKiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 974 NLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLL 1053
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1054 AELEDSKDHLAEKMGKVEELNNQ-----------------LMKRDEELQHQLTRY-------------DEESANVTLMQK 1103
Cdd:TIGR04523 482 QNLEQKQKELKSKEKELKKLNEEkkeleekvkdltkkissLKEKIEKLESEKKEKeskisdledelnkDDFELKKENLEK 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1104 QMRDMQTTIDELREDMETERNARNKAEmtrrEVVAQLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEqiqhTME 1183
Cdd:TIGR04523 562 EIDEKNKEIEELKQTQKSLKKKQEEKQ----ELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLS----SII 633
|
330 340 350
....*....|....*....|....*....|...
gi 1767286957 1184 GKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEK 1216
Cdd:TIGR04523 634 KNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIK 666
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
838-1474 |
1.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENE-KKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRN----QEL 912
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLpasaEEF 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 913 EYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVE-LQDAYDKL-- 989
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELpf 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 990 ---LKEKRLLEEK----VE----GLTTQLL---DHEERAKH---GVKAKGRLenQLHELEQDLNRERQYKSeleqHKRKL 1052
Cdd:COG4913 463 vgeLIEVRPEEERwrgaIErvlgGFALTLLvppEHYAAALRwvnRLHLRGRL--VYERVRTGLPDPERPRL----DPDSL 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1053 LAELeDSKDHLAEkmgkvEELNNQLMKR--------DEELQHQ---LTRYDEESANVTLMQKQMRDMQTT---------- 1111
Cdd:COG4913 537 AGKL-DFKPHPFR-----AWLEAELGRRfdyvcvdsPEELRRHpraITRAGQVKGNGTRHEKDDRRRIRSryvlgfdnra 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1112 -IDELREDMETERNARNKAEmtrrEVVAQLEKVKGDVLDKVDEATMLQDLmSRKDEEVNATKRAIEQiqhtmegkIEEQK 1190
Cdd:COG4913 611 kLAALEAELAELEEELAEAE----ERLEALEAELDALQERREALQRLAEY-SWDEIDVASAEREIAE--------LEAEL 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1191 akfsRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRkihEAHLMEIQANLAESDEHKRTL 1270
Cdd:COG4913 678 ----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL---DELQDRLEAAEDLARLELRAL 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1271 IDQLERSRDELDHLNRVREeeehafaNMQRRLATAEGQIQELNEQIqeetRLKIANINraRQLEDEKNALLDEKEEAEGL 1350
Cdd:COG4913 751 LEERFAAALGDAVERELRE-------NLEERIDALRARLNRAEEEL----ERAMRAFN--REWPAETADLDADLESLPEY 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1351 RAHLEKeihAARQGAGEARRKAEESVNQQleelrkkNLRDVEHLQKQLEES-EVAKERIlqskKKIQQEL------EDSS 1423
Cdd:COG4913 818 LALLDR---LEEDGLPEYEERFKELLNEN-------SIEFVADLLSKLRRAiREIKERI----DPLNDSLkripfgPGRY 883
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1424 MELEnVRASH-----------RDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETR 1474
Cdd:COG4913 884 LRLE-ARPRPdpevrefrqelRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWR 944
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1666-1912 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1666 READRKFRAVEAEREQLREANEGLMQARKQlelendeleelRAKGGGISSEEKRRLEAKIAQLEEELEEEQSNCELAIDK 1745
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQ-----------IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1746 QRKAQVQLEQITTDLsmertlnQKTEAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNVEGQEKT 1825
Cdd:COG4913 290 LELLEAELEELRAEL-------ARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1826 AANRAARRLEKRLNDTTQQFEDEKRaneQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLT 1905
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
....*..
gi 1767286957 1906 RELMNLR 1912
Cdd:COG4913 440 ARLLALR 446
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1496-1908 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1496 RRSLQQELQDSISNKDDfgknvHELEKAKRSLEAELNDMRVQMEELEDNLQIA----EDARLRLEVTNQALKS----ESD 1567
Cdd:PRK02224 185 QRGSLDQLKAQIEEKEE-----KDLHERLNGLESELAELDEEIERYEEQREQAretrDEADEVLEEHEERREEletlEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1568 RAISNKDVEAEEKRRGLLK-QIRDLENELE------NEKRGKSG-------AVS-HRKKIENQIGELEQQLEVANRLKEE 1632
Cdd:PRK02224 260 IEDLRETIAETEREREELAeEVRDLRERLEeleeerDDLLAEAGlddadaeAVEaRREELEDRDEELRDRLEECRVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1633 YNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKggg 1712
Cdd:PRK02224 340 HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE--- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1713 iSSEEKRRLEAKIAQLEEELEEEQsncelaiDKQRKAQVQLEQittdlsmertlnQKTEAEKQSLERSNR-----DYKAK 1787
Cdd:PRK02224 417 -LREERDELREREAELEATLRTAR-------ERVEEAEALLEA------------GKCPECGQPVEGSPHvetieEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1788 ITELESgAQSRARAQMAALEAKVQYLEDqlnvegqektaanraARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNR 1867
Cdd:PRK02224 477 VEELEA-ELEDLEEEVEEVEERLERAED---------------LVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1767286957 1868 NLRRQLDEAEDEMSRERTKHRNVQREADDLLDANEQLTREL 1908
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1747-1914 |
1.57e-03 |
|
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: 43.52 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1747 RKAQVQLEQITTDLS-MERTLNQKT------EAEKQSLERSNRDYKAKITELESGAQSRARAQMAALEAKVQYLEDQLNV 1819
Cdd:TIGR02169 233 EALERQKEAIERQLAsLEEELEKLTeeiselEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1820 EGQEKTAANRAARRLEKRLNDTTQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEAEDEMSRERTKHRNVQREADDLLD 1899
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
|
170
....*....|....*
gi 1767286957 1900 ANEQLTRELMNLRGN 1914
Cdd:TIGR02169 393 KLEKLKREINELKRE 407
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
957-1099 |
1.60e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 957 ARQKLLLDKTNVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKgrlenQLHELEQDLN 1036
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEIE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1037 RERQYKSELEQHKRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVT 1099
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
843-1237 |
1.70e-03 |
|
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: 43.27 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 843 DDEIRAKDDELRATKERLLKMEHDFRENEKKLDqviveraVIQEQLQQESENSA----ELDDIRGRLQTRNQEL----EY 914
Cdd:pfam10174 295 KQELSKKESELLALQTKLETLTNQNSDCKQHIE-------VLKESLTAKEQRAAilqtEVDALRLRLEEKESFLnkktKQ 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 915 I-------------VNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQKLLLDKTNVDQRLRNLEERLVE 981
Cdd:pfam10174 368 LqdlteekstlageIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSE 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 982 LQDAYDKLLKEK----RLLEEKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKLLAELE 1057
Cdd:pfam10174 448 KERIIERLKEQReredRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1058 DSKDHL---------AEKMGKVEELNNQLMKRDEELQHQLTRYDEESAnvtlmqKQMRDMQTTIDELREdMETERNARNK 1128
Cdd:pfam10174 528 QKKEECsklenqlkkAHNAEEAVRTNPEINDRIRLLEQEVARYKEESG------KAQAEVERLLGILRE-VENEKNDKDK 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1129 A-----EMTRREVVAQLEKVK----GDVLDKVDEATMLQDLMSRKDEEV-NATKRAIEQIQHTME---GKIEEQKAKFSR 1195
Cdd:pfam10174 601 KiaeleSLTLRQMKEQNKKVAnikhGQQEMKKKGAQLLEEARRREDNLAdNSQQLQLEELMGALEktrQELDATKARLSS 680
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1767286957 1196 QVEELHDQIEQHKKQRSQLEKQQnqadQERADMAQEiALLQA 1237
Cdd:pfam10174 681 TQQSLAEKDGHLTNLRAERRKQL----EEILEMKQE-ALLAA 717
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
860-1652 |
1.89e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 860 LLKMEHDFRENEKKLDQVIVERAVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDErrK 939
Cdd:PTZ00440 648 LDDHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDNIIKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLN--Q 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 940 QMETVRDLEEQLEQEEQARQKLLLDKTNVDQRlrnLEERLVELQDAYDKLLKEKRLLEEKVEglttqlldheerakhgvk 1019
Cdd:PTZ00440 726 YTIKYNDLKSSIEEYKEEEEKLEVYKHQIINR---KNEFILHLYENDKDLPDGKNTYEEFLQ------------------ 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1020 akgrlenqlhELEQDLNRERQYKSELEQHKRkllaELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANVT 1099
Cdd:PTZ00440 785 ----------YKDTILNKENKISNDINILKE----NKKNNQDLLNSYNILIQKLEAHTEKNDEELKQLLQKFPTEDENLN 850
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1100 LMQ--KQMRDMQTTIDELREDMETER---------NARNKAEMTRREVVAQLEKVKGDVLDKVDEATML--QDLMSRKDE 1166
Cdd:PTZ00440 851 LKEleKEFNENNQIVDNIIKDIENMNkniniiktlNIAINRSNSNKQLVEHLLNNKIDLKNKLEQHMKIinTDNIIQKNE 930
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1167 EVNATKRAIEQiqhtmEGKIEEQ--KAKFSRQVEELHDQIEQHKKQRSQLE-------KQQNQADQERADMAQEIALLQA 1237
Cdd:PTZ00440 931 KLNLLNNLNKE-----KEKIEKQlsDTKINNLKMQIEKTLEYYDKSKENINgndgthlEKLDKEKDEWEHFKSEIDKLNV 1005
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1238 SRADIDKK-----RKIHEAHLMEIQANLAESDEHKRTLIDQlersrdELDHLNRVREEEEHAFANMQRRL---ATAEGQI 1309
Cdd:PTZ00440 1006 NYNILNKKiddliKKQHDDIIELIDKLIKEKGKEIEEKVDQ------YISLLEKMKTKLSSFHFNIDIKKyknPKIKEEI 1079
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1310 QELNEQIqeETRLKiaNINrarqleDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGeARRKAEESVNQQLEELRKK--N 1387
Cdd:PTZ00440 1080 KLLEEKV--EALLK--KID------ENKNKLIEIKNKSHEHVVNADKEKNKQTEHYN-KKKKSLEKIYKQMEKTLKEleN 1148
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1388 LRDVEHLQKQLEESEVAKERIL--QSKKKIQQELEDSSMELENVRASHRDSEKRQKKfesqMAEERVAVQKAlLDRDAMS 1465
Cdd:PTZ00440 1149 MNLEDITLNEVNEIEIEYERILidHIVEQINNEAKKSKTIMEEIESYKKDIDQVKKN----MSKERNDHLTT-FEYNAYY 1223
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1466 QELRDRETRVLSLLNEVDIMKE------HLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLeaELNDMRVQME 1539
Cdd:PTZ00440 1224 DKATASYENIEELTTEAKGLKGeanrstNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNMYEFL--ISIDSEKILK 1301
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1540 ELEDNLQIAEDArlrlevtnqalksesdraisNKDVEAE-EKRRGLLKQIRDLENELENEKRGKSGAVSHrKKIENQIGE 1618
Cdd:PTZ00440 1302 EILNSTKKAEEF--------------------SNDAKKElEKTDNLIKQVEAKIEQAKEHKNKIYGSLED-KQIDDEIKK 1360
|
810 820 830
....*....|....*....|....*....|....
gi 1767286957 1619 LEQQLEVANRLKEEYNKQLKKnqqiIKEYQIECE 1652
Cdd:PTZ00440 1361 IEQIKEEISNKRKEINKYLSN----IKSNKEKCD 1390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1378-1545 |
1.92e-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: 41.83 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1378 QQLEELRKKnlrdVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQM-----AEERV 1452
Cdd:COG1579 17 SELDRLEHR----LKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1453 AVQKALldrDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISnkddfgknvhELEKAKRSLEAELN 1532
Cdd:COG1579 93 ALQKEI---ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA----------ELDEELAELEAELE 159
|
170
....*....|...
gi 1767286957 1533 DMRVQMEELEDNL 1545
Cdd:COG1579 160 ELEAEREELAAKI 172
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1024-1364 |
1.95e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1024 LENQLHELEQDLNR----ERQYKSELEQHKRKL--LAELEDSKDHLAEkmgkveelnNQLMKRDEELQHQLTRYDEESAN 1097
Cdd:COG3096 841 LRQRRSELERELAQhraqEQQLRQQLDQLKEQLqlLNKLLPQANLLAD---------ETLADRLEELREELDAAQEAQAF 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1098 VTLMQKQMRDMQTTIDELREDMEternarnkaemtrrevvaQLEKVKGDVLDkvdeatmLQDLMSRKDEEVNATKRAIEQ 1177
Cdd:COG3096 912 IQQHGKALAQLEPLVAVLQSDPE------------------QFEQLQADYLQ-------AKEQQRRLKQQIFALSEVVQR 966
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1178 IQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRadiDKKRKIHEAHLMEIQ 1257
Cdd:COG3096 967 RPHFSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSR---DAKQQTLQELEQELE 1043
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1258 A--------NLAESDEHKRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQE-----ETRLKI 1324
Cdd:COG3096 1044 ElgvqadaeAEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQakagwCAVLRL 1123
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1767286957 1325 ANINRA-RQLEDEKNALLDekeeAEGLRAHLEKEIHAARQG 1364
Cdd:COG3096 1124 ARDNDVeRRLHRRELAYLS----ADELRSMSDKALGALRLA 1160
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1609-1684 |
2.52e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.11 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1609 RKKIENQIGELEQQLEVANRLKEEYNKQLK----KNQQIIKEYQIECEEAR-----QAKEDIAALLREADrkfRAVEAER 1679
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAearaEAQEIIEEARKEAEKIKeeilaEAKEEAERILEQAK---AEIEQEK 108
|
....*
gi 1767286957 1680 EQLRE 1684
Cdd:cd06503 109 EKALA 113
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
882-1282 |
2.64e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 42.87 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 882 AVIQEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEK-----NNDERRKQMETVRDLEEQ------ 950
Cdd:PRK10246 429 VALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADvkticEQEARIKDLEAQRAQLQAgqpcpl 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 951 ----LEQEEQARQKLLLDktnVDQRlrnleeRLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVKAKGRLEN 1026
Cdd:PRK10246 509 cgstSHPAVEAYQALEPG---VNQS------RLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQ 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1027 QLHELEQDLNRERQYKSEL-------EQHKRKL--LAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRY------ 1091
Cdd:PRK10246 580 QWQAVCASLNITLQPQDDIqpwldaqEEHERQLrlLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYaltlpq 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1092 -----------DEESANVTLMQKQMRDMQTTIDELREDMETERnarnkaemTRREVVAQLEKVKGDVLDKV-DEATMLQ- 1158
Cdd:PRK10246 660 edeeaswlatrQQEAQSWQQRQNELTALQNRIQQLTPLLETLP--------QSDDLPHSEETVALDNWRQVhEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1159 DLMSRKDEEVNATKRAIEQIQH---TMEGKIEEQKAKFSR---------QVEELHDQIEQHKKQRSQLEKQQNQADQER- 1225
Cdd:PRK10246 732 QLQTLQQQDVLEAQRLQKAQAQfdtALQASVFDDQQAFLAalldeetltQLEQLKQNLENQRQQAQTLVTQTAQALAQHq 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1226 ------ADMAQEIALLQASRADIDKKRKIHEAHLMEIQANL---AESDEHKRTLIDQLERSRDELD 1282
Cdd:PRK10246 812 qhrpdgLDLTVTVEQIQQELAQLAQQLRENTTRQGEIRQQLkqdADNRQQQQALMQQIAQATQQVE 877
|
|
| HpsJ_fam |
NF038305 |
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ... |
1283-1379 |
2.69e-03 |
|
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.
Pssm-ID: 468465 [Multi-domain] Cd Length: 230 Bit Score: 41.42 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1283 HLNRVREEEEHAFANMQRRLATAEGQIQ-------------ELNEQIQEETRLKIAnINRARQLEDEKNALLDEKEEAEG 1349
Cdd:NF038305 98 HLNNTRRLSTQALQQINQQAGQQETQLQqqlnqlqaqtspqQLNQLLKSEQKQGQA-LASGQLPEEQKEQLQQFKSNPQA 176
|
90 100 110
....*....|....*....|....*....|
gi 1767286957 1350 LRAHLEKEIHAARQGAGEARRKAEESVNQQ 1379
Cdd:NF038305 177 LDKFLAQQLTQIRTQAEEAEKQARLEALKS 206
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1187-1637 |
2.84e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 42.59 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1187 EEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQANLAESDEH 1266
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1267 KRTLIDQLERSRDELDHLNRVREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANINRARQLEDEKNALLDEKEE 1346
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1347 AEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMEL 1426
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1427 ENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDS 1506
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1507 IsnkddfGKNVHELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLK 1586
Cdd:COG5278 402 A------AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1767286957 1587 QIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQL 1637
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1534-1638 |
2.88e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1534 MRVQMEELEDNLQIAEDARLRLEVTNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIE 1613
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELE 481
|
90 100
....*....|....*....|....*...
gi 1767286957 1614 NQ---IGELEQQLEVANRLKEEYNKQLK 1638
Cdd:COG0542 482 QRygkIPELEKELAELEEELAELAPLLR 509
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1246-1493 |
3.01e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1246 RKIHEAHLMEIQaNLAESDEHKRT--LIDQLERSRDELDHLNRVREEEEHAFANMQR-RLATAEGQIQELNE---QIQEE 1319
Cdd:PRK05771 23 EALHELGVVHIE-DLKEELSNERLrkLRSLLTKLSEALDKLRSYLPKLNPLREEKKKvSVKSLEELIKDVEEeleKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1320 TRLKIANINrarQLEDEKNALLDEKEEAEGLRAhLEKEIHAARQG------------AGEARRKAEESVNQQLEELRKKN 1387
Cdd:PRK05771 102 IKELEEEIS---ELENEIKELEQEIERLEPWGN-FDLDLSLLLGFkyvsvfvgtvpeDKLEELKLESDVENVEYISTDKG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1388 -------------------LRDVEHLQKQLEESEVAKERILQSKKKIqQELEDssmELENVRASHRDSEKRQKKFESQMA 1448
Cdd:PRK05771 178 yvyvvvvvlkelsdeveeeLKKLGFERLELEEEGTPSELIREIKEEL-EEIEK---ERESLLEELKELAKKYLEELLALY 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1767286957 1449 EERVAV-QKA-LLDRDAMSQEL--------RDRETRVLSLLNEVDIMKEHLEESD 1493
Cdd:PRK05771 254 EYLEIElERAeALSKFLKTDKTfaiegwvpEDRVKKLKELIDKATGGSAYVEFVE 308
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1056-1246 |
3.25e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1056 LEDSKDHLAEKMGKVEEL-NNQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRR 1134
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKNiEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1135 EVVAQLEKVKGDV--LDKVDEA-TMLQDLmSRKDEEVNATKRAIEQIQHTME---------GKIEEQKAKFSRQVEELHD 1202
Cdd:PHA02562 266 KIKSKIEQFQKVIkmYEKGGVCpTCTQQI-SEGPDRITKIKDKLKELQHSLEkldtaidelEEIMDEFNEQSKKLLELKN 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1767286957 1203 QIEQHK-------KQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKR 1246
Cdd:PHA02562 345 KISTNKqslitlvDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTK 395
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1519-1665 |
3.27e-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: 41.45 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1519 ELEKAKRSLEAELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESdraisnKDVEAEEKR-RGLLKQIRD------L 1591
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEI------EEVEARIKKyEEQLGNVRNnkeyeaL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1592 ENELENEKRGKSGAVSHRKKIENQIGELEQQLEVAN----RLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALL 1665
Cdd:COG1579 95 QKEIESLKRRISDLEDEILELMERIEELEEELAELEaelaELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1626-1809 |
3.32e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 41.75 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1626 ANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQlreaneglMQARKQLELENDELEE 1705
Cdd:TIGR02794 52 ANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQA--------EQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1706 LRAKGggiSSEEKRRLEAKIAQLEEELEEEQSncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQsLERSNRDYK 1785
Cdd:TIGR02794 124 AKAKQ---AAEAKAKAEAEAERKAKEEAAKQA--EEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK-AKAEEAKAK 197
|
170 180
....*....|....*....|....
gi 1767286957 1786 AKITELESGAQSRARAQMAALEAK 1809
Cdd:TIGR02794 198 AEAAKAKAAAEAAAKAEAEAAAAA 221
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1518-1723 |
3.43e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1518 HELEKAKRSLEA--ELNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSES-DRAISNKDVE---AEEKRRGLLKQIRDL 1591
Cdd:COG4913 242 EALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELlEAELEELRAElarLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1592 ENE---LENEKRGKSGavshrkkieNQIGELEQQLEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREA 1668
Cdd:COG4913 322 REEldeLEAQIRGNGG---------DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAAL 392
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1767286957 1669 DRKFRAVEAE-REQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEA 1723
Cdd:COG4913 393 LEALEEELEAlEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1419-1863 |
3.48e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1419 LEDSSMELENVRASHRD-SEKRQKKFESQMAEERV--AVQKALLDRDAMSQELR-------DRETRVLSLLNEVDIMKEH 1488
Cdd:PTZ00108 906 LESETLKEKDVIVDYRDySTANTVHFTVKLNDGVLeqWEEEGIEKVFKLKSTISttnmvlfDENGKIKKYSDALDILKEF 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1489 LE---ESDRVRRS-----LQQELQdSISNKDDFGKNVHELE-----KAKRSLEAELNdmRVQMEELEDNLQIAEDARLRL 1555
Cdd:PTZ00108 986 YLvrlDLYKKRKEyllgkLERELA-RLSNKVRFIKHVINGElvitnAKKKDLVKELK--KLGYVRFKDIIKKKSEKITAE 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1556 EVTNQALKSESDRAISNKDVEAEEKRRGLLK---------QIRDLENELeNEKRGKSGAVSHR----------KKIENQI 1616
Cdd:PTZ00108 1063 EEEGAEEDDEADDEDDEEELGAAVSYDYLLSmpiwsltkeKVEKLNAEL-EKKEKELEKLKNTtpkdmwledlDKFEEAL 1141
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1617 GELEQQlEVANRLKEEYNKQLKKNQQIIKEYQIECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQL 1696
Cdd:PTZ00108 1142 EEQEEV-EEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS 1220
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1697 ELENDELEELRAKGGGISSEEKRRLEAKIAQLEEELEEEQSncELAIDKQRKAQVQLEQITTDLSMERTLNQKTEAEKQS 1776
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFS--SDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNG 1298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1777 LERSNRDYKAKItelesgaQSRARAQMAALEAKVQylEDQLNVEGQEKTAA---------NRAARRLEKRLNDTTQQFED 1847
Cdd:PTZ00108 1299 GSKPSSPTKKKV-------KKRLEGSLAALKKKKK--SEKKTARKKKSKTRvkqasasqsSRLLRRPRKKKSDSSSEDDD 1369
|
490
....*....|....*.
gi 1767286957 1848 EKRANEQAKELLEKSN 1863
Cdd:PTZ00108 1370 DSEVDDSEDEDDEDDE 1385
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1391-1808 |
3.52e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.98 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1391 VEHLQKQLEESEVAKERILQSKKKIQQELEDSSM---ELENVRASHRDSEKRQKKFESQMAEERVAVQKALLDRDAMSQE 1467
Cdd:pfam19220 33 IEPIEAILRELPQAKSRLLELEALLAQERAAYGKlrrELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1468 LRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQdsisnkddfgknvhELEKAKRSLEAELNDMRVQMEELEDnlqi 1547
Cdd:pfam19220 113 LRDKTAQAEALERQLAAETEQNRALEEENKALREEAQ--------------AAEKALQRAEGELATARERLALLEQ---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1548 aEDARLRLEVTNQALKSESdraISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVShrkKIENQIGELEQQLEVAN 1627
Cdd:pfam19220 175 -ENRRLQALSEEQAAELAE---LTRRLAELETQLDATRARLRALEGQLAAEQAERERAEA---QLEEAVEAHRAERASLR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1628 RLKEEYNKQLKKNQQIIKEyqieceeARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELR 1707
Cdd:pfam19220 248 MKLEALTARAAATEQLLAE-------ARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRAR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1708 AKGGGISSEEKRRLEAKIAQLeeeleeeqsncELAIDKQRKAQVQLEQittdlsmertLNQKTEAEKQSLERSNRDYKAk 1787
Cdd:pfam19220 321 AELEERAEMLTKALAAKDAAL-----------ERAEERIASLSDRIAE----------LTKRFEVERAALEQANRRLKE- 378
|
410 420
....*....|....*....|.
gi 1767286957 1788 itELESGAQSRARAQmAALEA 1808
Cdd:pfam19220 379 --ELQRERAERALAQ-GALEI 396
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
972-1363 |
4.15e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 41.59 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 972 LRNLEERLVELQDAYDKLLKEkrLLEEKVEGLTTQLLDHEERAKHGvkakgRLENQLHELEQDLNRERQYKSELEQHKRK 1051
Cdd:pfam19220 22 LRSLKADFSQLIEPIEAILRE--LPQAKSRLLELEALLAQERAAYG-----KLRRELAGLTRRLSAAEGELEELVARLAK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1052 LLAELEDSKDHLAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNarnkaem 1131
Cdd:pfam19220 95 LEAALREAEAAKEELRIELRDKTAQA----EALERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELA------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1132 TRREVVAQLEkvkgdvldkvDEATMLQDLMSRKDEEVNATKRAIEQiqhtMEGKIEEQKAKFSRQVEELHDQIEQHKKQR 1211
Cdd:pfam19220 164 TARERLALLE----------QENRRLQALSEEQAAELAELTRRLAE----LETQLDATRARLRALEGQLAAEQAERERAE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1212 SQLEKQQNQADQERADMAQEIALLQASRA--------------DIDKKRKIHEAHLMEIQANLAESDEHKRTLIDQLERS 1277
Cdd:pfam19220 230 AQLEEAVEAHRAERASLRMKLEALTARAAateqllaearnqlrDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1278 RDELDHLNRVREEEEH-------AFANMQRRLATAEGQIQELNEQIQEETRlkiANINRARQLEDEKNALLDEKEEAEGL 1350
Cdd:pfam19220 310 TQQFQEMQRARAELEEraemltkALAAKDAALERAEERIASLSDRIAELTK---RFEVERAALEQANRRLKEELQRERAE 386
|
410
....*....|...
gi 1767286957 1351 RAHLEKEIHAARQ 1363
Cdd:pfam19220 387 RALAQGALEIARE 399
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1371-1577 |
4.24e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.80 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1371 KAEESVNQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFESQMAEE 1450
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1451 RVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAE 1530
Cdd:pfam07888 128 EARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1767286957 1531 LNDMRVQMEELEDNLQIAEDARLRLEVTNQALKSESDR-AISNKDVEA 1577
Cdd:pfam07888 208 VLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERlNASERKVEG 255
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1188-1456 |
4.37e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 41.34 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1188 EQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLMEI-------QANL 1260
Cdd:pfam15905 66 QKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELtrvnellKAKF 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1261 AESDEHKRTLIDQLErsrdeLDHLNRVREEEEHAFANMQRRLataEGQIQELNEQIqEETRLKIANI-NRARQLEDEKNa 1339
Cdd:pfam15905 146 SEDGTQKKMSSLSME-----LMKLRNKLEAKMKEVMAKQEGM---EGKLQVTQKNL-EHSKGKVAQLeEKLVSTEKEKI- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1340 llDEKEEAEGLRAHLEkEIHAARQGAGEARRKAeesvnQQLEELRKKNLRDVEHLQKQLEESEVAKERILQSKKKIQQEL 1419
Cdd:pfam15905 216 --EEKSETEKLLEYIT-ELSCVSEQVEKYKLDI-----AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLL 287
|
250 260 270
....*....|....*....|....*....|....*..
gi 1767286957 1420 EDssmELENVRASHRDSEKRQKKfESQMAEERVAVQK 1456
Cdd:pfam15905 288 ES---EKEELLREYEEKEQTLNA-ELEELKEKLTLEE 320
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
972-1349 |
4.41e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 41.94 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 972 LRNLEERLVELQDAYDKLLKEKRL--------------LEEKVEGLTTQLLDHEE-----RAKHgvkakgrLENQLHELE 1032
Cdd:pfam05701 140 LKSVKEELESLRKEYASLVSERDIaikraeeavsaskeIEKTVEELTIELIATKEslesaHAAH-------LEAEEHRIG 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1033 QDLNRER---QYKSELEQHK---RKLLAELEDSKDHLAekmgKVEELNNQLMKRDEEL-QHQLTRYDEESANVTLMQKQM 1105
Cdd:pfam05701 213 AALAREQdklNWEKELKQAEeelQRLNQQLLSAKDLKS----KLETASALLLDLKAELaAYMESKLKEEADGEGNEKKTS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1106 RDMQTTIDELREDMETERNARNKA--EMTRREVVA-----QLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQI 1178
Cdd:pfam05701 289 TSIQAALASAKKELEEVKANIEKAkdEVNCLRVAAaslrsELEKEKAELASLRQREGMASIAVSSLEAELNRTKSEIALV 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1179 QhTMEGKIEEQKAKFSRQVEELHDQIEQHKKQ----RSQLEKQQNQADQERADMAQEIALLQASRADIDKKRKIHEAHLM 1254
Cdd:pfam05701 369 Q-AKEKEAREKMVELPKQLQQAAQEAEEAKSLaqaaREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1255 EIQAnLAESDEHKRTlIDQLERSR------DELDHLN-RVREEEEHAfanmQRRLATAEGQIQELNEqiqEETRL--KIA 1325
Cdd:pfam05701 448 AIKA-LQESESSAES-TNQEDSPRgvtlslEEYYELSkRAHEAEELA----NKRVAEAVSQIEEAKE---SELRSleKLE 518
|
410 420
....*....|....*....|....
gi 1767286957 1326 NINraRQLEDEKNALLDEKEEAEG 1349
Cdd:pfam05701 519 EVN--REMEERKEALKIALEKAEK 540
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1025-1618 |
4.49e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.13 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1025 ENQLHELEQDLNRERQYKSELEQH------KRKLLAELEDSKDHLAEKMGKVEELNNQLMKRDEELQHQLTRYDEESANV 1098
Cdd:PTZ00440 549 LQSIETLIKDEKLKRSMKNDIKNKikyieeNVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYI 628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1099 tLMQKQMRDMQTTIDEL------REDMETERNARNKAEMTRREVVAQLEKVKGDVLDKVDEatMLQDLMSRKDEEVNATK 1172
Cdd:PTZ00440 629 -LNKFYKGDLQELLDELshflddHKYLYHEAKSKEDLQTLLNTSKNEYEKLEFMKSDNIDN--IIKNLKKELQNLLSLKE 705
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1173 RAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQERADMaqeIALLQASRADIDKKRKIHEAH 1252
Cdd:PTZ00440 706 NIIKKQLNNIEQDISNSLNQYTIKYNDLKSSIEEYKEEEEKLEVYKHQIINRKNEF---ILHLYENDKDLPDGKNTYEEF 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1253 LmeiqanlaesdEHKRTLidqLERSRDELDHLNRVREEEEhafaNMQRRLATAEGQIQELneqiQEETRLKIANINRARQ 1332
Cdd:PTZ00440 783 L-----------QYKDTI---LNKENKISNDINILKENKK----NNQDLLNSYNILIQKL----EAHTEKNDEELKQLLQ 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1333 LEDEKNALLDEKEeaeglrahLEKEIHaarqgagEARRKAEESVNQQleELRKKNLRDVEHLQKQLEESEVAK---ERIL 1409
Cdd:PTZ00440 841 KFPTEDENLNLKE--------LEKEFN-------ENNQIVDNIIKDI--ENMNKNINIIKTLNIAINRSNSNKqlvEHLL 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1410 QSKKKIQQELEDSSMELENVRAShRDSEKrqKKFESQMAEERVAVQKALLDrdamsQELRDRETRVLSLLNEVDIMKE-- 1487
Cdd:PTZ00440 904 NNKIDLKNKLEQHMKIINTDNII-QKNEK--LNLLNNLNKEKEKIEKQLSD-----TKINNLKMQIEKTLEYYDKSKEni 975
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1488 ------HLEESDRVRRS---LQQELQDSISNKDDFGKNVHELEKAKRSLEAELNDMRVQ------MEELEDNLQIAEDAR 1552
Cdd:PTZ00440 976 ngndgtHLEKLDKEKDEwehFKSEIDKLNVNYNILNKKIDDLIKKQHDDIIELIDKLIKekgkeiEEKVDQYISLLEKMK 1055
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1553 LRLEV--TNQALKSESDRAISNKDVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGE 1618
Cdd:PTZ00440 1056 TKLSSfhFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTE 1123
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1334-1416 |
5.26e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.86 E-value: 5.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1334 EDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVN-----QQLEELRKKNLRDVEHLQKQ-----LEESEV 1403
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVAleglaAELEEKQQELEAQLEQLQEKaaetsQERKQK 217
|
90
....*....|...
gi 1767286957 1404 AKERILQSKKKIQ 1416
Cdd:PRK11448 218 RKEITDQAAKRLE 230
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1303-1502 |
5.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1303 ATAEGQIQELNEQIQEetrlkiaNINRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARR---KAEESVNQQ 1379
Cdd:COG3883 12 AFADPQIQAKQKELSE-------LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAeiaEAEAEIEER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1380 LEELRK------KNLRDVEHLQkQLEESE---------VAKERILQSKKKIQQELEDSSMELENVRASHRDSEKRQKKFE 1444
Cdd:COG3883 85 REELGEraralyRSGGSVSYLD-VLLGSEsfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1767286957 1445 SQMAEERVAVQKALLDRDAMSQELRDRETRVLSLLNEVDIMKEHLEESDRVRRSLQQE 1502
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1493-1915 |
6.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1493 DRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAELNdmrvQMEELEDNLQIAEDARLRLEVTNQALKSESDRaisn 1572
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEK---- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1573 kdVEAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLKK----NQQIIKEYQ 1648
Cdd:COG4717 121 --LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1649 IECEEARQAKEDIAALLREADRKFRAVEAEREQLREANEGLMQARKQLELENDELEELRAKGGGISSEEKRRLEAKIAQL 1728
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1729 EEELEEEQSNCELAIDKQRKAQVQLEQITTDLSMERTLNQKT-----EAEKQSLERSNRDYKAKITELESGAQSRARAQM 1803
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1804 AALEAKVQYLEDQLNVEGQEKTAANRAArrLEKRLNDTtQQFEDEKRANEQAKELLEKSNLKNRNLRRQLDEA--EDEMS 1881
Cdd:COG4717 359 LEEELQLEELEQEIAALLAEAGVEDEEE--LRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELE 435
|
410 420 430
....*....|....*....|....*....|....
gi 1767286957 1882 RERTKHRNVQREADDLLDANEQLTRELMNLRGNN 1915
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
998-1247 |
7.02e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.66 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 998 EKVEGLTTQLLDHEERAKHGVKAKGRLENQLHELEQDLNRERQYKSELEQHKRKL---LAELEDSKDHLAEKMGKVEELN 1074
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreeAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1075 NQLMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNK--------AEMTRR-EVVAQLEKVKG 1145
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEekelvekiKELEKElEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1146 DVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEGKIEEQKaKFSRQVEELHDQIEQHKKQRSQLEKQQNQADQER 1225
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD-ELRKEADELHKEIVEAQEKADELHEEIIELQKEL 239
|
250 260
....*....|....*....|..
gi 1767286957 1226 ADMAQEIALLQASRADIDKKRK 1247
Cdd:COG1340 240 RELRKELKKLRKKQRALKREKE 261
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1374-1594 |
7.04e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 41.18 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1374 ESVNQQLEELRKknlrdvEHLQKQ-LEESEVAKeRILQSKKKIQQELEDSSmELENVRAS-HRDSEKRQKKFESqmAEER 1451
Cdd:pfam10168 535 QLLSRATQVFRE------EYLKKHdLAREEIQK-RVKLLKLQKEQQLQELQ-SLEEERKSlSERAEKLAEKYEE--IKDK 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1452 vavQKALLDRdamsqelrdretrvlsllnevdiMKehleesdRVRRSLQQELQDSISNKDDFGKNVHELEKAKRSLEAEL 1531
Cdd:pfam10168 605 ---QEKLMRR-----------------------CK-------KVLQRLNSQLPVLSDAEREMKKELETINEQLKHLANAI 651
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1767286957 1532 NDMRVQMEELEDNLQIAEDARLRLEVTnqaLKSESDRAISNKDVEAEEKRRGLLKQIRDLENE 1594
Cdd:pfam10168 652 KQAKKKMNYQRYQIAKSQSIRKKSSLS---LSEKQRKTIKEILKQLGSEIDELIKQVKDINKH 711
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1576-1689 |
7.68e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1576 EAEEKRRGLLKQIRDLENELENEKRGKSGAVSHRKKIENQIGELEQQLEVANRLKEEYNKQLK--KNQQIIKEYQIECEE 1653
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIES 100
|
90 100 110
....*....|....*....|....*....|....*.
gi 1767286957 1654 ARQAKEDIAALLREADRKFRAVEAEREQLREANEGL 1689
Cdd:COG1579 101 LKRRISDLEDEILELMERIEELEEELAELEAELAEL 136
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1162-1305 |
8.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 8.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1162 SRKDEEVNATKRAIEQIQHTMEGKIEEQKAKFSRQVEELHDQIEQhkkqrsqLEKQQNQADQERADMAQEIALLQASRAD 1241
Cdd:PRK12704 53 AIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN-------LDRKLELLEKREEELEKKEKELEQKQQE 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1767286957 1242 IDKKRKIHEAHLMEIQANLAE-----SDEHKRTLIDQLE-RSRDELDHLNRVREEEEHAFANMQRR--LATA 1305
Cdd:PRK12704 126 LEKKEEELEELIEEQLQELERisgltAEEAKEILLEKVEeEARHEAAVLIKEIEEEAKEEADKKAKeiLAQA 197
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
871-1280 |
8.77e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 8.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 871 EKKLDQVIVERAviqEQLQQESENSAELDDIRGRLQTRNQELEYIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQ 950
Cdd:pfam07888 33 QNRLEECLQERA---ELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 951 LEQEEQARQKLLLDKTNVDQRLRNLEERLvelqdaydKLLKEKRLLEEkvegltTQLLDHEERAKhgvkakgRLENQLHE 1030
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRELEEDI--------KTLTQRVLERE------TELERMKERAK-------KAGAQRKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1031 LEQDlnrERQYKSELEQHK---RKLLAELEDSKDHLAEKMGKVEELNNQLMKrdeeLQHQLTRYDEESANVTLMQKQMRD 1107
Cdd:pfam07888 169 EEAE---RKQLQAKLQQTEeelRSLSKEFQELRNSLAQRDTQVLQLQDTITT----LTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1108 MQTTIDELREDMETERNARNKAEMTRREVVAQLEKVKgdvLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTMEgKIE 1187
Cdd:pfam07888 242 LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR---LQAAQLTLQLADASLALREGRARWAQERETLQQSAE-ADK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1188 EQKAKFSRQVEELHDQIEQHKKQRSQLEKQQNQ-ADQERADMAQEIALLQASRADIDKKRKIHEAHLMEIQanlaESDEH 1266
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKLEVELGReKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQ----ELLEY 393
|
410
....*....|....
gi 1767286957 1267 KRTLIDQLERSRDE 1280
Cdd:pfam07888 394 IRQLEQRLETVADA 407
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1139-1399 |
9.01e-03 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 40.83 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1139 QLEKVKGDVLDKVDEATMLQDLMSRKDEEVNATKRAIEQIQHTME------------GKIEEQKAKFSRQVEELHDQIEQ 1206
Cdd:COG4192 38 SLSNQIRYILDDSLPKLQASLKLEENSNELVAALPEFAAATNTTErsqlrnqlntqlADIEELLAELEQLTQDAGDLRAA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1207 HKKQRSQLEkQQNQADQERADMAQEialLQASRADIdkkRKIHEAHLMEIQANLAESDEHKRTLIDQLErsrdeldhLNR 1286
Cdd:COG4192 118 VADLRNLLQ-QLDSLLTQRIALRRR---LQELLEQI---NWLHQDFNSELTPLLQEASWQQTRLLDSVE--------TTE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1287 VREEEEHAFANMQRRLATAEGQIQELNEQIQEETRLKIANInrARQLE------DEKNALLDEKEEAEGLRAHLEKEIHA 1360
Cdd:COG4192 183 SLRNLQNELQLLLRLLAIENQIVSLLREVAAARDQADVDNL--FDRLQylkdelDRNLQALKNYPSTITLRQLIDELLAI 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1767286957 1361 AR-QGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQLE 1399
Cdd:COG4192 261 GSgEGGLPSLRRDELAAQATLEALAEENNSILEQLRTQIS 300
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
838-1185 |
9.61e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 838 QVTRTDDEIRAKDDELRATKERLLKMEHDFRENEKkLDQVIVERAVIQEQLQQESENSAELDDIRGR----LQTRNQELE 913
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEA-LKLQMAEKDKVIEILRQQIENMTQLVGQHGRtagaMQVEKAQLE 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 914 YIVNDMRDRLSEEEQQNEKNNDERRKQMETVRDLEEQLEQEEQARQkllldktnvdQRLRNLEerlvELQDAYDKLLKEK 993
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGS----------ERLRAVK----DIKQERDQLLNEV 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 994 RLLEEKVEGLTTqllDHEERAKHGVKAKGRLENQLHELEQDLnreRQYKSELEQhKRKLLAELEDSKDH----------- 1062
Cdd:pfam15921 663 KTSRNELNSLSE---DYEVLKRNFRNKSEEMETTTNKLKMQL---KSAQSELEQ-TRNTLKSMEGSDGHamkvamgmqkq 735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1063 LAEKMGKVEELNNQLmkrdEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDMETERNARNKAEMTRREVVAQLEK 1142
Cdd:pfam15921 736 ITAKRGQIDALQSKI----QFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEV 811
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1767286957 1143 vkgdVLDKVD-EATMLQDLMSRKDEEVNATKraieqIQHTMEGK 1185
Cdd:pfam15921 812 ----ALDKASlQFAECQDIIQRQEQESVRLK-----LQHTLDVK 846
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
967-1139 |
9.77e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 9.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 967 NVDQRLRNLEERLVELQDAYDKLLKEKRLLEEKVEGLTTQLLDHEERAKHGVK--AKGRLENQLHELEQDLNRERQYKSE 1044
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTP 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1045 LEQHKRKLLAELEDSKDHLAEKMGKV-EELNNQ---LMKRDEELQHQLTRYDEESANVTLMQKQMRDMQTTIDELREDME 1120
Cdd:COG3206 289 NHPDVIALRAQIAALRAQLQQEAQRIlASLEAEleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYE 368
|
170
....*....|....*....
gi 1767286957 1121 TERNARNKAEMTRREVVAQ 1139
Cdd:COG3206 369 SLLQRLEEARLAEALTVGN 387
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1328-1426 |
9.84e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 38.62 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767286957 1328 NRARQLEDEKNALLDEKEEAEGLRAHLEKEIHAARQGAGEARRKAEESVNQQLEELRKKNLRDVEHLQKQleesevAKER 1407
Cdd:COG0711 31 ERQEKIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQ------AEAE 104
|
90
....*....|....*....
gi 1767286957 1408 ILQSKKKIQQELEDSSMEL 1426
Cdd:COG0711 105 IEQERAKALAELRAEVADL 123
|
|
| |
