|
Name |
Accession |
Description |
Interval |
E-value |
| MYSc_Myh2_insects_mollusks |
cd14911 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
145-814 |
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: 1457.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14911 1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPH----PAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 300
Cdd:cd14911 81 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHpavnPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 301 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 380
Cdd:cd14911 161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 381 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 460
Cdd:cd14911 241 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 461 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 540
Cdd:cd14911 321 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 541 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVA 620
Cdd:cd14911 401 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLY 700
Cdd:cd14911 481 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRTVSHLY 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 701 KEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIP 780
Cdd:cd14911 561 KEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIP 640
|
650 660 670
....*....|....*....|....*....|....
gi 62471805 781 KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14911 641 KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
|
|
| MYSc_class_II |
cd01377 |
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ... |
145-814 |
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: 1294.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01377 1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd01377 81 ESGAGKTENTKKVIQYLASVAASSKKKKESGKKK----GTLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGST 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV-KSYAFLSNGSLPVPGVDDYAEFQATVKS 383
Cdd:cd01377 157 GKIAGADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGDpSYYFFLSQGELTIDGVDDAEEFKLTDEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd01377 237 FDILGFSEEEKMSIFKIVAAILHLGNIKFKQRRREEQAELDGTEEADKAAHLLGVNSSDLLKALLKPRIKVGREWVTKGQ 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd01377 317 NKEQVVFSVGALAKALYERLFLWLVKRINKTLD-TKSKRQYFIGVLDIAGFEIFEFNSFEQLCINYTNEKLQQFFNHHMF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG-GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK--TDFRGVA 620
Cdd:cd01377 396 VLEQEEYKKEGIEWTFIDFGLDLQPTIDLIEKPNmGILSILDEECVFPKATDKTFVEKLYSNHLGKSKNFKkpKPKKSEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGmaqqaltDTQFGARTRKGMFRTVSHLY 700
Cdd:cd01377 476 HFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLFKDYEESG-------GGGGKKKKKGGSFRTVSQLH 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 701 KEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIP 780
Cdd:cd01377 549 KEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILAPNAIP 628
|
650 660 670
....*....|....*....|....*....|....
gi 62471805 781 KGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd01377 629 KGFDDGKAACEKILKALQLDPELYRIGNTKVFFK 662
|
|
| Myosin_head |
pfam00063 |
Myosin head (motor domain); |
133-814 |
0e+00 |
|
Myosin head (motor domain);
Pssm-ID: 395017 [Multi-domain] Cd Length: 674 Bit Score: 1157.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 133 VEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNML 212
Cdd:pfam00063 1 VEDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 213 GDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGavphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSR 292
Cdd:pfam00063 81 QDKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNV---------GRLEEQILQSNPILEAFGNAKTVRNNNSSR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 293 FGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGV 371
Cdd:pfam00063 152 FGKYIEIQFDAKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQsGCYTIDGI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 372 DDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPR 451
Cdd:pfam00063 232 DDSEEFKITDKAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKERNDEQAVPDDTENLQKAASLLGIDSTELEKALCKRR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 452 IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTN 531
Cdd:pfam00063 312 IKTGRETVSKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASFIGVLDIYGFEIFEKNSFEQLCINYVN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 532 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 610
Cdd:pfam00063 392 EKLQQFFNHHMFKLEQEEYVREGIEWTFIDFG-DNQPCIDLIEkKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHPH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 611 FMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRK 690
Cdd:pfam00063 471 FQKPRLQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAELFPDYETAESAAANESGKSTPKRTKK 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 691 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 770
Cdd:pfam00063 551 KRFITVGSQFKESLGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQR 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....
gi 62471805 771 YELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:pfam00063 631 YRILAPKTWPKWKGDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
|
|
| MYSc_Myh10 |
cd14920 |
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
145-814 |
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: 1141.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14920 1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAAS-KPKGSGAVPhpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14920 81 ESGAGKTENTKKVIQYLAHVASShKGRKDHNIP------GELERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKS 383
Cdd:cd14920 155 TGYIVGANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQDKDNFQETMEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14920 235 MHIMGFSHEEILSMLKVVSSVLQFGNISFKKERNTDQASMPENTVAQKLCHLLGMNVMEFTRAILTPRIKVGRDYVQKAQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14920 315 TKEQADFAVEALAKATYERLFRWLVHRINKALDRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DFRGV 619
Cdd:cd14920 395 ILEQEEYQREGIEWNFIDFGLDLQPCIDLIERPAnppGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrQLKDK 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 620 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA--RTRKGMFRT 695
Cdd:cd14920 475 ADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAELWKDVDrIVGLDQVTgMTETAFGSayKTKKGMFRT 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 696 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 775
Cdd:cd14920 555 VGQLYKESLTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILT 634
|
650 660 670
....*....|....*....|....*....|....*....
gi 62471805 776 PNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14920 635 PNAIPKGFMDGKQACERMIRALELDPNLYRIGQSKIFFR 673
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
891-1971 |
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: 1072.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 891 TKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQEL 970
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 971 ETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEER 1050
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1051 ANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAK 1130
Cdd:pfam01576 161 ISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1131 REEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQE 1210
Cdd:pfam01576 241 KEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1211 LRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSR 1290
Cdd:pfam01576 321 LRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1291 QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEE 1370
Cdd:pfam01576 401 QDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1371 TRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQ 1450
Cdd:pfam01576 481 TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1451 VKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLS 1530
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALS 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1531 VSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEV 1610
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEV 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1611 NMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHA 1690
Cdd:pfam01576 721 NMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQL 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1691 KKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLM 1770
Cdd:pfam01576 801 KKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSAL 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1771 IDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETA 1850
Cdd:pfam01576 881 QDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGT 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1851 QRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLD 1930
Cdd:pfam01576 961 VKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLE 1040
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 62471805 1931 ETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKL 1971
Cdd:pfam01576 1041 EAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| MYSc |
smart00242 |
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ... |
126-826 |
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: 1054.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 126 NPPKFDKVEDMAELTCLNEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITD 205
Cdd:smart00242 1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 206 SAYRNMLGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGavphpavligeLEQQLLQANPILEAFGNAKTV 285
Cdd:smart00242 81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSGSNTEVGS-----------VEDQILESNPILEAFGNAKTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 286 KNDNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG- 364
Cdd:smart00242 150 RNNNSSRFGKFIEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGg 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 365 SLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNT-VAQKIAHLLGLSVTDM 443
Cdd:smart00242 230 CLTVDGIDDAEEFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAASTVKDKeELSNAAELLGVDPEEL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 444 TRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFE 523
Cdd:smart00242 310 EKALTKRKIKTGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLS-FKDGSTYFIGVLDIYGFEIFEVNSFE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 524 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLV 602
Cdd:smart00242 389 QLCINYANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFF-DNQDCIDLIeKKPPGILSLLDEECRFPKGTDQTFLEKLN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 603 SAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdt 682
Cdd:smart00242 468 QHHKKHPHFSKPKKKGRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASLFPSGV------------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 683 qfGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRI 762
Cdd:smart00242 536 --SNAGSKKRFQTVGSQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRL 613
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 763 PFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFRAGVLAHLEEERD 826
Cdd:smart00242 614 PFDEFLQRYRVLLPDTWPPWGGDAKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEELRE 677
|
|
| MYSc_Myh18 |
cd14932 |
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
145-814 |
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: 1050.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14932 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAAS----KPKGSGAVPHpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 300
Cdd:cd14932 81 ESGAGKTENTKKVIQYLAYVASSfktkKDQSSIALSH-----GELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 301 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQAT 380
Cdd:cd14932 156 FDVNGYIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQDKELFAET 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 381 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVT 460
Cdd:cd14932 236 MEAFRIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASMPDDTAAQKVCHLLGMNVTDFTRAILSPRIKVGRDYVQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 461 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 540
Cdd:cd14932 316 KAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 541 TMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDF 616
Cdd:cd14932 396 TMFILEQEEYQREGIEWSFIDFGLDLQPCIELIEKPNgppGILALLDEECWFPKATDKSFVEKVVQEQGNNPKFQKpKKL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 617 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQFGA-RTRKGMF 693
Cdd:cd14932 476 KDDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSELWKDVDrIVGLDKVAgMGESLHGAfKTRKGMF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 694 RTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 773
Cdd:cd14932 556 RTVGQLYKEQLMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEI 635
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 62471805 774 LTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14932 636 LTPNAIPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
|
|
| MYSc_Myh11 |
cd14921 |
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ... |
145-814 |
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: 996.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14921 1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKpKGSgavpHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14921 81 ESGAGKTENTKKVIQYLAVVASSH-KGK----KDTSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14921 156 GYIVGANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQDDEMFQETLEAM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd14921 236 SIMGFSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd14921 316 KEQADFAIEALAKATYERLFRWILTRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DFRGVA 620
Cdd:cd14921 396 LEQEEYQREGIEWNFIDFGLDLQPCIELIERPNnppGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKPkQLKDKT 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF--GARTRKGMFRTV 696
Cdd:cd14921 476 EFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDrIVGLDQMAkMTESSLpsASKTKKGMFRTV 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14921 556 GQLYKEQLGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAA 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 777 NVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14921 636 NAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
|
|
| MYSc_Myh9 |
cd14919 |
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ... |
145-814 |
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: 985.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14919 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14919 81 ESGAGKTENTKKVIQYLAHVASSHKSKKDQ--------GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14919 153 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQDKDMFQETMEAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd14919 233 RIMGIPEEEQMGLLRVISGVLQLGNIVFKKERNTDQASMPDNTAAQKVSHLLGINVTDFTRGILTPRIKVGRDYVQKAQT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd14919 313 KEQADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASFIGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMFI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDFRGVA 620
Cdd:cd14919 393 LEQEEYQREGIEWNFIDFGLDLQPCIDLIEKPAgppGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKpKQLKDKA 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQA-LTDTQF-GA-RTRKGMFRTV 696
Cdd:cd14919 473 DFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSELWKDVDrIIGLDQVAgMSETALpGAfKTRKGMFRTV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14919 553 GQLYKEQLAKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILTP 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 777 NVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14919 633 NSIPKGFMDGKQACVLMIKALELDSNLYRIGQSKVFFR 670
|
|
| MYSc_Myh14_mammals |
cd14930 |
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ... |
145-814 |
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: 984.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14930 1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASkPKGSGAVPHPavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14930 81 ESGAGKTENTKKVIQYLAHVASS-PKGRKEPGVP----GELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGvDDYAEFQATVKSM 384
Cdd:cd14930 156 GYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPG-QERELFQETLESL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd14930 235 RVLGFSHEEITSMLRMVSAVLQFGNIVLKRERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd14930 315 KEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT-DFRGVA 620
Cdd:cd14930 395 LEQEEYQREGIPWTFLDFGLDLQPCIDLIERPAnppGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPrHLRDQA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQ-QALTDTQFGARTRKGMFRTVSH 698
Cdd:cd14930 475 DFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEgIVGLEQvSSLGDGPPGGRPRRGMFRTVGQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 699 LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV 778
Cdd:cd14930 555 LYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNA 634
|
650 660 670
....*....|....*....|....*....|....*.
gi 62471805 779 IPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14930 635 IPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFR 670
|
|
| MYSc_Myh19 |
cd15896 |
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ... |
145-814 |
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: 973.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd15896 1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKpKGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd15896 81 ESGAGKTENTKKVIQYLAHVASSH-KTKKDQNSLALSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd15896 160 GYIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQDKDLFTETMEAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd15896 240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKERHTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKAQT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd15896 320 QEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPG---GIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK-TDFRGVA 620
Cdd:cd15896 400 LEQEEYQREGIEWSFIDFGLDLQPCIDLIEKPAsppGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKpKKLKDEA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE-IVGMAQQALTDTQFGA-RTRKGMFRTVSH 698
Cdd:cd15896 480 DFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSELWKDVDrIVGLDKVSGMSEMPGAfKTRKGMFRTVGQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 699 LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV 778
Cdd:cd15896 560 LYKEQLSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILTPNA 639
|
650 660 670
....*....|....*....|....*....|....*.
gi 62471805 779 IPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd15896 640 IPKGFMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
82-1504 |
0e+00 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 872.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 82 VWVPHENQGFVAASI-KREHGDEVEVELA--ETGKRVMILRDDIQ--KMNPPKFDKVEDMAELTCLNEASVLHNIKDRYY 156
Cdd:COG5022 12 CWIPDEEKGWIWAEIiKEAFNKGKVTEEGkkEDGESVSVKKKVLGndRIKLPKFDGVDDLTELSYLNEPAVLHNLEKRYN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 157 SGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTENTKK 236
Cdd:COG5022 92 NGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLSEKENQTIIISGESGAGKTENAKR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 237 VIQFLAYVAASKPkgsgavphpaVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGFISGANIETYL 316
Cdd:COG5022 172 IMQYLASVTSSST----------VEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDENGEICGAKIETYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 317 LEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLP-VPGVDDYAEFQATVKSMNIMGMTSEDFN 395
Cdd:COG5022 242 LEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDkIDGIDDAKEFKITLDALKTIGIDEEEQD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 396 SIFRIVSAVLLFGSMKFRQERnNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAI 475
Cdd:COG5022 322 QIFKILAAILHIGNIEFKEDR-NGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIVVPLNLEQALAIRDSL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 476 AKACYERMFKWLVNRINRSLDRTKRQGaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGI 555
Cdd:COG5022 401 AKALYSNLFDWIVDRINKSLDHSAAAS-NFIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQFFNQHMFKLEQEEYVKEGI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 556 EWKFIDFgLDLQPTIDLIDK--PGGIMALLDEECWFPKATDKTFVDKLVSA--HSMHPKFMKTDFRGVAdFAIVHYAGRV 631
Cdd:COG5022 480 EWSFIDY-FDNQPCIDLIEKknPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKKSRFRDNK-FVVKHYAGDV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 632 DYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdtqfgARTRKGMFRTVSHLYKEQLAKLMDTL 711
Cdd:COG5022 558 EYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTLFDDEE---------------NIESKGRFPTLGSRFKESLNSLMSTL 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 712 RNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV----IPKGFMDGK 787
Cdd:COG5022 623 NSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPSKswtgEYTWKEDTK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 788 KACEKMIQALELDSNLYRVGQSKIFFRAGVLAHLEEERDFKISDLIVNFQAFCRGFLARRNYQKRLQQLNAIRIIQRNCA 867
Cdd:COG5022 703 NAVKSILEELVIDSSKYQIGNTKVFFKAGVLAALEDMRDAKLDNIATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFR 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 868 AYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKLDT--LAKNTQEYERKYQQA-LVEKTTLAEQLQAEIE 944
Cdd:COG5022 783 LRRLVDYELKWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKRekKLRETEEVEFSLKAEvLIQKFGRSLKAKKRFS 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 945 LcaeaeESRSRLMARKQELEDMMQELETRIEEEEERVLALGgekkklELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIK 1024
Cdd:COG5022 863 L-----LKKETIYLQSAQRVELAERQLQELKIDVKSISSLK------LVNLELESEIIELKKSLSSDLIENLEFKTELIA 931
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1025 KYEEDLALTDDQNQklLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELeerlhkdQQQRQESDRSKRKIe 1104
Cdd:COG5022 932 RLKKLLNNIDLEEG--PSIEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREG-------NKANSELKNFKKEL- 1001
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1105 TEVADLKEQLNERRVQVDEMQAQLAkreeELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaekaarakaekvr 1184
Cdd:COG5022 1002 AELSKQYGALQESTKQLKELPVEVA----ELQSASKIISSESTELSILKPLQKLKGLLLLENNQ---------------- 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1185 rdLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQ--LENLRKAK 1262
Cdd:COG5022 1062 --LQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQeiSKFLSQLV 1139
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1263 TVLEKAKGTLEAENADLATELRSVN----------------SSRQEN--DRRRKQAESQIAELQVKLAEIER---ARSEL 1321
Cdd:COG5022 1140 NTLEPVFQKLSVLQLELDGLFWEANlealpspppfaalsekRLYQSAlyDEKSKLSSSEVNDLKNELIALFSkifSGWPR 1219
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1322 QEKCTKLQQEAENITNQLEEAE-------LKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQ 1394
Cdd:COG5022 1220 GDKLKKLISEGWVPTEYSTSLKgfnnlnkKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFN 1299
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1395 ----------LEEDDEAKRNYERK--------LAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIA 1456
Cdd:COG5022 1300 alrtkasslrWKSATEVNYNSEELddwcrefeISDVDEELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPAEIQNLKS 1379
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1457 QNDRLDKS---KKKIQSELEDATIELEAQRTkVLELEKKQKNFDKILAEEK 1504
Cdd:COG5022 1380 RYDPADKEnnlPKEILKKIEALLIKQELQLS-LEGKDETEVHLSEIFSEEK 1429
|
|
| MYSc |
cd00124 |
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ... |
145-814 |
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: 856.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRH-EVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd00124 1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSaDLPPHVFAVADAAYRAMLRDGQNQSILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd00124 81 GESGAGKTETTKLVLKYLAALSGSGSSKSSSSAS------SIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL-----SNGSLPVPGVDDYAEFQ 378
Cdd:cd00124 155 TGRLVGASIETYLLEKSRVVSQAPGERNFHIFYQLLAGLSDGAREELKLELLLSYYYLndylnSSGCDRIDGVDDAEEFQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 379 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF--RQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 456
Cdd:cd00124 235 ELLDALDVLGFSDEEQDSIFRILAAILHLGNIEFeeDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGG 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 457 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQ-GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 535
Cdd:cd00124 315 ETITKPLTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDAAeSTSFIGILDIFGFENFEVNSFEQLCINYANEKLQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 536 QLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKT 614
Cdd:cd00124 395 QFFNQHVFKLEQEEYEEEGIDWSFIDF-PDNQDCLDLIEgKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 615 DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSqdpfvvniwkdaeivgmaqqaltdTQFgartrkgmfr 694
Cdd:cd00124 474 KRKAKLEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVDLLRSG------------------------SQF---------- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 695 tvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 774
Cdd:cd00124 520 ------RSQLDALMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRIL 593
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 62471805 775 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd00124 594 APGATEKASDSKKAAVLALLLLLKLDSSGYQLGKTKVFLR 633
|
|
| MYSc_Myh7b |
cd14927 |
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ... |
145-814 |
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: 785.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14927 1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLIG-ELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14927 81 ESGAGKTVNTKRVIQYFAIVAALGDGPGKKAQFLATKTGgTLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVK 382
Cdd:cd14927 161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPELQDMLLVSmNPYDYHFCSQGVTTVDNMDDGEELMATDH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 383 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKA 462
Cdd:cd14927 241 AMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQREEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGNEYVTKG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 463 QTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 542
Cdd:cd14927 321 QSVEQVVYAVGALAKATYDRMFKWLVSRINQTLD-TKLPRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 543 FILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMK----TDFR 617
Cdd:cd14927 400 FILEQEEYKREGIEWVFIDFGLDLQACIDLIEKPLGILSILEEECMFPKASDASFKAKLYDNHlGKSPNFQKprpdKKRK 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeIVGMAQQALTDTQFGARTRKGM-FRTV 696
Cdd:cd14927 480 YEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQNKLLATLYEN--YVGSDSTEDPKSGVKEKRKKAAsFQTV 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14927 558 SQLHKENLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADFKQRYRILNP 637
|
650 660 670
....*....|....*....|....*....|....*....
gi 62471805 777 NVIPK-GFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14927 638 SAIPDdKFVDSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
|
|
| MYSc_Myh1_insects_crustaceans |
cd14909 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
145-814 |
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: 782.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14909 1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKgsgavPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14909 81 ESGAGKTENTKKVIAYFATVGASKKT-----DEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQATVKS 383
Cdd:cd14909 156 GKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKEMCLLsDNIYDYYIVSQGKVTVPNVDDGEEFSLTDQA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14909 236 FDILGFTKQEKEDVYRITAAVMHMGGMKFKQRGREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14909 316 NVQQVTNSIGALCKGVFDRLFKWLVKKCNETLD-TQQKRQHFIGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFFNHHMF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTD----FRG 618
Cdd:cd14909 395 VLEQEEYKREGIDWAFIDFGMDLLACIDLIEKPMGILSILEEESMFPKATDQTFSEKLTNTHlGKSAPFQKPKppkpGQQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 619 VADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTRKGM-FRTVS 697
Cdd:cd14909 475 AAHFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA----GQSGGGEQAKGGRGKKGGgFATVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14909 551 SAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKILNPA 630
|
650 660 670
....*....|....*....|....*....|....*..
gi 62471805 778 VIpKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14909 631 GI-QGEEDPKKAAEIILESIALDPDQYRLGHTKVFFR 666
|
|
| MYSc_Myh3 |
cd14913 |
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ... |
146-814 |
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: 780.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14913 2 AVLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14913 82 SGAGKTVNTKRVIQYFATIAAT---GDLAKKKDSKMKGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKF-ILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14913 159 KLASADIETYLLEKSRVTFQLKAERSYHIFYQILSNKKPELIELLlITTNPYDYPFISQGEILVASIDDAEELLATDSAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14913 239 DILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14913 318 TVDQVHHAVNALSKSVYEKLFLWMVTRINQQLD-TKLPRQHFIGVLDIAGFEIFEYNSLEQLCINFTNEKLQQFFNHHMF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMKTdfR 617
Cdd:cd14913 397 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYdqhlgkSNNFQKPKVVKG--R 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTRKGMFRTVS 697
Cdd:cd14913 475 AEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKSSNRLLAHLYATFA----TADADSGKKKVAKKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14913 551 ALFRENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNAS 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14913 631 AIPEGqFIDSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh16 |
cd14934 |
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ... |
145-814 |
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: 744.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14934 1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14934 81 ESGAGKTENTKKVIQYFANIGGTGKQSSDGK-------GSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQATVKS 383
Cdd:cd14934 154 GKLAGADIESYLLEKSRVISQQAAERGYHIFYQILSNKKPELIESLLLvPNPKEYHWVSQGVTVVDNMDDGEELQITDVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14934 234 FDVLGFSAEEKIGVYKLTGGIMHFGNMKFKQKPREEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14934 314 NMEQCNNSIGALGKAVYDKMFKWLVVRINKTLD-TKMQRQFFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFNHHMF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH-SMHPKFMKTDF-RGV-- 619
Cdd:cd14934 393 VLEQEEYKREGIEWVFIDFGLDLQACIDLLEKPMGIFSILEEQCVFPKATDATFKAALYDNHlGKSSNFLKPKGgKGKgp 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 620 -ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAQQaltdtqfgaRTRKGMFRTVSH 698
Cdd:cd14934 473 eAHFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQKSSLGLLALLFKEEEAPAGSKK---------QKRGSSFMTVSN 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 699 LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV 778
Cdd:cd14934 544 FYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLNPNV 623
|
650 660 670
....*....|....*....|....*....|....*.
gi 62471805 779 IPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14934 624 IPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
|
|
| MYSc_Myh15_mammals |
cd14929 |
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ... |
145-814 |
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: 733.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14929 1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAAskpkgsgaVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14929 81 ESGAGKTVNTKHIIQYFATIAA--------MIESKKKLGALEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14929 153 GMLSSADIDIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAEELLATEQAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd14929 233 DILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd14929 313 IEQVTYAVGALSKSIYERMFKWLVARINRVLD-AKLSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMKTDFRg 618
Cdd:cd14929 392 LEQEEYRKEGIDWVSIDFGLDLQACIDLIEKPMGIFSILEEECMFPKATDLTFKTKLFdnhfgkSVHFQKPKPDKKKFE- 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 619 vADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqaltdTQFGARTRK--GMFRTV 696
Cdd:cd14929 471 -AHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYISTDSA------IQFGEKKRKkgASFQTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14929 544 ASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNP 623
|
650 660 670
....*....|....*....|....*....|....*....
gi 62471805 777 NVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14929 624 RTFPKSkFVSSRKAAEELLGSLEIDHTQYRFGITKVFFK 662
|
|
| MYSc_Myh7 |
cd14917 |
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ... |
146-814 |
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: 720.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14917 2 AVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14917 82 SGAGKTVNTKRVIQYFAVIAAI---GDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14917 159 KLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLItNNPYDYAFISQGETTVASIDDAEELMATDNAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14917 239 DVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQREEQAE-PDGTEeADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14917 318 NVQQVIYATGALAKAVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMKTdfR 617
Cdd:cd14917 397 VLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFdnhlgkSNNFQKPRNIKG--K 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTRKGMFRTVS 697
Cdd:cd14917 475 PEAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYA----GADAPIEKGKGKAKKGSSFQTVS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14917 551 ALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 630
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14917 631 AIPEGqFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
|
|
| MYSc_Myh6 |
cd14916 |
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ... |
146-814 |
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: 704.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14916 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14916 82 SGAGKTVNTKRVIQYFASIAAIGDRSKKENPNANK--GTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIL-DDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14916 160 KLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVtNNPYDYAFVSQGEVSVASIDDSEELLATDSAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNTV-AQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14916 240 DVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAE-PDGTEdADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14916 319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLE-TKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMKTdfR 617
Cdd:cd14916 398 VLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKASDMTFKAKLYdnhlgkSNNFQKPRNVKG--K 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeiVGMAQQALTDTQFGARTRKGMFRTVS 697
Cdd:cd14916 476 QEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFST---YASADTGDSGKGKGGKKKGSSFQTVS 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14916 553 ALHRENLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPA 632
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14916 633 AIPEGqFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
|
|
| MYSc_Myh1_mammals |
cd14910 |
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ... |
146-814 |
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: 697.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14910 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLiGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14910 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEATSGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14910 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14910 241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14910 320 TVQQVYNAVGALAKAVYDKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH------SMHPKFMKTDFR 617
Cdd:cd14910 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksnnFQKPKPAKGKVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 gvADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgMAQQALTDTQFGARTRKGMFRTVS 697
Cdd:cd14910 479 --AHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSMKTLALLFSGAA---AAEAEEGGGKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14910 554 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14910 634 AIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myh8 |
cd14918 |
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ... |
147-814 |
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: 693.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 147 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGES 226
Cdd:cd14918 3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 227 GAGKTENTKKVIQFLAYVAASkpkGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGF 306
Cdd:cd14918 83 GAGKTVNTKRVIQYFATIAVT---GEKKKEESGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 307 ISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVKSMN 385
Cdd:cd14918 160 LASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPDLIEMLLITtNPYDYAFVSQGEITVPSIDDQEELMATDSAID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 386 IMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd14918 240 ILGFTPEEKVSIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd14918 319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMKTdfRG 618
Cdd:cd14918 398 LEQEEYKKEGIEWTFIDFGMDLAACIELIEKPLGIFSILEEECMFPKATDTSFKNKLYdqhlgkSANFQKPKVVKG--KA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 619 VADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmAQQALTDTQFGARTRKGMFRTVSH 698
Cdd:cd14918 476 EAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQKSAMKTLASLFSTYA----SAEADSGAKKGAKKKGSSFQTVSA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 699 LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV 778
Cdd:cd14918 552 LFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLNASA 631
|
650 660 670
....*....|....*....|....*....|....*..
gi 62471805 779 IPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14918 632 IPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
|
|
| MYSc_Myh2_mammals |
cd14912 |
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ... |
146-814 |
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: 691.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14912 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLiGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14912 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEITSGKMQ-GTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14912 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQITSNKKPELIEMLLITtNPYDYPFVSQGEISVASIDDQEELMATDSAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14912 241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQREEQAE-PDGTeVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14912 320 TVEQVTNAVGALAKAVYEKMFLWMVARINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLV------SAHSMHPKFMKTdfR 617
Cdd:cd14912 399 VLEQEEYKKEGIEWTFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYeqhlgkSANFQKPKVVKG--K 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEiVGMAQQALTDTQFGARTRKGMFRTVS 697
Cdd:cd14912 477 AEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLFSGAQ-TAEGASAGGGAKKGGKKKGSSFQTVS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14912 556 ALFRENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNAS 635
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14912 636 AIPEGqFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
|
|
| MYSc_Myh13 |
cd14923 |
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ... |
146-814 |
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: 688.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14923 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAvpHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14923 82 SGAGKTVNTKRVIQYFATIAVTGDKKKEQ--QPGKMQGTLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14923 160 KLASADIETYLLEKSRVTFQLSSERSYHIFYQIMSNKKPELIDLLLIStNPFDFPFVSQGEVTVASIDDSEELLATDNAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14923 240 DILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVTKGQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14923 319 NVQQVTNSVGALAKAVYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH------SMHPKFMKTdfR 617
Cdd:cd14923 398 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgksnnFQKPKPAKG--K 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeIVGMAQQALTDTQFGARTRKGMFRTVS 697
Cdd:cd14923 476 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSSLKLLSFLFSN--YAGAEAGDSGGSKKGGKKKGSSFQTVS 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14923 554 AVFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNAS 633
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14923 634 AIPEGqFIDSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
|
|
| MYSc_Myo5 |
cd01380 |
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ... |
146-814 |
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: 682.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSG-LIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01380 2 AVLHNLKVRFCQRnAIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd01380 82 ESGAGKTVSAKYAMRYFATVGGSSSGET-----------QVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLP-VPGVDDYAEFQATVKS 383
Cdd:cd01380 151 YRIIGANMRTYLLEKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPvIDGVDDAAEFEETRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd01380 231 LTLLGISEEEQMEIFRILAAILHLGNVEIKATRNDSASISPDDEHLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGA-SFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTM 542
Cdd:cd01380 311 TLQQAIVARDALAKHIYAQLFDWIVDRINKALASPVKEKQhSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 543 FILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK--FMKTDFRGVA 620
Cdd:cd01380 391 FKLEQEEYVKEEIEWSFIDF-YDNQPCIDLIEGKLGILDLLDEECRLPKGSDENWAQKLYNQHLKKPNkhFKKPRFSNTA 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 621 dFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDpfvvniwkdaeivgmaqqaltdtqfgartRKgmfRTVSHLY 700
Cdd:cd01380 470 -FIVKHFADDVEYQVEGFLEKNRDTVSEEHLNVLKASKN-----------------------------RK---KTVGSQF 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 701 KEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIP 780
Cdd:cd01380 517 RDSLILLMETLNSTTPHYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEW 596
|
650 660 670
....*....|....*....|....*....|....
gi 62471805 781 KGfMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd01380 597 LR-DDKKKTCENILENLILDPDKYQFGKTKIFFR 629
|
|
| MYSc_Myh4 |
cd14915 |
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ... |
146-814 |
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: 681.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14915 2 AVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVPhPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14915 82 SGAGKTVNTKRVIQYFATIAVTGEKKKEEAA-SGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14915 161 KLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITtNPYDFAFVSQGEITVPSIDDQEELMATDSAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATlPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQ 463
Cdd:cd14915 241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQREEQAE-PDGTeVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14915 320 TVQQVYNSVGALAKAIYEKMFLWMVTRINQQLD-TKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH------SMHPKFMKTdfR 617
Cdd:cd14915 399 VLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgksnnFQKPKPAKG--K 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGS---QDPFVVNIWKDAEIVGMAQQAltdtqfGARTRKGMFR 694
Cdd:cd14915 477 AEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSgmkTLAFLFSGGQTAEAEGGGGKK------GGKKKGSSFQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 695 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 774
Cdd:cd14915 551 TVSALFRENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVL 630
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 62471805 775 TPNVIPKG-FMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14915 631 NASAIPEGqFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
|
|
| MYSc_Myo22 |
cd14883 |
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ... |
146-814 |
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: 666.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14883 2 GINTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAaSKPKgsgavphpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14883 82 SGAGKTETTKLILQYLCAVT-NNHS-------------WVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGA--TPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQATVK 382
Cdd:cd14883 148 HIKGAIIQDYLLEQSRITFQAPGERNYHVFYQLLAGAkhSKELKEKLKLGEPEDYHYLNqSGCIRIDNINDKKDFDHLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 383 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ-ERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVgRDFVTK 461
Cdd:cd14883 228 AMNVLGIPEEMQEGIFSVLSAILHLGNLTFEDiDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINV-RGNVTE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 462 AQTK-EQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGaSFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 540
Cdd:cd14883 307 IPLKvQEARDNRDAMAKALYSRTFAWLVNHINSCTNPGQKNS-RFIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNH 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 541 TMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDK-PGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV 619
Cdd:cd14883 386 YVFKLEQEEYEKEGINWSHIVFT-DNQECLDLIEKpPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEKPDRRRW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 620 AD-FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWK--DAEIVGMAQQALTDTQFGARTRKGMfRTV 696
Cdd:cd14883 465 KTeFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKELFTypDLLALTGLSISLGGDTTSRGTSKGK-PTV 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14883 544 GDTFKHQLQSLVDVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDP 623
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 777 NVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14883 624 RARSADHKETCGAVRALMGLGGLPEDEWQVGKTKVFLR 661
|
|
| MYSc_Myo1 |
cd01378 |
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ... |
146-814 |
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: 654.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd01378 2 AINENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQflaYVAASKPKGSGAVPHpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd01378 82 SGAGKTEASKRIMQ---YIAAVSGGSESEVER-------VKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGVDDYAEFQATVKSM 384
Cdd:cd01378 152 EPVGGHITNYLLEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKsGCFDVDGIDDAADFKEVLNAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRI----KVGRDFVT 460
Cdd:cd01378 232 KVIGFTEEEQDSIFRILAAILHLGNIQF-AEDEEGNAAISDTSVLDFVAYLLGVDPDQLEKA-LTHRTietgGGGRSVYE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 461 KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNH 540
Cdd:cd01378 310 VPLNVEQAAYARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKVIGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 541 TMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFP-KATDKTFVDKLVSAHSMHPKFM--KTDF 616
Cdd:cd01378 390 LTLKAEQEEYVREGIEWTPIKY-FNNKIICDLIEeKPPGIFAILDDACLTAgDATDQTFLQKLNQLFSNHPHFEcpSGHF 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 617 R-GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmaqqaltdtqfgaRTRKGMFRT 695
Cdd:cd01378 469 ElRRGEFRIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSLFPEGVD---------------LDSKKRPPT 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 696 VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLT 775
Cdd:cd01378 534 AGTKFKNSANALVETLMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLS 613
|
650 660 670
....*....|....*....|....*....|....*....
gi 62471805 776 PNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd01378 614 PKTWPAWDGTWQGGVESILKDLNIPPEEYQMGKTKIFIR 652
|
|
| MYSc_Myo11 |
cd01384 |
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ... |
145-814 |
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: 648.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd01384 1 PGVLHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAasKPKGSGAVPhpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd01384 81 GESGAGKTETTKMLMQYLAYMG--GRAVTEGRS--------VEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQATVK 382
Cdd:cd01384 151 AGRISGAAIRTYLLERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNqSKCFELDGVDDAEEYRATRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 383 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPD---NTVAQKIAHLLGLSVTDMTRAfLTPRIKVGRD-F 458
Cdd:cd01384 231 AMDVVGISEEEQDAIFRVVAAILHLGNIEFSKGEEDDSSVPKDeksEFHLKAAAELLMCDEKALEDA-LCKRVIVTPDgI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 459 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 538
Cdd:cd01384 310 ITKPLDPDAATLSRDALAKTIYSRLFDWLVDKINRSIGQDPNS-KRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHF 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 539 NHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDfR 617
Cdd:cd01384 389 NQHVFKMEQEEYTKEEIDWSYIEF-VDNQDVLDLIEkKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRFSKPK-L 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 618 GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdtqfGARTRKGM-FRTV 696
Cdd:cd01384 467 SRTDFTIDHYAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGLFPPLP--------------REGTSSSSkFSSI 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd01384 533 GSRFKQQLQELMETLNTTEPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAP 612
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 777 NViPKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 814
Cdd:cd01384 613 EV-LKGSDDEKAACKKILEKAGLKG--YQIGKTKVFLR 647
|
|
| MYSc_Myo8 |
cd01383 |
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ... |
146-814 |
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: 647.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKgiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd01383 2 SVLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAYR--QKLLDSPHVYAVADTAYREMMRDEINQSIIISGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAAskpkGSGAVphpavligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd01383 80 SGAGKTETAKIAMQYLAALGG----GSSGI----------ENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd01383 146 KICGAKIQTYLLEKSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNqSNCLTIDGVDDAKKFHELKEAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd01383 226 DTVGISKEDQEHIFQMLAAVLWLGNISFQVIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd01383 306 LQQAIDARDALAKAIYASLFDWLVEQINKSLEVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGvadFA 623
Cdd:cd01383 386 LEQEEYELDGIDWTKVDF-EDNQECLDLIEkKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGERGGA---FT 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 624 IVHYAGRVDYSAAKWLMKNMDPLNENIVSLLqGSQDPFVVNIWkdAEIVGMAQQALTdTQFGARTRKGMFRTVSHLYKEQ 703
Cdd:cd01383 462 IRHYAGEVTYDTSGFLEKNRDLLHSDLIQLL-SSCSCQLPQLF--ASKMLDASRKAL-PLTKASGSDSQKQSVATKFKGQ 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 704 LAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYE-LLTPNVIPKG 782
Cdd:cd01383 538 LFKLMQRLENTTPHFIRCIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGfLLPEDVSASQ 617
|
650 660 670
....*....|....*....|....*....|..
gi 62471805 783 fmDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd01383 618 --DPLSTSVAILQQFNILPEMYQVGYTKLFFR 647
|
|
| MYSc_Myo7 |
cd01381 |
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ... |
145-814 |
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: 639.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01381 1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVaaskpkgSGAvpHPAVligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd01381 81 ESGAGKTESTKLILQYLAAI-------SGQ--HSWI-----EQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-SLPVPGVDDYAEFQATVKS 383
Cdd:cd01381 147 GVIEGAKIEQYLLEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGnCLTCEGRDDAAEFADIRSA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ-ERNNDQAT-LPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTK 461
Cdd:cd01381 227 MKVLMFTDEEIWDIFKLLAAILHLGNIKFEAtVVDNLDASeVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 462 AQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAS--FIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 539
Cdd:cd01381 307 PLSAEQALDVRDAFVKGIYGRLFIWIVNKINSAIYKPRGTDSSrtSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 540 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRG 618
Cdd:cd01381 387 RHIFKLEQEEYDKEGINWQHIEF-VDNQDVLDLIaLKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYLKPKSDL 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 619 VADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeivgmaqqaltDTQFGARTRKGMfRTVSH 698
Cdd:cd01381 466 NTSFGINHFAGVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFNE------------DISMGSETRKKS-PTLSS 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 699 LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNV 778
Cdd:cd01381 533 QFRKSLDQLMKTLSACQPFFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVPGI 612
|
650 660 670
....*....|....*....|....*....|....*.
gi 62471805 779 IPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd01381 613 PPAHKTDCRAATRKICCAVLGGDADYQLGKTKIFLK 648
|
|
| MYSc_Myo4 |
cd14872 |
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ... |
145-814 |
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: 573.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14872 1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14872 81 ESGAGKTEATKQCLSFFAEVAGST--------------NGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKfiLDDVKSYAFLSNGS-LPVPGVDDYAEFQATVKS 383
Cdd:cd14872 147 GRICGASTENYLLEKSRVVYQIKGERNFHIFYQLLASPDPASRGG--WGSSAAYGYLSLSGcIEVEGVDDVADFEEVVLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQA---TLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKV-GRDFV 459
Cdd:cd14872 225 MEQLGFDDADINNVMSLIAAILKLGNIEFASGGGKSLVsgsTVANRDVLKEVATLLGVDAATLEEALTSRLMEIkGCDPT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 460 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 539
Cdd:cd14872 305 RIPLTPAQATDACDALAKAAYSRLFDWLVKKINESMRPQKGAKTTFIGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 540 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDK-PGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRG 618
Cdd:cd14872 385 QYTFKLEEALYQSEGVKFEHIDF-IDNQPVLDLIEKkQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRT 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 619 V-ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFvvniwkdaeIVGMAQQALTDTQFGARTRKGMFRtvs 697
Cdd:cd14872 464 SrTEFIVKHYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSKNKL---------IAVLFPPSEGDQKTSKVTLGGQFR--- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 hlykEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLtPN 777
Cdd:cd14872 532 ----KQLSALMTALNATEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFL-VK 606
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKGFM-DGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14872 607 TIAKRVGpDDRQRCDLLLKSLKQDFSKVQVGKTRVLYR 644
|
|
| MYSc_Myo6 |
cd01382 |
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ... |
145-814 |
0e+00 |
|
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276833 Cd Length: 649 Bit Score: 568.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd01382 1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAaskpkGSGAvphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd01382 81 GESGAGKTESTKYILRYLTESW-----GSGA--------GPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDdvksyaflsngslpvPGVDDYAEFQATVKS 383
Cdd:cd01382 148 KSSVVGGFVSHYLLEKSRICVQSKEERNYHIFYRLCAGAPEDLREKLLKD---------------PLLDDVGDFIRMDKA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN-------DQATLPDNTVAqkiAHLLGLSVTDM-----TRAFLTPR 451
Cdd:cd01382 213 MKKIGLSDEEKLDIFRVVAAVLHLGNIEFEENGSDsgggcnvKPKSEQSLEYA---AELLGLDQDELrvsltTRVMQTTR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 452 IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrqGASFIGILDMAGFEIFELNSFEQLCINYTN 531
Cdd:cd01382 290 GGAKGTVIKVPLKVEEANNARDALAKAIYSKLFDHIVNRINQCIPFET--SSYFIGVLDIAGFEYFEVNSFEQFCINYCN 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 532 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 610
Cdd:cd01382 368 EKLQQFFNERILKEEQELYEKEGLGVKEVEY-VDNQDCIDLIEaKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNHFR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 611 FMK------TDFRGVAD---FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGmaqqALTD 681
Cdd:cd01382 447 LSIprksklKIHRNLRDdegFLIRHFAGAVCYETAQFIEKNNDALHASLESLICESKDKFIRSLFESSTNNN----KDSK 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 682 TQFGartrKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNR 761
Cdd:cd01382 523 QKAG----KLSFISVGNKFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSR 598
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 762 IPFQEFRQRYELLTPNVIPKgfMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd01382 599 TSFHDLYNMYKKYLPPKLAR--LDPRLFCKALFKALGLNENDFKFGLTKVFFR 649
|
|
| MYSc_Myo15 |
cd01387 |
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ... |
145-814 |
2.68e-176 |
|
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: 551.67 E-value: 2.68e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01387 1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAaskpkgsgavPHPAVLIGEleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDaS 304
Cdd:cd01387 81 ESGSGKTEATKLIMQYLAAVN----------QRRNNLVTE---QILEATPLLEAFGNAKTVRNDNSSRFGKYLEVFFE-G 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-SLPVPGVDDYAEFQATVKS 383
Cdd:cd01387 147 GVIVGAITSQYLLEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGgNCEIAGKSDADDFRRLLAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKF--RQERN-NDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKVGR-DFV 459
Cdd:cd01387 227 MQVLGFSSEEQDSIFRILASVLHLGNVYFhkRQLRHgQEGVSVGSDAEIQWVAHLLQISPEGLQKA-LTFKVTETRrERI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 460 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINrSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 539
Cdd:cd01387 306 FTPLTIDQALDARDAIAKALYALLFSWLVTRVN-AIVYSGTQDTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFN 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 540 HTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFrG 618
Cdd:cd01387 385 KHVFKLEQEEYIREQIDWTEIAF-ADNQPVINLIsKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRM-P 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 619 VADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDaeivgMAQQALTDTQFGAR----TRKGMFR 694
Cdd:cd01387 463 LPEFTIKHYAGQVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHLFSS-----HRAQTDKAPPRLGKgrfvTMKPRTP 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 695 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 774
Cdd:cd01387 538 TVAARFQDSLLQLLEKMERCNPWFVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCL 617
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 62471805 775 TPNVIPKGfMDGKKACEKMIQALELD-SNLYRVGQSKIFFR 814
Cdd:cd01387 618 VALKLPRP-APGDMCVSLLSRLCTVTpKDMYRLGATKVFLR 657
|
|
| MYSc_Myo42 |
cd14903 |
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ... |
145-814 |
2.88e-174 |
|
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: 546.30 E-value: 2.88e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14903 1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAaskpkgsGAVPHPAVligeleQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14903 81 GESGAGKTETTKILMNHLATIA-------GGLNDSTI------KKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFlSNGSLPVPGVDDYAEFQATVKS 383
Cdd:cd14903 148 NGTLVGAKCRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTG-ANKTIKIEGMSDRKHFARTKEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATL--PDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTK 461
Cdd:cd14903 227 LSLIGVSEEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAiaPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 462 AQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHT 541
Cdd:cd14903 307 PLKKDQAEDCRDALAKAIYSNVFDWLVATINASLGNDAKM-ANHIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 542 MFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAH--SMH----PKFMKTd 615
Cdd:cd14903 386 VFKTVQIEYEEEGIRWAHIDF-ADNQDVLAVIEDRLGIISLLNDEVMRPKGNEESFVSKLSSIHkdEQDviefPRTSRT- 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 616 frgvaDFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKD-AEIVGMAQQALTDTQFGARTRKGMFR 694
Cdd:cd14903 464 -----QFTIKHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFKEkVESPAAASTSLARGARRRRGGALTTT 538
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 695 TVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 774
Cdd:cd14903 539 TVGTQFKDSLNELMTTIRSTNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLF 618
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 62471805 775 TPNViPKGFMDGKKACEKMIQALELDS-NLYRVGQSKIFFR 814
Cdd:cd14903 619 LPEG-RNTDVPVAERCEALMKKLKLESpEQYQMGLTRIYFQ 658
|
|
| MYSc_Myo40 |
cd14901 |
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ... |
145-812 |
1.10e-172 |
|
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: 542.07 E-value: 1.10e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY------KGIKRHEVPPHVFAITDSAYRNMLGDRE-- 216
Cdd:cd14901 1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDDETKEAYyehgerRAAGERKLPPHVYAVADKAFRAMLFASRgq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 217 --DQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVligelEQQLLQANPILEAFGNAKTVKNDNSSRFG 294
Cdd:cd14901 81 kcDQSILVSGESGAGKTETTKIIMNYLASVSSATTHGQNATERENV-----RDRVLESNPILEAFGNARTNRNNNSSRFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 295 KFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL--SNGSLPVPGVD 372
Cdd:cd14901 156 KFIRLGFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLnsSQCYDRRDGVD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 373 DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF-RQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPR 451
Cdd:cd14901 236 DSVQYAKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFvKKDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTRE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 452 IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAS-FIGILDMAGFEIFELNSFEQLCINYT 530
Cdd:cd14901 316 IRAGGEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESIAYSESTGASrFIGIVDIFGFEIFATNSLEQLCINFA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 531 NEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgldlqPTIDLI-----DKPGGIMALLDEECWFPKATDKTFVDKLVSAH 605
Cdd:cd14901 396 NEKLQQLFGKFVFEMEQDEYVAEAIPWTFVEY-----PNNDACvamfeARPTGLFSLLDEQCLLPRGNDEKLANKYYDLL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 606 SMHPKFMKTDF-RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNiwkdaeivgmaqqaltdtqf 684
Cdd:cd14901 471 AKHASFSVSKLqQGKRQFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFLSS-------------------- 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 685 gartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPF 764
Cdd:cd14901 531 ----------TVVAKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPH 600
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 765 QEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNL-----YRVGQSKIF 812
Cdd:cd14901 601 DAFVHTYSCLAPDGASDTWKVNELAERLMSQLQHSELNIehlppFQVGKTKVF 653
|
|
| MYSc_Myo29 |
cd14890 |
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ... |
145-814 |
2.03e-170 |
|
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: 535.90 E-value: 2.03e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAY----RNMLGDREDQS 219
Cdd:cd14890 1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYtqliQSGVLDPSNQS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 220 ILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAV-----LIGELEQQLLQANPILEAFGNAKTVKNDNSSRFG 294
Cdd:cd14890 81 IIISGESGAGKTEATKIIMQYLARITSGFAQGASGEGEAASeaieqTLGSLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 295 KFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY 374
Cdd:cd14890 161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYLRGECSSIPSCDDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 375 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErnNDQATLPDNTVAQ---KIAHLLGLSVTDMTRAFLTPR 451
Cdd:cd14890 241 KAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFESE--NDTTVLEDATTLQslkLAAELLGVNEDALEKALLTRQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 452 IKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQgASFIGILDMAGFEIFELNSFEQLCINYTN 531
Cdd:cd14890 319 LFVGGKTIVQPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDK-WGFIGVLDIYGFEKFEWNTFEQLCINYAN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 532 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLD--EECWFPKAT--DKTFVDKLVSAH- 605
Cdd:cd14890 398 EKLQRHFNQHMFEVEQVEYSNEGIDWQYITFN-DNQACLELIEgKVNGKPGIFItlDDCWRFKGEeaNKKFVSQLHASFg 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 606 ------------SMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQdpfvvniwkdaeivg 673
Cdd:cd14890 477 rksgsggtrrgsSQHPHFVHPKFDADKQFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSR--------------- 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 674 maqqaltdtqfgaRTRKGMfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRI 753
Cdd:cd14890 542 -------------RSIREV--SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMMEAIQI 606
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 754 CRQGFPNRIPFQEFRQRYELLTPNVipkgfMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14890 607 RQQGFALREEHDSFFYDFQVLLPTA-----ENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
|
|
| MYSc_Myo3 |
cd01379 |
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ... |
146-814 |
1.18e-166 |
|
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276830 [Multi-domain] Cd Length: 633 Bit Score: 524.53 E-value: 1.18e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd01379 2 TIVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKgsgavphpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd01379 82 SGAGKTESANLLVQQLTVLGKANNR-------------TLEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQR-EKFILDDVKSYAFLSNGSLPVPGV---DDYAE-FQAT 380
Cdd:cd01379 149 AVTGARISEYLLEKSRVVHQAIGERNFHIFYYIYAGLAEDKKlAKYKLPENKPPRYLQNDGLTVQDIvnnSGNREkFEEI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 381 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQ----ATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKVGR 456
Cdd:cd01379 229 EQCFKVIGFTKEEVDSVYSILAAILHIGDIEFTEVESNHQtdksSRISNPEALNNVAKLLGIEADELQEA-LTSHSVVTR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 457 -DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL--DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEK 533
Cdd:cd01379 308 gETIIRNNTVEEATDARDAMAKALYGRLFSWIVNRINSLLkpDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 534 LQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDK----LVSAHSMH 608
Cdd:cd01379 388 IQYYFNQHIFAWEQQEYLNEGIDVDLIEYE-DNRPLLDmFLQKPMGLLALLDEESRFPKATDQTLVEKfhnnIKSKYYWR 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 609 PKfmktdfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaQQaltdtqfgart 688
Cdd:cd01379 467 PK------SNALSFGIHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLV-------------RQ----------- 516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 689 rkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFR 768
Cdd:cd01379 517 ------TVATYFRYSLMDLLSKMVVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFL 590
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 62471805 769 QRYELLTPN----VIPKgfmdgKKACEKMIQALELDSnlYRVGQSKIFFR 814
Cdd:cd01379 591 KRYYFLAFKwneeVVAN-----RENCRLILERLKLDN--WALGKTKVFLK 633
|
|
| MYSc_Myo9 |
cd01385 |
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ... |
145-814 |
5.52e-164 |
|
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: 519.63 E-value: 5.52e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01385 1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAaSKPKGSGavphpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd01385 81 ESGSGKTESTNFLLHHLTALS-QKGYGSG-----------VEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYREN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQATVKS 383
Cdd:cd01385 149 GMVRGAVVEKYLLEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNqSDCYTLEGEDEKYEFERLKQA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNT-VAQKIAHLLGLSVTDMTRAFLTPRIK-VGRDFVT 460
Cdd:cd01385 229 MEMVGFLPETQRQIFSVLSAVLHLGNIEYKKKAyHRDESVTVGNPeVLDIISELLRVKEETLLEALTTKKTVtVGETLIL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 461 KAQTKEQVEfAVEAIAKACYERMFKWLVNRINRSL----DRTKRQGASfIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 536
Cdd:cd01385 309 PYKLPEAIA-TRDAMAKCLYSALFDWIVLRINHALlnkkDLEEAKGLS-IGVLDIFGFEDFGNNSFEQFCINYANEHLQY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 537 LFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD 615
Cdd:cd01385 387 YFNQHIFKLEQEEYKKEGISWHNIEY-TDNTGCLQLISkKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQ 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 616 FRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ----------DPFVVNIWKDAEIVGMAQQALTDTqfG 685
Cdd:cd01385 466 VMEPA-FIIAHYAGKVKYQIKDFREKNLDLMRPDIVAVLRSSSsafvreligiDPVAVFRWAVLRAFFRAMAAFREA--G 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 686 ARTRKG--------MFRTVSHL---------------YKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQL 742
Cdd:cd01385 543 RRRAQRtaghsltlHDRTTKSLlhlhkkkkppsvsaqFQTSLSKLMETLGQAEPFFIRCIKSNAEKKPLRFDDELVLRQL 622
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 743 RCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMiqalELDSNLYRVGQSKIFFR 814
Cdd:cd01385 623 RYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKL----NLDRDNYQIGKTKVFLK 690
|
|
| MYSc_Myo27 |
cd14888 |
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ... |
145-776 |
8.73e-164 |
|
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: 518.09 E-value: 8.73e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKgIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14888 1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIPgLYSDEMLLKFI-QPSISKSPHVFSTASSAYQGMCNNKKSQTILIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD- 302
Cdd:cd14888 80 GESGAGKTESTKYVMKFLACAGSEDIKKRSLV----------EAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSk 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 303 --------ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPV------ 368
Cdd:cd14888 150 lkskrmsgDRGRLCGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREAKNTGLSYEENDEKLAKGADAKPIsidmss 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 369 ------------------PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQ 430
Cdd:cd14888 230 fephlkfryltksschelPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNEACSEGAVVSASCTD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 431 ---KIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIG 507
Cdd:cd14888 310 dleKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDNSLLFCG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 508 ILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEE 586
Cdd:cd14888 390 VLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFP-DNQDCVDLLqEKPLGIFCMLDEE 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 587 CWFPKATDKTFVDKLVSAHSMHPKFM--KTDfrgVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVN 664
Cdd:cd14888 469 CFVPGGKDQGLCNKLCQKHKGHKRFDvvKTD---PNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISN 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 665 IWKdaeivgmaqqALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRC 744
Cdd:cd14888 546 LFS----------AYLRRGTDGNTKKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKY 615
|
650 660 670
....*....|....*....|....*....|..
gi 62471805 745 NGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14888 616 GGVLQAVQVSRAGYPVRLSHAEFYNDYRILLN 647
|
|
| MYSc_Myo36 |
cd14897 |
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ... |
145-814 |
1.37e-163 |
|
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: 516.17 E-value: 1.37e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKG-IKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14897 1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNlSVRSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAASKPkgsgavphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14897 81 GESGAGKTESTKYMIKHLMKLSPSDD-------------SDLLDKIVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAE------- 376
Cdd:cd14897 148 NGQLLGAKIDDYLLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILRDDNRNRPVFNDSEEleyyrqm 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 377 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGR 456
Cdd:cd14897 228 FHDLTNIMKLIGFSEEDISVIFTILAAILHLTNIVFIPDEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 457 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL----DRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNE 532
Cdd:cd14897 308 ERIQSWKSLRQANDSRDALAKDLYSRLFGWIVGQINRNLwpdkDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 533 KLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKF 611
Cdd:cd14897 388 RLQQYFNDYVFPRERSEYEIEGIEWRDIEYH-DNDDVLELFfKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRY 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 612 MKTdFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaqqaltdtqfgartrKG 691
Cdd:cd14897 467 VAS-PGNRVAFGIRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSNNEFI---------------------------SD 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 692 MFrtVSHlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 771
Cdd:cd14897 519 LF--TSY-FKRSLSDLMTKLNSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRY 595
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 62471805 772 ELLTPNViPKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 814
Cdd:cd14897 596 KEICDFS-NKVRSDDLGKCQKILKTAGIKG--YQFGKTKVFLK 635
|
|
| MYSc_Myo31 |
cd14892 |
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ... |
145-814 |
4.72e-163 |
|
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: 515.85 E-value: 4.72e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTE--KIMERYKGIKRHEV-PPHVFAITDSAYRNMLGDR----ED 217
Cdd:cd14892 1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPLLYDvpGFDSQRKEEATASSpPPHVFSIAERAYRAMKGVGkgqgTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 218 QSILCTGESGAGKTENTKKVIQFLAyvAASK-PKGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 296
Cdd:cd14892 81 QSIVVSGESGAGKTEASKYIMKYLA--TASKlAKGASTSKGAANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 297 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDDYA 375
Cdd:cd14892 159 IQIHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNcVEVDGVDDAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 376 EFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQ--KIAHLLGLSVTDMTRAFLTPRIK 453
Cdd:cd14892 239 EFKQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNvaKAAGLLGVDAAELMFKLVTQTTS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 454 VGRDFVTK-AQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQ---------GASFIGILDMAGFEIFELNSFE 523
Cdd:cd14892 319 TARGSVLEiKLTAREAKNALDALCKYLYGELFDWLISRINACHKQQTSGvtggaasptFSPFIGILDIFGFEIMPTNSFE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 524 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDK-PGGIMALLDEECWFP-KATDKTFVDKL 601
Cdd:cd14892 399 QLCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQ-DNQDCLDLIQKkPLGLLPLLEEQMLLKrKTTDKQLLTIY 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 602 VSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQgsqdpfvvniwkdaeivgmaqqaltd 681
Cdd:cd14892 478 HQTHLDKHPHYAKPRFECDEFVLRHYAGDVTYDVHGFLAKNNDNLHDDLRDLLR-------------------------- 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 682 tqfgaRTRKgmFRTvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNR 761
Cdd:cd14892 532 -----SSSK--FRT-------QLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIR 597
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 762 IPFQEFRQRYELLTPNVI-------PKGFMDGKKACEKMIQAlELDSNLYRVGQSKIFFR 814
Cdd:cd14892 598 RQFEEFYEKFWPLARNKAgvaaspdACDATTARKKCEEIVAR-ALERENFQLGRTKVFLR 656
|
|
| MYSc_Myo10 |
cd14873 |
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ... |
145-814 |
2.33e-162 |
|
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: 513.57 E-value: 2.33e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14873 1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14873 81 GESGAGKTESTKLILKFLSVISQQSLELSLKEKTSCV-----EQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPGVDDYAEFQATVK 382
Cdd:cd14873 156 KGNIQGGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNqSGCVEDKTISDQESFREVIT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 383 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrqeRNNDQATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKVGR-DFVTK 461
Cdd:cd14873 236 AMEVMQFSKEEVREVSRLLAGILHLGNIEF---ITAGGAQVSFKTALGRSAELLGLDPTQLTDA-LTQRSMFLRgEEILT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 462 AQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLdrTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHT 541
Cdd:cd14873 312 PLNVQQAVDSRDSLAMALYARCFEWVIKKINSRI--KGKEDFKSIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 542 MFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFrGVAD 621
Cdd:cd14873 390 IFSLEQLEYSREGLVWEDIDW-IDNGECLDLIEKKLGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRV-AVNN 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 622 FAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWkdaEIVGMAQQalTDTQFGARTRKGmfRTVSHLYK 701
Cdd:cd14873 468 FGVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDLF---EHVSSRNN--QDTLKCGSKHRR--PTVSSQFK 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 702 EQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPK 781
Cdd:cd14873 541 DSLHSLMATLSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRNLALP 620
|
650 660 670
....*....|....*....|....*....|...
gi 62471805 782 GFMDGKkaCEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14873 621 EDVRGK--CTSLLQLYDASNSEWQLGKTKVFLR 651
|
|
| MYSc_Myo46 |
cd14907 |
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ... |
145-814 |
1.01e-149 |
|
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276872 [Multi-domain] Cd Length: 669 Bit Score: 479.53 E-value: 1.01e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRH--------EVPPHVFAITDSAYRNMLGDR 215
Cdd:cd14907 1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQIIQngeyfdikKEPPHIYAIAALAFKQLFENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 216 EDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLIGEL------EQQLLQANPILEAFGNAKTVKNDN 289
Cdd:cd14907 81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSEEVLTLTSSIRATSkstksiEQKILSCNPILEAFGNAKTVRNDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 290 SSRFGKFIRINFD-ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS---YAFLS-NG 364
Cdd:cd14907 161 SSRFGKYVSILVDkKKRKILGARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQLSgdrYDYLKkSN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 365 SLPVPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNT-VAQKIAHLLGLSVTD 442
Cdd:cd14907 241 CYEVDTINDEKLFKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTlDDNSPCCVKNKeTLQIIAKLLGIDEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 443 MTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL-------DRTKRQGASFIGILDMAGFE 515
Cdd:cd14907 321 LKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTImpkdekdQQLFQNKYLSIGLLDIFGFE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 516 IFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKF--IDFgLDLQPTIDLIDK-PGGIMALLDEECWFPKA 592
Cdd:cd14907 401 VFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYLnqLSY-TDNQDVIDLLDKpPIGIFNLLDDSCKLATG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 593 TDKTFVDKLVSAHSMHPKFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAeiv 672
Cdd:cd14907 480 TDEKLLNKIKKQHKNNSKLIFPNKINKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSKNRIISSIFSGE--- 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 673 gmaQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIR 752
Cdd:cd14907 557 ---DGSQQQNQSKQKKSQKKDKFLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIR 633
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 753 ICRQGFPNRIPFQEFRQRYELLTPNVIpkgfmdgkkacekmiqaleldsnlyrVGQSKIFFR 814
Cdd:cd14907 634 VRKQGYPYRKSYEDFYKQYSLLKKNVL--------------------------FGKTKIFMK 669
|
|
| MYSc_Myo28 |
cd14889 |
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ... |
147-814 |
2.32e-149 |
|
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: 478.25 E-value: 2.32e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 147 VLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLG----DREDQSILC 222
Cdd:cd14889 3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLGrlarGPKNQCIVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 223 TGESGAGKTENTKKVIQFLAYVAaskpKGSGavphpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFd 302
Cdd:cd14889 83 SGESGAGKTESTKLLLRQIMELC----RGNS----------QLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 303 ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY-AEFQATV 381
Cdd:cd14889 148 RNGHVKGAKINEYLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWkKKYDEVC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 382 KSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrqERNNDQA---TLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKVGR-D 457
Cdd:cd14889 228 NAMDMVGFTEQEEVDMFTILAGILSLGNITF--EMDDDEAlkvENDSNGWLKAAAGQFGVSEEDLLKT-LTCTVTFTRgE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 458 FVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQG--ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 535
Cdd:cd14889 305 QIQRHHTKQQAEDARDSIAKVAYGRVFGWIVSKINQLLAPKDDSSveLREIGILDIFGFENFAVNRFEQACINLANEQLQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 536 QLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDL-IDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFmKT 614
Cdd:cd14889 385 YFFNHHIFLMEQKEYKKEGIDWKEITY-KDNKPILDLfLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYY-GK 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 615 DFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDP-----FVVNIWKDAEIVGMAQQALTDTQFGARTR 689
Cdd:cd14889 463 SRSKSPKFTVNHYAGKVTYNASGFLEKNRDTIPASIRTLFINSATPllsvlFTATRSRTGTLMPRAKLPQAGSDNFNSTR 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 690 KgmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 769
Cdd:cd14889 543 K---QSVGAQFKHSLGVLMEKMFAASPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAE 619
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 62471805 770 RYELLtpnVIPKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 814
Cdd:cd14889 620 RYKIL---LCEPALPGTKQSCLRILKATKLVG--WKCGKTRLFFK 659
|
|
| MYSc_Myo43 |
cd14904 |
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ... |
145-814 |
5.68e-142 |
|
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: 457.48 E-value: 5.68e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14904 1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavligeleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14904 81 GESGAGKTETTKIVMNHLASVAGGRKDKTIA-------------KVIDVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL--SNGSLPVPGVDDYAEFQATV 381
Cdd:cd14904 148 RGKLIGAKCETYLLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLgdSLAQMQIPGLDDAKLFASTQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 382 KSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQkIAHLLGLSVTDMTRAFLTPRIKVGRDFVTK 461
Cdd:cd14904 228 KSLSLIGLDNDAQRTLFKILSGVLHLGEVMFDKSDENGSRISNGSQLSQ-VAKMLGLPTTRIEEALCNRSVVTRNESVTV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 462 AQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHT 541
Cdd:cd14904 307 PLAPVEAEENRDALAKAIYSKLFDWMVVKINAAISTDDDRIKGQIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 542 MFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV-- 619
Cdd:cd14904 387 VFKTVEEEYIREGLQWDHIEYQ-DNQGIVEVIDGKMGIIALMNDHLRQPRGTEEALVNKIRTNHQTKKDNESIDFPKVkr 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 620 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaLTDTQFGARTRKGMF--RTVS 697
Cdd:cd14904 466 TQFIINHYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFGSSE--------APSETKEGKSGKGTKapKSLG 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 698 HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPN 777
Cdd:cd14904 538 SQFKTSLSQLMDNIKTTNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPP 617
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 778 VIPKGfmDGKKACEKMIQALELDSNL-YRVGQSKIFFR 814
Cdd:cd14904 618 SMHSK--DVRRTCSVFMTAIGRKSPLeYQIGKSLIYFK 653
|
|
| MYSc_Myo39 |
cd14900 |
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ... |
146-771 |
1.14e-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: 452.84 E-value: 1.14e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERY-------------KGikRHEVPPHVFAITDSAYRNM 211
Cdd:cd14900 2 TILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSDTMAKYllsfearssstrnKG--SDPMPPHIYQVAGEAYKAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 212 ----LGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLIGEleqQLLQANPILEAFGNAKTVKN 287
Cdd:cd14900 80 mlglNGVMSDQSILVSGESGSGKTESTKFLMEYLAQAGDNNLAASVSMGKSTSGIAA---KVLQTNILLESFGNARTLRN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 288 DNSSRFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIlddvksyaflsngslp 367
Cdd:cd14900 157 DNSSRFGKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARKRDM---------------- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 368 vpgvddyaeFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQK-------IAHLLGLSV 440
Cdd:cd14900 221 ---------YRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGQLKSDLAPSsiwsrdaAATLLSVDA 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 441 TDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRIN---RSLDRTKRQGAS-FIGILDMAGFEI 516
Cdd:cd14900 292 TKLEKALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNaflKMDDSSKSHGGLhFIGILDIFGFEV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 517 FELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDK 595
Cdd:cd14900 372 FPKNSFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFC-DNQDCVNLISqRPTGILSLIDEECVMPKGSDT 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 596 TFVDKLVSAHSMHPKFMKTDF-RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQgsqdpfvvniwkdaeivgm 674
Cdd:cd14900 451 TLASKLYRACGSHPRFSASRIqRARGLFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLFV------------------- 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 675 aqqalTDTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRIC 754
Cdd:cd14900 512 -----YGLQF----------------KEQLTTLLETLQQTNPHYVRCLKPNDLCKAGIYERERVLNQLRCNGVMEAVRVA 570
|
650
....*....|....*..
gi 62471805 755 RQGFPNRIPFQEFRQRY 771
Cdd:cd14900 571 RAGFPIRLLHDEFVARY 587
|
|
| MYSc_Myo30 |
cd14891 |
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ... |
145-814 |
3.51e-140 |
|
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276856 Cd Length: 645 Bit Score: 451.81 E-value: 3.51e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRyySGLI----YTYSGLFCVVVNPYKKLPiytEKIMERYKGIKRHEVPPHVFAITDSAYRNML---GDRED 217
Cdd:cd14891 1 AGILHNLEER--SKLDnqrpYTFMANVLIAVNPLRRLP---EPDKSDYINTPLDPCPPHPYAIAEMAYQQMClgsGRMQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 218 QSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVLIG-----ELEQQLLQANPILEAFGNAKTVKNDNSSR 292
Cdd:cd14891 76 QSIVISGESGAGKTETSKIILRFLTTRAVGGKKASGQDIEQSSKKRklsvtSLDERLMDTNPILESFGNAKTLRNHNSSR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 293 FGKFIRINFDASGF-ISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLS-NGSLPVPG 370
Cdd:cd14891 156 FGKFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNqSGCVSDDN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 371 VDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ----ERNNDQATLPDNTVAQKIAHLLGLSVTDMTRA 446
Cdd:cd14891 236 IDDAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEedtsEGEAEIASESDKEALATAAELLGVDEEALEKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 447 FLTPRIkVGRD--FVTKAQTKEQVeFAVEAIAKACYERMFKWLVNRINRSLDRtKRQGASFIGILDMAGFEIFEL-NSFE 523
Cdd:cd14891 316 ITQREI-VTRGetFTIKRNAREAV-YSRDAIAKSIYERLFLWIVQQINTSLGH-DPDPLPYIGVLDIFGFESFETkNDFE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 524 QLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLV 602
Cdd:cd14891 393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWP-DNRECLDLIaSKPNGILPLLDNEARNPNPSDAKLNETLH 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 603 SAHSMHPKFMKT---DFRGVadFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQdpfvvniwkdaeivgmaqqal 679
Cdd:cd14891 472 KTHKRHPCFPRPhpkDMREM--FIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASSA--------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 680 tdtqfgartrkgmfrtvshLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFP 759
Cdd:cd14891 529 -------------------KFSDQMQELVDTLEATRCNFIRCIKPNAAMKVGVFDNRYVVDQLRCSGILQTCEVLKVGLP 589
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 760 NRIPFQEFRQRY-ELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14891 590 TRVTYAELVDVYkPVLPPSVTRLFAENDRTLTQAILWAFRVPSDAYRLGRTRVFFR 645
|
|
| MYSc_Myo47 |
cd14908 |
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ... |
145-814 |
9.21e-139 |
|
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: 449.36 E-value: 9.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYK--GIKRHE-------VPPHVFAITDSAYRNML-GD 214
Cdd:cd14908 1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRqeGLLRSQgiespqaLGPHVFAIADRSYRQMMsEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 215 REDQSILCTGESGAGKTENTKKVIQFLAYVAAskpkGSGAVPHPAVLIGELE--QQLLQANPILEAFGNAKTVKNDNSSR 292
Cdd:cd14908 81 RASQSILISGESGAGKTESTKIVMLYLTTLGN----GEEGAPNEGEELGKLSimDRVLQSNPILEAFGNARTLRNDNSSR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 293 FGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKS--------YAFLSNG 364
Cdd:cd14908 157 FGKFIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDGITgglqlpneFHYTGQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 365 SLP-VPGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKI----AHLLGLS 439
Cdd:cd14908 237 GAPdLREFTDEDGLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEF-ESKEEDGAAEIAEEGNEKClarvAKLLGVD 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 440 VTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL--DRTKRQGASfIGILDMAGFEIF 517
Cdd:cd14908 316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSInwENDKDIRSS-VGVLDIFGFECF 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 518 ELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFP-KATDK 595
Cdd:cd14908 395 AHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFP-DNQDCLDTIQaKKKGILTMLDDECRLGiRGSDA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 596 TFVDKLVSA--------HSMHPKFMKTDF-RGVADFAIVHYAGRVDYSAAKWLM-KNMDPLNENIVSLLQGSQdpfvvni 665
Cdd:cd14908 474 NYASRLYETylpeknqtHSENTRFEATSIqKTKLIFAVRHFAGQVQYTVETTFCeKNKDEIPLTADSLFESGQ------- 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 666 wkdaeivgmaqqaltdtQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCN 745
Cdd:cd14908 547 -----------------QF----------------KAQLHSLIEMIEDTDPHYIRCIKPNDAAKPDLVTRKRVTEQLRYG 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 746 GVLEGIRICRQGFPNRIPFQEFRQRYELLTP----NVIPKGFM--DGKKACEKMI----------QALELDSNL----YR 805
Cdd:cd14908 594 GVLEAVRVARSGYPVRLPHKDFFKRYRMLLPlipeVVLSWSMErlDPQKLCVKKMckdlvkgvlsPAMVSMKNIpedtMQ 673
|
....*....
gi 62471805 806 VGQSKIFFR 814
Cdd:cd14908 674 LGKSKVFMR 682
|
|
| PTZ00014 |
PTZ00014 |
myosin-A; Provisional |
143-856 |
1.28e-137 |
|
myosin-A; Provisional
Pssm-ID: 240229 [Multi-domain] Cd Length: 821 Bit Score: 451.02 E-value: 1.28e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 143 NEASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHE-VPPHVFAITDSAYRNMLGDREDQSIL 221
Cdd:PTZ00014 108 NIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDAKDSDkLPPHVFTTARRALENLHGVKKSQTII 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 222 CTGESGAGKTENTKKVIQFLAyvaaSKPKGSGAvphpavliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 301
Cdd:PTZ00014 188 VSGESGAGKTEATKQIMRYFA----SSKSGNMD--------LKIQNAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLQL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 302 DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATV 381
Cdd:PTZ00014 256 GEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVKDFEEVM 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 382 KSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN---DQATLPDNT--VAQKIAHLLGLSVTDMTRAFLTPRIKVGR 456
Cdd:PTZ00014 336 ESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEGgltDAAAISDESleVFNEACELLFLDYESLKKELTVKVTYAGN 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 457 DFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGAsFIGILDMAGFEIFELNSFEQLCINYTNEKLQQ 536
Cdd:PTZ00014 416 QKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFKV-FIGMLDIFGFEVFKNNSLEQLFINITNEMLQK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 537 LFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTD 615
Cdd:PTZ00014 495 NFVDIVFERESKLYKDEGISTEELEY-TSNESVIDLLcGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNLKNNPKYKPAK 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 616 FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIV--GMAQQALTDTQFgartrkgmf 693
Cdd:PTZ00014 574 VDSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDLFEGVEVEkgKLAKGQLIGSQF--------- 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 694 rtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 773
Cdd:PTZ00014 645 -------LNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 774 LTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR---AGVLAHLEEERDFKISDLIVNFQAFCRGFLARRNYQ 850
Cdd:PTZ00014 718 LDLAVSNDSSLDPKEKAEKLLERSGLPKDSYAIGKTMVFLKkdaAKELTQIQREKLAAWEPLVSVLEALILKIKKKRKVR 797
|
....*.
gi 62471805 851 KRLQQL 856
Cdd:PTZ00014 798 KNIKSL 803
|
|
| MYSc_Myo14 |
cd14876 |
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ... |
145-812 |
1.30e-135 |
|
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: 439.42 E-value: 1.30e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRH-EVPPHVFAITDSAYRNMLGDREDQSILCT 223
Cdd:cd14876 1 PCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDAPDLtKLPPHVFYTARRALENLHGVNKSQTIIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAYvaaskpKGSGAVPHpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14876 81 GESGAGKTEATKQIMRYFAS------AKSGNMDL------RIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKS 383
Cdd:cd14876 149 EGGIRYGSVVAFLLEKSRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDVPGIDDVADFEEVLES 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNN---DQATL--PDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDF 458
Cdd:cd14876 229 LKSMGLTEEQIDTVFSIVSGVLLLGNVKITGKTEQgvdDAAAIsnESLEVFKEACSLLFLDPEALKRELTVKVTKAGGQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 459 VTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDrtKRQG-ASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQL 537
Cdd:cd14876 309 IEGRWTKDDAEMLKLSLAKAMYDKLFLWIIRNLNSTIE--PPGGfKNFMGMLDIFGFEVFKNNSLEQLFINITNEMLQKN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 538 FNHTMFILEQEEYQREGIEWKFIDFgLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF 616
Cdd:cd14876 387 FIDIVFERESKLYKDEGIPTAELEY-TSNAEVIDvLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFKPAKV 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 617 RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVG--MAQQALTDTQFGArtrkgmfr 694
Cdd:cd14876 466 DSNINFIVVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVVEKgkIAKGSLIGSQFLK-------- 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 695 tvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELL 774
Cdd:cd14876 538 --------QLESLMGLINSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFL 609
|
650 660 670
....*....|....*....|....*....|....*...
gi 62471805 775 TPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIF 812
Cdd:cd14876 610 DLGIANDKSLDPKVAALKLLESSGLSEDEYAIGKTMVF 647
|
|
| MYSc_Myo41 |
cd14902 |
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ... |
145-776 |
2.39e-135 |
|
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: 440.87 E-value: 2.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYK--------GIKRHEVPPHVFAITDSAYRNML-GD 214
Cdd:cd14902 1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLkPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 215 REDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHpAVLIGeleQQLLQANPILEAFGNAKTVKNDNSSRFG 294
Cdd:cd14902 81 RRNQSILVSGESGSGKTESTKFLMQFLTSVGRDQSSTEQEGSD-AVEIG---KRILQTNPILESFGNAQTIRNDNSSRFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 295 KFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL-----SNGSLPVP 369
Cdd:cd14902 157 KFIKIQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLnsygpSFARKRAV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 370 GVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVA---QKIAHLLGLSVTDMTRA 446
Cdd:cd14902 237 ADKYAQLYVETVRAFEDTGVGELERLDIFKILAALLHLGNVNFTAENGQEDATAVTAASRfhlAKCAELMGVDVDKLETL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 447 FLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD--------RTKRQGASFIGILDMAGFEIFE 518
Cdd:cd14902 317 LSSREIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRLSDEINyfdsavsiSDEDEELATIGILDIFGFESLN 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 519 LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFV 598
Cdd:cd14902 397 RNGFEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALS 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 599 DKLVSAHSmhpkfmktdfrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMAqqa 678
Cdd:cd14902 477 TKFYRYHG-----------GLGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVVVAIGADENRDSPG--- 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 679 lTDTQFGARTRKGMFRT--VSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQ 756
Cdd:cd14902 543 -ADNGAAGRRRYSMLRApsVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARH 621
|
650 660
....*....|....*....|
gi 62471805 757 GFPNRIPFQEFRQRYELLTP 776
Cdd:cd14902 622 GYSVRLAHASFIELFSGFKC 641
|
|
| MYSc_Myo35 |
cd14896 |
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ... |
145-814 |
7.69e-132 |
|
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: 428.43 E-value: 7.69e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14896 1 SSVLLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKGSGAvphpavligeleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDaS 304
Cdd:cd14896 81 HSGSGKTEAAKKIVQFLSSLYQDQTEDRLR-------------QPEDVLPILESFGHAKTILNANASRFGQVLRLHLQ-H 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNG-SLPVPGVDDYAEFQATVKS 383
Cdd:cd14896 147 GVIVGASVSHYLLETSRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGgACRLQGKEDAQDFEGLLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQ--ATLPDNTVAQKIAHLLGLSVTDMTRAfLTPRIKV---GRDF 458
Cdd:cd14896 227 LQGLGLCAEELTAIWAVLAAILQLGNICFSSSERESQevAAVSSWAEIHTAARLLQVPPERLEGA-VTHRVTEtpyGRVS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 459 vtkaqTKEQVEFAVEA---IAKACYERMFKWLVNRINRSLDRTKRQGA-SFIGILDMAGFEIFELNSFEQLCINYTNEKL 534
Cdd:cd14896 306 -----RPLPVEGAIDArdaLAKTLYSRLFTWLLKRINAWLAPPGEAESdATIGVVDAYGFEALRVNGLEQLCINLASERL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 535 QQLFNHTMFILEQEEYQREGIEWKFIDfGLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 613
Cdd:cd14896 381 QLFSSQTLLAQEEEECQRELLPWVPIP-QPPRESCLDLLvDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAK 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 614 TDFrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqqaltdTQFGARTRKGmf 693
Cdd:cd14896 460 PQL-PLPVFTVRHYAGTVTYQVHKFLNRNRDQLDPAVVEMLAQSQLQLVGSLFQEAE-----------PQYGLGQGKP-- 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 694 rTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 773
Cdd:cd14896 526 -TLASRFQQSLGDLTARLGRSHVYFIHCLNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGA 604
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 62471805 774 LTpNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14896 605 LG-SERQEALSDRERCGAILSQVLGAESPLYHLGATKVLLK 644
|
|
| MYSc_Myo18 |
cd01386 |
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ... |
145-814 |
2.34e-126 |
|
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: 414.40 E-value: 2.34e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd01386 1 SSVLHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKgsgavphpaVLIGEleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd01386 81 RSGSGKTTNCRHILEYLVTAAGSVGG---------VLSVE---KLNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSyaflSNGSLPVPGV------DDYAEFQ 378
Cdd:cd01386 149 GQLASASIQTLLLERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQLAE----SNSFGIVPLQkpedkqKAAAAFS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 379 ATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRA-F---------- 447
Cdd:cd01386 225 KLQAAMKTLGISEEEQRAIWSILAAIYHLGAAGATKAASAGRKQFARPEWAQRAAYLLGCTLEELSSAiFkhhlsggpqq 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 448 -LTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASfIGILDMAGFEIFELN------ 520
Cdd:cd01386 305 sTTSSGQESPARSSSGGPKLTGVEALEGFAAGLYSELFAAVVSLINRSLSSSHHSTSS-ITIVDTPGFQNPAHSgsqrga 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 521 SFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfIDFGLD---LQPTIDLIDK---------------PGGIMAL 582
Cdd:cd01386 384 TFEDLCHNYAQERLQLLFHERTFVAPLERYKQENVE---VDFDLPelsPGALVALIDQapqqalvrsdlrdedRRGLLWL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 583 LDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGVAD----FAIVHYAGR--VDYSAAKWLMK-NMDPLNENIVSLLQ 655
Cdd:cd01386 461 LDEEALYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSEgplqFVLGHLLGTnpVEYDVSGWLKAaKENPSAQNATQLLQ 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 656 GSQDpfvvniwkdaeivgmaqqaltdtQFGARTRKGMFRTVshlyKEQLAKLMDTLRNTNPNFVRCIIPNH--EKRAGK- 732
Cdd:cd01386 541 ESQK-----------------------ETAAVKRKSPCLQI----KFQVDALIDTLRRTGLHFVHCLLPQHnaGKDERSt 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 733 ---------IDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGF-----MDGKKACEKMIQALE 798
Cdd:cd01386 594 sspaagdelLDVPLLRSQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLGlnsevADERKAVEELLEELD 673
|
730
....*....|....*.
gi 62471805 799 LDSNLYRVGQSKIFFR 814
Cdd:cd01386 674 LEKSSYRIGLSQVFFR 689
|
|
| MYSc_Myo19 |
cd14880 |
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ... |
145-776 |
1.21e-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: 400.00 E-value: 1.21e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKR-HEVPPHVFAITDSAYRNMLGDRE--DQSI 220
Cdd:cd14880 1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAAPQpQKLKPHIFTVGEQTYRNVKSLIEpvNQSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 221 LCTGESGAGKTENTKKVIQFLAYVAASKpkgsgAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 300
Cdd:cd14880 81 VVSGESGAGKTWTSRCLMKFYAVVAASP-----TSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 301 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNgslPVPGVDDyAEFQAT 380
Cdd:cd14880 156 LNRAQQMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPN---PERNLEE-DCFEVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 381 VKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTV---AQKIAHLLGLSVTDMTRAFLTPRIKVGRD 457
Cdd:cd14880 232 REAMLHLGIDTPTQNNIFKVLAGLLHLGNIQFADSEDEAQPCQPMDDTkesVRTSALLLKLPEDHLLETLQIRTIRAGKQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 458 FVT--KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQ 535
Cdd:cd14880 312 QQVfkKPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTFIGLLDVYGFESFPENSLEQLCINYANEKLQ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 536 QLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKT-FVDKLVSAHSMHPKFMK 613
Cdd:cd14880 392 QHFVAHYLRAQQEEYAVEGLEWSFINYQ-DNQTCLDLIEgSPISICSLINEECRLNRPSSAAqLQTRIESALAGNPCLGH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 614 TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEivgmaqQALTDTQFGARTRKGMF 693
Cdd:cd14880 471 NKLSREPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------EEKTQEEPSGQSRAPVL 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 694 RTVSHlYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYEL 773
Cdd:cd14880 545 TVVSK-FKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVERYKL 623
|
...
gi 62471805 774 LTP 776
Cdd:cd14880 624 LRR 626
|
|
| MYSc_Myo34 |
cd14895 |
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ... |
146-814 |
1.11e-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: 398.94 E-value: 1.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNML-------GDREDQ 218
Cdd:cd14895 2 AFVDYLAQRYGVDQVYCRSGAVLIAVNPFKHIPGLYDLHKYREEMPGWTALPPHVFSIAEGAYRSLRrrlhepgASKKNQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 219 SILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAVlIGEleqQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 298
Cdd:cd14895 82 TILVSGESGAGKTETTKFIMNYLAESSKHTTATSSSKRRRAI-SGS---ELLSANPILESFGNARTLRNDNSSRFGKFVR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 299 INF-----DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDV--KSYAFLSNGSLPV--P 369
Cdd:cd14895 158 MFFeghelDTSLRMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLELLsaQEFQYISGGQCYQrnD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 370 GVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNND---------------QATLPDNTVAQK--- 431
Cdd:cd14895 238 GVRDDKQFQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFVASSEDEgeedngaasapcrlaSASPSSLTVQQHldi 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 432 IAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTK----------RQ 501
Cdd:cd14895 318 VSKLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASPQRQfalnpnkaanKD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 502 GASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDlQPTIDLID-KPGGIM 580
Cdd:cd14895 398 TTPCIAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDN-SVCLEMLEqRPSGIF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 581 ALLDEECWFPKATDKTFVDKLVSAHSMHPKFM--KTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ 658
Cdd:cd14895 477 SLLDEECVVPKGSDAGFARKLYQRLQEHSNFSasRTDQADVA-FQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTS 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 659 DPFVVNIWKDAEIVGMAQQALTdtQFGARTRKGMFRTVS--HLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAP 736
Cdd:cd14895 556 DAHLRELFEFFKASESAELSLG--QPKLRRRSSVLSSVGigSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMA 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 737 LVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgfmdGKKACEkmIQALELDSNLYR----VGQSKIF 812
Cdd:cd14895 634 KVSSQLRYGGVLKAVEIMRQSYPVRMKHADFVKQYRLLVA---------AKNASD--ATASALIETLKVdhaeLGKTRVF 702
|
..
gi 62471805 813 FR 814
Cdd:cd14895 703 LR 704
|
|
| MYSc_Myo25 |
cd14886 |
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ... |
145-814 |
1.82e-116 |
|
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: 385.01 E-value: 1.82e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKG--IKR---HEVPPHVFAITDSAYRNMLGDREDQ 218
Cdd:cd14886 1 AVVIDILRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRQadTSRgfpSDLPPHSYAVAQSALNGLISDGISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 219 SILCTGESGAGKTENTKKVIQFLAYVAASkpkGSGAVphpavligelEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIR 298
Cdd:cd14886 81 SCIVSGESGAGKTETAKQLMNFFAYGHST---SSTDV----------QSLILGSNPLLESFGNAKTLRNNNSSRFGKFIK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 299 INFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGS-LPVPGVDDYAEF 377
Cdd:cd14886 148 LLVGPDGGLKGGKITSYMLELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKcYDAPGIDDQKEF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 378 QATVKSMNIMgMTSEDFNSIFRIVSAVLLFGSMKFRQERNN---DQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKV 454
Cdd:cd14886 228 APVRSQLEKL-FSKNEIDSFYKCISGILLAGNIEFSEEGDMgviNAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 455 GRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINR--SLDRTKRQgasFIGILDMAGFEIFELNSFEQLCINYTNE 532
Cdd:cd14886 307 NNETIISPVTQAQAEVNIRAVAKDLYGALFELCVDTLNEiiQFDADARP---WIGILDIYGFEFFERNTYEQLLINYANE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 533 KLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDKPG-GIMALLDEECWFPKATDKTFVDKLVSaHSMHPKF 611
Cdd:cd14886 384 RLQQYFINQVFKSEIQEYEIEGIDHSMITFT-DNSNVLAVFDKPNlSIFSFLEEQCLIQTGSSEKFTSSCKS-KIKNNSF 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 612 MKTDfRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaQQALTDTQFGARTRKG 691
Cdd:cd14886 462 IPGK-GSQCNFTIVHTAATVTYNTEEFVDKNKHKLSVDILELLMGSTNPIV-------------NKAFSDIPNEDGNMKG 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 692 MFrtVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 771
Cdd:cd14886 528 KF--LGSTFQLSIDQLMKTLSATKSHFIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRN 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 62471805 772 ELLT--PNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14886 606 KILIshNSSSQNAGEDLVEAVKSILENLGIPCSDYRIGKTKVFLR 650
|
|
| MYSc_Myo13 |
cd14875 |
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ... |
145-814 |
3.36e-115 |
|
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: 381.85 E-value: 3.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYS-GLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGI-KRHEVPPHVFAITDSAYRNM-LGDREDQSIL 221
Cdd:cd14875 1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 222 CTGESGAGKTENTKKVIQFLAYVAASKPKGsgavPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 301
Cdd:cd14875 81 ISGESGSGKTENAKMLIAYLGQLSYMHSSN----TSQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKLYF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 302 D-ASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKF-ILDDVKSYAFLSNGSLPVP-GVD-----D 373
Cdd:cd14875 157 DpTSGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRrGVDgktldD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 374 YAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLtprIK 453
Cdd:cd14875 237 AHEFQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESD-QNDKAQIADETPFLTACRLLQLDPAKLRECFL---VK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 454 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLD-RTKRQGASFIGILDMAGFEIFELNSFEQLCINYTNE 532
Cdd:cd14875 313 SKTSLVTILANKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITpQGDCSGCKYIGLLDIFGFENFTRNSFEQLCINYANE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 533 KLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLID-KPGGIMALLDEECWFPKATDKTFVDKLVSA-HSMHPK 610
Cdd:cd14875 393 SLQNHYNKYTFINDEEECRREGIQIPKIEFP-DNSECVNMFDqKRTGIFSMLDEECNFKGGTTERFTTNLWDQwANKSPY 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 611 FMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaeivgmaqQALTDTQFGARTRK 690
Cdd:cd14875 472 FVLPKSTIPNQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFI--------------RTLLSTEKGLARRK 537
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 691 gmfRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 770
Cdd:cd14875 538 ---QTVAIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRY 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 771 YELLTPNVIPKGFMDGK--KACEKMIQALEldsNLYR-------VGQSKIFFR 814
Cdd:cd14875 615 FYLIMPRSTASLFKQEKysEAAKDFLAYYQ---RLYGwakpnyaVGKTKVFLR 664
|
|
| MYSc_Myo45 |
cd14906 |
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ... |
145-810 |
3.94e-114 |
|
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: 380.48 E-value: 3.94e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKR-HEVPPHVFAITDSAYRNMLGDREDQSILC 222
Cdd:cd14906 1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQnKSPIPHIYAVALRAYQSMVSEKKNQSIII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 223 TGESGAGKTENTKKVIQFLAYVAASKPKGSGAVPHPAvliGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFD 302
Cdd:cd14906 81 SGESGSGKTEASKTILQYLINTSSSNQQQNNNNNNNN---NSIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 303 ASGF-ISGANIETYLLEKSR-AIRQAKDERTFHIFYQLLAGATPEQREKFILD-DVKSYAFL--------------SNGS 365
Cdd:cd14906 158 SSDGkIDGASIETYLLEKSRiSHRPDNINLSYHIFYYLVYGASKDERSKWGLNnDPSKYRYLdarddvissfksqsSNKN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 366 LPVPGVDDYAE-FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQ---KIAHLLGLSVT 441
Cdd:cd14906 238 SNHNNKTESIEsFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDFSKYAYQKDKVTAsleSVSKLLGYIES 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 442 DMTRAFLTPRIKVGRDFVTKAQTKE--QVEFAVEAIAKACYERMFKWLVNRINRSLDR----------TKRQGASFIGIL 509
Cdd:cd14906 318 VFKQALLNRNLKAGGRGSVYCRPMEvaQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqsndlaggSNKKNNLFIGVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 510 DMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPG-GIMALLDEECW 588
Cdd:cd14906 398 DIFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNF-IDNKECIELIEKKSdGILSLLDDECI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 589 FPKATDKTFVDKLVSA-HSMHPKFMKTDFRGVadFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWK 667
Cdd:cd14906 477 MPKGSEQSLLEKYNKQyHNTNQYYQRTLAKGT--LGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASSNFLKKSLFQ 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 668 daeivgmaQQALTDTQFGARTRKGMfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGV 747
Cdd:cd14906 555 --------QQITSTTNTTKKQTQSN--TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGV 624
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 748 LEGIRICRQGFPNRIPFQEFRQRYELLTPNVIPKGFMDGKKACEKMIQALELDSNLYRVGQSK 810
Cdd:cd14906 625 LNTIKVRKMGYSYRRDFNQFFSRYKCIVDMYNRKNNNNPKLASQLILQNIQSKLKTMGISNNK 687
|
|
| MYSc_Myo38 |
cd14899 |
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ... |
145-771 |
3.21e-106 |
|
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: 357.48 E-value: 3.21e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKgiKRHEVP------------PHVFAITDSAYRNM 211
Cdd:cd14899 1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYA--YDHNSQfgdrvtstdprePHLFAVARAAYIDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 212 LGDREDQSILCTGESGAGKTENTKKVIQFLAYVAAS----KPKGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKN 287
Cdd:cd14899 79 VQNGRSQSILISGESGAGKTEATKIIMTYFAVHCGTgnnnLTNSESISPPASPSRTTIEEQVLQSNPILEAFGNARTVRN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 288 DNSSRFGKFIRINF-DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAG----ATPEQREKFILDDVKSYAFLS 362
Cdd:cd14899 159 DNSSRFGKFIELRFrDERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGGPQSFRLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 363 NGSLPVP---GVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQ--ERNNDQATLPDNTVAQ------- 430
Cdd:cd14899 239 NQSLCSKrrdGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQipHKGDDTVFADEARVMSsttgafd 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 431 ---KIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRT--------- 498
Cdd:cd14899 319 hftKAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLQRQasapwgade 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 499 -----KRQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLI 573
Cdd:cd14899 399 sdvddEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFP-NNRACLELF 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 574 D-KPGGIMALLDEECWFPKATDKTFVDKL---VSAHSMHPKFMKTD-FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNE 648
Cdd:cd14899 478 EhRPIGIFSLTDQECVFPQGTDRALVAKYyleFEKKNSHPHFRSAPlIQRTTQFVVAHYAGCVTYTIDGFLAKNKDSFCE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 649 NIVSLLQGSQDPFVVNIWKDAEIVGMAQQALTDTQFGARTRKGMFRT----VSHLYKEQLAKLMDTLRNTNPNFVRCIIP 724
Cdd:cd14899 558 SAAQLLAGSSNPLIQALAAGSNDEDANGDSELDGFGGRTRRRAKSAIaavsVGTQFKIQLNELLSTVRATTPRYVRCIKP 637
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 62471805 725 NHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 771
Cdd:cd14899 638 NDSHVGSLFQSTRVVEQLRSGGVLEAVRVARAGFPVRLTHKQFLGRY 684
|
|
| MYSc_Myo17 |
cd14879 |
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ... |
142-813 |
3.77e-104 |
|
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: 349.16 E-value: 3.77e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 142 LNEASVLHNIKDRYYSGLIYTY---SGLfcVVVNPYKKLPIYTEKIMERYK-------GIKRHEVPPHVFAITDSAYRNM 211
Cdd:cd14879 1 PSDDAITSHLASRFRSDLPYTRlgsSAL--VAVNPYKYLSSNSDASLGEYGseyydttSGSKEPLPPHAYDLAARAYLRM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 212 LGDREDQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSgavphpavligELEQQLLQANPILEAFGNAKTVKNDNSS 291
Cdd:cd14879 79 RRRSEDQAVVFLGETGSGKSESRRLLLRQLLRLSSHSKKGT-----------KLSSQISAAEFVLDSFGNAKTLTNPNAS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 292 RFGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFL-SNGSLPV-- 368
Cdd:cd14879 148 RFGRYTELQFNERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLaSYGCHPLpl 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 369 -PGVDDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQER-NNDQATLPDNT-VAQKIAHLLGLSVTDMTR 445
Cdd:cd14879 228 gPGSDDAEGFQELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHeGGEESAVVKNTdVLDIVAAFLGVSPEDLET 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 446 AfLTPRIK-VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASFIGILDMAGFEIF---ELNS 521
Cdd:cd14879 308 S-LTYKTKlVRKELCTVFLDPEGAAAQRDELARTLYSLLFAWVVETINQKLCAPEDDFATFISLLDFPGFQNRsstGGNS 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 522 FEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEwkfidfgLDLQPTID-------LIDKPGGIMALLDEEC-WFPKAT 593
Cdd:cd14879 387 LDQFCVNFANERLHNYVLRSFFERKAEELEAEGVS-------VPATSYFDnsdcvrlLRGKPGGLLGILDDQTrRMPKKT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 594 DKTFVDKLVSAHSMHPKF----MKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSqdpfvvniwkda 669
Cdd:cd14879 460 DEQMLEALRKRFGNHSSFiavgNFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA------------ 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 670 eivgmaqqaltdTQFgartrkgmfrtvshlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLE 749
Cdd:cd14879 528 ------------TQL----------------NAALSELLDTLDRTRLWSVFCIRPNDSQLPNSFDKRRVKAQIRSLGLPE 579
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 750 GIRICRQGFPNRIPFQEFRQRYELLTPnvipkgFMDGKKACEKMIQALELDSNLYRVGQSKIFF 813
Cdd:cd14879 580 LAARLRVEYVVSLEHAEFCERYKSTLR------GSAAERIRQCARANGWWEGRDYVLGNTKVFL 637
|
|
| MYSc_Myo37 |
cd14898 |
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ... |
146-776 |
3.02e-95 |
|
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: 321.08 E-value: 3.02e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKlpIYTEKIMERYKGIKRHeVPPHVFAITDSAYRNmLGDREDQSILCTGE 225
Cdd:cd14898 2 ATLEILEKRYASGKIYTKSGLVFLALNPYET--IYGAGAMKAYLKNYSH-VEPHVYDVAEASVQD-LLVHGNQTIVISGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKgsgavphpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDasG 305
Cdd:cd14898 78 SGSGKTENAKLVIKYLVERTASTTS--------------IEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKFD--G 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFIldDVKSYAflSNGSLPVPGVDDYaefQATVKSMN 385
Cdd:cd14898 142 KITGAKFETYLLEKSRVTHHEKGERNFHIFYQFCASKRLNIKNDFI--DTSSTA--GNKESIVQLSEKY---KMTCSAMK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 386 IMGMTSedFNSIFRIVSAVLLFGSMKFrqerNNDQAT-LPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQT 464
Cdd:cd14898 215 SLGIAN--FKSIEDCLLGILYLGSIQF----VNDGILkLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 465 KEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTkrqGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFI 544
Cdd:cd14898 289 LKQARTIRNSMARLLYSNVFNYITASINNCLEGS---GERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFR 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 545 LEQEEYQREGIEWKFIDFgLDLQPTIDLIDKPGGIMALLDEECWFPKATDKTFvdkLVSAHSMHPKFMKTDFRGvaDFAI 624
Cdd:cd14898 366 AKQGMYKEEGIEWPDVEF-FDNNQCIRDFEKPCGLMDLISEESFNAWGNVKNL---LVKIKKYLNGFINTKARD--KIKV 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 625 VHYAGRVDYSAAKWLMKNMDplnenivsllQGSQDPFvvniwKDAEIVgmaqqaltdtqfgartRKGMFRTVSHLYKEQL 704
Cdd:cd14898 440 SHYAGDVEYDLRDFLDKNRE----------KGQLLIF-----KNLLIN----------------DEGSKEDLVKYFKDSM 488
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 705 AKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTP 776
Cdd:cd14898 489 NKLLNSINETQAKYIKCIRPNEECRPWCFDRDLVSKQLAECGILETIRLSKQCFPQEIPKDRFEERYRILGI 560
|
|
| MYSc_Myo24A |
cd14937 |
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
145-814 |
3.76e-95 |
|
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: 322.73 E-value: 3.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYtekiMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14937 1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFlaYVAASKPKGsgavphpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14937 77 ESGSGKTEASKLVIKY--YLSGVKEDN------------EISNTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVKSM 384
Cdd:cd14937 143 QNIVSSSIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAKDFGNLMISF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 385 NIMGMtSEDFNSIFRIVSAVLLFGSMKFRQERNNDQAT---LPDNT--VAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 459
Cdd:cd14937 223 DKMNM-HDMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNcseLDKNNleLVNEISNLLGINYENLKDCLVFTEKTIANQKI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 460 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFN 539
Cdd:cd14937 302 EIPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNK-ELNNYIGILDIFGFEIFSKNSLEQLLINIANEEIHSIYL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 540 HTMFILEQEEYQREGIEWKFIDFGLDlQPTIDLIDKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRGV 619
Cdd:cd14937 381 YIVYEKETELYKAEDILIESVKYTTN-ESIIDLLRGKTSIISILEDSCLGPVKNDESIVSVYTNKFSKHEKYASTKKDIN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 620 ADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIvgmaqqalTDTQfgarTRKGMfrtVSHL 699
Cdd:cd14937 460 KNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSLYEDVEV--------SESL----GRKNL---ITFK 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 700 YKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRIcRQGFPNRIPFQEFRQRYELLTPNVI 779
Cdd:cd14937 525 YLKNLNNIISYLKSTNIYFIKCIKPNENKEKNNFNQKKVFPQLFSLSIIETLNI-SFFFQYKYTFDVFLSYFEYLDYSTS 603
|
650 660 670
....*....|....*....|....*....|....*
gi 62471805 780 PKGFMDGKKACEKMIQAlELDSNLYRVGQSKIFFR 814
Cdd:cd14937 604 KDSSLTDKEKVSMILQN-TVDPDLYKVGKTMVFLK 637
|
|
| MYSc_Myo26 |
cd14887 |
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ... |
145-814 |
3.09e-93 |
|
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: 320.06 E-value: 3.09e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYS--------GLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDRE 216
Cdd:cd14887 1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 217 DQSILCTGESGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 296
Cdd:cd14887 81 SQSILISGESGAGKTETSKHVLTYLAAVSDRRHGADSQG---------LEARLLQSGPVLEAFGNAHTVLNANSSRFGKM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 297 IRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKfilddvksyaflsngSLPVPGVDDYAE 376
Cdd:cd14887 152 LLLHFTGRGKLTRASVATYLLANERVVRIPSDEFSFHIFYALCNAAVAAATQK---------------SSAGEGDPESTD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 377 FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNT--------VAQKIAHLL-------GLSVT 441
Cdd:cd14887 217 LRRITAAMKTVGIGGGEQADIFKLLAAILHLGNVEFTTDQEPETSKKRKLTsvsvgceeTAADRSHSSevkclssGLKVT 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 442 DMTRAFLT--------PRIKVGRDFVTKAQTKEQVE------------FAVEAIAKACYERMFKWLVNRINRSLDRTKR- 500
Cdd:cd14887 297 EASRKHLKtvarllglPPGVEGEEMLRLALVSRSVRetrsffdldgaaAARDAACKNLYSRAFDAVVARINAGLQRSAKp 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 501 ------------QGASFIGILDMAGFEIFE---LNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREG--IEWKFIDFG 563
Cdd:cd14887 377 sesdsdedtpstTGTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGvfQNQDCSAFP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 564 LDLQPTIDLIDKPGGIMALL------DEECWFPKATDKTFVDKLVSAHSMHPKFMKTDF--------------------- 616
Cdd:cd14887 457 FSFPLASTLTSSPSSTSPFSptpsfrSSSAFATSPSLPSSLSSLSSSLSSSPPVWEGRDnsdlfyeklnkniinsakykn 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 617 ------RGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDpfvvniwkdaeivgMAQQALTDTQFGARTRK 690
Cdd:cd14887 537 itpalsRENLEFTVSHFACDVTYDARDFCRANREATSDELERLFLACST--------------YTRLVGSKKNSGVRAIS 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 691 GMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQR 770
Cdd:cd14887 603 SRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVHRQLRCSGMSDLLRVMADGFPCRLPYVELWRR 682
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 62471805 771 YELLTPNVIpKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 814
Cdd:cd14887 683 YETKLPMAL-REALTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
|
|
| MYSc_Myo16 |
cd14878 |
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ... |
145-814 |
4.64e-92 |
|
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276844 [Multi-domain] Cd Length: 656 Bit Score: 314.45 E-value: 4.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERY---KGIKRHEVPPHVFAITDSAYRNMLGDREDQSIL 221
Cdd:cd14878 1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYlssSGQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 222 CTGESGAGKTENTKKVIQFLAYVAASkpkgSGAVphpavligeLEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 301
Cdd:cd14878 81 LSGERGSGKTEASKQIMKHLTCRASS----SRTT---------FDSRFKHVNCILEAFGHAKTTLNDLSSCFIKYFELQF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 302 -DASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGslpVPGVDDYAE---- 376
Cdd:cd14878 148 cERKKHLTGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQT---MREDVSTAErsln 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 377 ---FQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIK 453
Cdd:cd14878 225 rekLAVLKQALNVVGFSSLEVENLFVILSAILHLGDIRFTALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQY 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 454 VGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRIN---RSLDRTKRQGASFIGILDMAGFEIFELNSFEQLCINYT 530
Cdd:cd14878 305 FKGDMIIRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNcclQSQDEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 531 NEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTID-LIDKPGGIMALLDEECWFPKATDKTFVDKL-----VSA 604
Cdd:cd14878 385 NEKMHHYINEVLFLQEQTECVQEGVTMETAYSPGNQTGVLDfFFQKPSGFLSLLDEESQMIWSVEPNLPKKLqslleSSN 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 605 HSMHPKFMKTDFRGVA------DFAIVHYAGRVDYSAAKWLMKNMDPLNENIVsllqgsqdpFVVNIWKDAEIVGMAQQA 678
Cdd:cd14878 465 TNAVYSPMKDGNGNVAlkdqgtAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLL---------FVMKTSENVVINHLFQSK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 679 LTdtqfgartrkgmfrTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGF 758
Cdd:cd14878 536 LV--------------TIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGY 601
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 759 PNRIPFQEFRQRYELLTPNVI-PKGFMDGKKACEKMIQALELDSnlYRVGQSKIFFR 814
Cdd:cd14878 602 PVRLSFSDFLSRYKPLADTLLgEKKKQSAEERCRLVLQQCKLQG--WQMGVRKVFLK 656
|
|
| MYSc_Myo20 |
cd14881 |
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ... |
146-813 |
7.29e-82 |
|
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: 283.93 E-value: 7.29e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKK----LPIYTEKIMERYkgikrhevpPHVFAITDSAYRNMLGDREDQSIL 221
Cdd:cd14881 2 AVMKCLQARFYAKEFFTNVGPILLSVNPYRDvgnpLTLTSTRSSPLA---------PQLLKVVQEAVRQQSETGYPQAII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 222 CTGESGAGKTENTKKVIQFLAYVAASKPKgSGAVPHpavligeleqqLLQANPILEAFGNAKTVKNDNSSRFGKFIRINF 301
Cdd:cd14881 73 LSGTSGSGKTYASMLLLRQLFDVAGGGPE-TDAFKH-----------LAAAFTVLRSLGSAKTATNSESSRIGHFIEVQV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 302 dASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILD--DVKSYAFLSNGSLPVPGVDDYAEFQA 379
Cdd:cd14881 141 -TDGALYRTKIHCYFLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHGDTRQNEAEDAARFQA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 380 TVKSMNIMGMTsedFNSIFRIVSAVLLFGSMKFrQERNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRIKVGRDFV 459
Cdd:cd14881 220 WKACLGILGIP---FLDVVRVLAAVLLLGNVQF-IDGGGLEVDVKGETELKSVAALLGVSGAALFRGLTTRTHNARGQLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 460 TKAQTKEQVEFAVEAIAKACYERMFKWLVNRINrSLdrtKRQGAS--------FIGILDMAGFEIFELNSFEQLCINYTN 531
Cdd:cd14881 296 KSVCDANMSNMTRDALAKALYCRTVATIVRRAN-SL---KRLGSTlgthatdgFIGILDMFGFEDPKPSQLEHLCINLCA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 532 EKLQQLFNHTMFILEQEEYQREGIEWKF-IDFgLDLQPTIDLIDK-PGGIMALLDEECwFPKATDKTFVDKLVSAHSMHP 609
Cdd:cd14881 372 ETMQHFYNTHIFKSSIESCRDEGIQCEVeVDY-VDNVPCIDLISSlRTGLLSMLDVEC-SPRGTAESYVAKIKVQHRQNP 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 610 KFMKTDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGsqdpfvvniwkdaeivgmaqqalTDTQFGARTR 689
Cdd:cd14881 450 RLFEAKPQDDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFYK-----------------------QNCNFGFATH 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 690 KGMFRTvshlykeQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQ 769
Cdd:cd14881 507 TQDFHT-------RLDNLLRTLVHARPHFVRCIRSNTTETPNHFDRGTVVRQIRSLQVLETVNLMAGGYPHRMRFKAFNA 579
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 770 RYELLTPNVIPKGFMDGKKACEKMI------QALELDSNL---YRVGQSKIFF 813
Cdd:cd14881 580 RYRLLAPFRLLRRVEEKALEDCALIlqfleaQPPSKLSSVstsWALGKRHIFL 632
|
|
| MYSc_Myo23 |
cd14884 |
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ... |
145-766 |
2.29e-79 |
|
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: 277.94 E-value: 2.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKGIKRHE-------VPPHVFAITDSAYRNMLGDRE 216
Cdd:cd14884 1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDVMNVYLHKKSNSaasaapfPKAHIYDIANMAYKNMRGKLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 217 DQSILCTGESGAGKTENTKKVIQFLAYVAASKpkgsgavphpavLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKF 296
Cdd:cd14884 81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDS------------QMTERIDKLIYINNILESMSNATTIKNNNSSRCGRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 297 IRINFDA---------SGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQ-REKFILDDVKSYAFLSN--- 363
Cdd:cd14884 149 NLLIFEEventqknmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlARRNLVRNCGVYGLLNPdes 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 364 -------GSLPVPGVD----------DYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQernndqatlpdn 426
Cdd:cd14884 229 hqkrsvkGTLRLGSDSldpseeekakDEKNFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYKA------------ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 427 tvaqkIAHLLGLSVTDMTRAFLTPRIKVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGA--- 503
Cdd:cd14884 297 -----AAECLQIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDEsdn 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 504 --------SFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGlDLQPTIDLIDK 575
Cdd:cd14884 372 ediysineAIISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAP-SYSDTLIFIAK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 576 pggIMALLDE-----ECWFPKATDKTFVD-----------KLVSAHSMHPKfmktDFRGVAD--------FAIVHYAGRV 631
Cdd:cd14884 451 ---IFRRLDDitklkNQGQKKTDDHFFRYllnnerqqqleGKVSYGFVLNH----DADGTAKkqnikkniFFIRHYAGLV 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 632 DYSAAKWLMKNMDPLNENIVSLLQGSQDPFvvniwkdaeivgmaqqaLTDTQFGArtRKGMFRTVSHLYKEQLAKLMDTL 711
Cdd:cd14884 524 TYRINNWIDKNSDKIETSIETLISCSSNRF-----------------LREANNGG--NKGNFLSVSKKYIKELDNLFTQL 584
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 712 RNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 766
Cdd:cd14884 585 QSTDMYYIRCFLPNAKMLPNTFKRLLVYRQLKQCGSNEMIKILNRGLSHKIPKKE 639
|
|
| MYSc_Myo44 |
cd14905 |
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ... |
146-814 |
2.21e-77 |
|
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: 271.97 E-value: 2.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLP-IYTEKIMERYKgiKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14905 2 TLINIIQARYKKEIIYTYIGPILVSVNPLRYLPfLHSQELVRNYN--QRRGLPPHLFALAAKAISDMQDFRRDQLIFIGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAYVAASKPKgsgavphpavligELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDAS 304
Cdd:cd14905 80 ESGSGKSENTKIIIQYLLTTDLSRSK-------------YLRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 305 GFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSN-GSLPVPGVDDYAEFQATVKS 383
Cdd:cd14905 147 GEIQGAKLYSYFLDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDDNRVFDRLKMS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 384 MNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQErnNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRikvgrdfvtKAQ 463
Cdd:cd14905 227 FVFFDFPSEKIDLIFKTLSFIIILGNVTFFQK--NGKTEVKDRTLIESLSHNITFDSTKLENILISDR---------SMP 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 464 TKEQVEfAVEAIAKACYERMFKWLVNRINRSLDRTkrQGASFIGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMF 543
Cdd:cd14905 296 VNEAVE-NRDSLARSLYSALFHWIIDFLNSKLKPT--QYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 544 ILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKpggIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMKTDFRgvadFA 623
Cdd:cd14905 373 KQEQREYQTERIPWMTPISFKDNEESVEMMEK---IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKPNK----FG 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 624 IVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNiwKDAEIVGMAQQALTDTQFGAR--TRKGMFRTVSHLYK 701
Cdd:cd14905 446 IEHYFGQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYLFS--RDGVFNINATVAELNQMFDAKntAKKSPLSIVKVLLS 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 702 ------------------------------------EQLAKLMDTLRNTNPN--FVRCIIPNHEKRAGKIDAPLVLDQLR 743
Cdd:cd14905 524 cgsnnpnnvnnpnnnsgggggggnsgggsgsggstyTTYSSTNKAINNSNCDfhFIRCIKPNSKKTHLTFDVKSVNEQIK 603
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 744 CNGVLEGIRICRQGFPNRIPFQEFRQRYELltpnvipkgFMDGKKACEKMIQALE-----LDSNL---YRVGQSKIFFR 814
Cdd:cd14905 604 SLCLLETTRIQRFGYTIHYNNKIFFDRFSF---------FFQNQRNFQNLFEKLKendinIDSILpppIQVGNTKIFLR 673
|
|
| MYSc_Myo12 |
cd14874 |
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ... |
145-776 |
1.63e-74 |
|
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: 262.11 E-value: 1.63e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 145 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYkgikrhevppHVFAITDSAYRNMLGDRED-QSILCT 223
Cdd:cd14874 1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 224 GESGAGKTENTKKVIQFLAyvaaSKPKGSGAVPHPAVLigeleqqllqaNPILEAFGNAKTVKNDNSSRFGKFIRINFDA 303
Cdd:cd14874 71 GESGSGKSYNAFQVFKYLT----SQPKSKVTTKHSSAI-----------ESVFKSFGCAKTLKNDEATRFGCSIDLLYKR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 304 SgFISGANIE-TYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDYAEFQATVK 382
Cdd:cd14874 136 N-VLTGLNLKyTVPLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNHFKHLED 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 383 SMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERN----NDQATLPDNTVAQKIAHLLGLSVtDMTRAFLTPRIKVGRDF 458
Cdd:cd14874 215 ALHVLGFSDDHCISIYKIISTILHIGNIYFRTKRNpnveQDVVEIGNMSEVKWVAFLLEVDF-DQLVNFLLPKSEDGTTI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 459 VTKAQTKEQvefavEAIAKACYERMFKWLVNRINRSLDRTKRQGAsfIGILDMAGFEIFELNSFEQLCINYTNEKLQQLF 538
Cdd:cd14874 294 DLNAALDNR-----DSFAMLIYEELFKWVLNRIGLHLKCPLHTGV--ISILDHYGFEKYNNNGVEEFLINSVNERIENLF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 539 NHTMFILEQEEYQREGIEwkfIDF----GLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPKFMK 613
Cdd:cd14874 367 VKHSFHDQLVDYAKDGIS---VDYkvpnSIENGKTVELLfKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGK 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 614 TDFRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDA------EIVGMAQQALTDTQfgar 687
Cdd:cd14874 444 ARNKERLEFGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLFESYssntsdMIVSQAQFILRGAQ---- 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 688 trkgmfrtvshlykeqlaKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEF 767
Cdd:cd14874 520 ------------------EIADKINGSHAHFVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTF 581
|
....*....
gi 62471805 768 RQRYELLTP 776
Cdd:cd14874 582 ARQYRCLLP 590
|
|
| MYSc_Myo21 |
cd14882 |
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ... |
146-774 |
1.61e-72 |
|
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: 256.59 E-value: 1.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGE 225
Cdd:cd14882 2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 226 SGAGKTENTKKVIQFLAYVAASKPKGSGAVphpavligeleqqlLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASG 305
Cdd:cd14882 82 SYSGKTTNARLLIKHLCYLGDGNRGATGRV--------------ESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 306 FISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREK-FILDDVKSYAFL------------SNGSLPVPGVD 372
Cdd:cd14882 148 KMSGAIFWMYQLEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLKeYNLKAGRNYRYLrippevppsklkYRRDDPEGNVE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 373 DYAEFQATVKSMNimgMTSEDFNSIFRIVSAVLLFGSMKFRQerNNDQATLPDNTVAQKIAHLLGLSVTDMTRAFLTPRI 452
Cdd:cd14882 228 RYKEFEEILKDLD---FNEEQLETVRKVLAAILNLGEIRFRQ--NGGYAELENTEIASRVAELLRLDEKKFMWALTNYCL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 453 KVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKrqgASF-----IGILDMAGFEIFELNSFEQLCI 527
Cdd:cd14882 303 IKGGSAERRKHTTEEARDARDVLASTLYSRLVDWIINRINMKMSFPR---AVFgdkysISIHDMFGFECFHRNRLEQLMV 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 528 NYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTID-LIDKPGGIMALLDEECwfPKATDKTFVdkLVSAHS 606
Cdd:cd14882 380 NTLNEQMQYHYNQRIFISEMLEMEEEDIPTINLRF-YDNKTAVDqLMTKPDGLFYIIDDAS--RSCQDQNYI--MDRIKE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 607 MHPKFMKTDfrGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAEIVGMaqqaltdtqfga 686
Cdd:cd14882 455 KHSQFVKKH--SAHEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMFTNSQVRNM------------ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 687 RTRKGMFRTVShlyKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQE 766
Cdd:cd14882 521 RTLAATFRATS---LELLKMLSIGANSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQE 597
|
....*...
gi 62471805 767 FRQRYELL 774
Cdd:cd14882 598 FLRRYQFL 605
|
|
| MYSc_Myo32 |
cd14893 |
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ... |
148-772 |
1.03e-67 |
|
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276858 Cd Length: 741 Bit Score: 244.88 E-value: 1.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 148 LHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKR----------HEVPPHVFAITDSAYRNMLGDRED 217
Cdd:cd14893 4 LYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSREqtplyekdtvNDAPPHVFALAQNALRCMQDAGED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 218 QSILCTGESGAGKTENTKKVIQFLAYV---AASKPKGSGA--VPHPavlIGeleQQLLQANPILEAFGNAKTVKNDNSSR 292
Cdd:cd14893 84 QAVILLGGMGAGKSEAAKLIVQYLCEIgdeTEPRPDSEGAsgVLHP---IG---QQILHAFTILEAFGNAATRQNRNSSR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 293 FGKFIRINFDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGAT--PEQREKFILDD-VKSYAFLSN-----G 364
Cdd:cd14893 158 FAKMISVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQhdPTLRDSLEMNKcVNEFVMLKQadplaT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 365 SLPVpgvdDYAEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKF-------------RQERNNDQAT--LPDNTVA 429
Cdd:cd14893 238 NFAL----DARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFvpdpeggksvggaNSTTVSDAQScaLKDPAQI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 430 QKIAHLLGLS--VTD---MTRAFLTpriKVGRDFVT--KAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSL----DRT 498
Cdd:cd14893 314 LLAAKLLEVEpvVLDnyfRTRQFFS---KDGNKTVSslKVVTVHQARKARDTFVRSLYESLFNFLVETLNGILggifDRY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 499 KRQG----ASFIGILDMAGFEIFE--LNSFEQLCINYTNEKLQQLF-NHTMFI----LEQEEYQREG--IEWKFIDFGLD 565
Cdd:cd14893 391 EKSNivinSQGVHVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYvQNTLAInfsfLEDESQQVENrlTVNSNVDITSE 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 566 LQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAH---------SMHPKFMKTDFRGVAD----FAIVHYAGRV 631
Cdd:cd14893 471 QEKCLQLFeDKPFGIFDLLTENCKVRLPNDEDFVNKLFSGNeavgglsrpNMGADTTNEYLAPSKDwrllFIVQHHCGKV 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 632 DYSAAKWLMKNMDPLNENIVSLLQGSQDPFVvniwkdaEIVGMAQQALTDTQFGA------RTRKGMFRTVSHLYKE--- 702
Cdd:cd14893 551 TYNGKGLSSKNMLSISSTCAAIMQSSKNAVL-------HAVGAAQMAAASSEKAAkqteerGSTSSKFRKSASSAREskn 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 703 -----------QLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRY 771
Cdd:cd14893 624 itdsaatdvynQADALLHALNHTGKNFLVCIKPNETLEEGVFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY 703
|
.
gi 62471805 772 E 772
Cdd:cd14893 704 K 704
|
|
| MYSc_Myo24B |
cd14938 |
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ... |
146-812 |
1.65e-59 |
|
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276898 [Multi-domain] Cd Length: 713 Bit Score: 219.71 E-value: 1.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 146 SVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKR-HEVPPHVFAITDSAYRNMLGDREDQSILCTG 224
Cdd:cd14938 2 SVLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYKCIDCiEDLSLNEYHVVHNALKNLNELKRNQSIIISG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 225 ESGAGKTENTKKVIQFLAY-VAASKPKGSGAVPHPAVLI---------GELEQQLLQANPILEAFGNAKTVKNDNSSRFG 294
Cdd:cd14938 82 ESGSGKSEIAKNIINFIAYqVKGSRRLPTNLNDQEEDNIhneentdyqFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 295 KFIRINFDASGfISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVPGVDDY 374
Cdd:cd14938 162 KFCTIHIENEE-IKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENYSMLNNEKGFEKFSDYS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 375 AEFQATVKSMNIMGMTSEDFNSIFRIVSAVLLFGS-------------MKFRQE-------------RNNDQATLPDNTV 428
Cdd:cd14938 241 GKILELLKSLNYIFDDDKEIDFIFSVLSALLLLGNteivkafrkksllMGKNQCgqninyetilselENSEDIGLDENVK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 429 AQKIA-HLLGLSVTDMTRAFLTPRIkVGRDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKR--QGASF 505
Cdd:cd14938 321 NLLLAcKLLSFDIETFVKYFTTNYI-FNDSILIKVHNETKIQKKLENFIKTCYEELFNWIIYKINEKCTQLQNinINTNY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 506 IGILDMAGFEIFELNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWKFIDFGLDLQPTIDLIDKPGgimalldE 585
Cdd:cd14938 400 INVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCEYNSENIDNEPLYNLLVGPT-------E 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 586 ECWFP---KATDKTFVDK------LVSAHSMHPKFMKTD--FRGVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLL 654
Cdd:cd14938 473 GSLFSlleNVSTKTIFDKsnlhssIIRKFSRNSKYIKKDdiTGNKKTFVITHSCGDIIYNAENFVEKNIDILTNRFIDMV 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 655 QGSQDPFV------VNIWKDAEIVG-----MAQQALTDTQFGARTRKGMFRTvshLYKEQLAKLMDTLRNTNPNFVRCII 723
Cdd:cd14938 553 KQSENEYMrqfcmfYNYDNSGNIVEekrrySIQSALKLFKRRYDTKNQMAVS---LLRNNLTELEKLQETTFCHFIVCMK 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 724 PNHEKRA-GKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLTPnvipkgfmDGKKACEKMIQALELDSN 802
Cdd:cd14938 630 PNESKRElCSFDANIVLRQVRNFSIVEASQLKVGYYPHKFTLNEFLSIFDIKNE--------DLKEKVEALIKSYQISNY 701
|
730
....*....|
gi 62471805 803 LYRVGQSKIF 812
Cdd:cd14938 702 EWMIGNNMIF 711
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
167-306 |
1.05e-54 |
|
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: 188.71 E-value: 1.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 167 FCVVVNPYKKLPIYTE-KIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTGESGAGKTENTKKVIQFLAYVA 245
Cdd:cd01363 1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 246 AS--KPKGSGAVPHPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDASGF 306
Cdd:cd01363 81 FNgiNKGETEGWVYLTEITVTLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEILLDIAGF 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1251-1981 |
2.39e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 147.90 E-value: 2.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1251 INDQLENLRKAKTVLEKAkgtleaenaDLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQ 1330
Cdd:TIGR02168 218 LKAELRELELALLVLRLE---------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1331 EAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLA 1410
Cdd:TIGR02168 289 ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1411 EVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQR--TKVLE 1488
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEleELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1489 LEKKQKNFDKILAEEKAISEQIAQERdTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADK 1568
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAE-QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1569 NVHELEKAKRALESQLAELkAQNEELEDDlqltEDAKLRLE---------VNMQALRSQFERDLLAKEEGAEEKRRGLVK 1639
Cdd:TIGR02168 528 LISVDEGYEAAIEAALGGR-LQAVVVENL----NAAKKAIAflkqnelgrVTFLPLDSIKGTEIQGNDREILKNIEGFLG 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1640 QLRDLETELDEERK---------------QRTAAVASKKK-------LEGDL----------------------KEIEtt 1675
Cdd:TIGR02168 603 VAKDLVKFDPKLRKalsyllggvlvvddlDNALELAKKLRpgyrivtLDGDLvrpggvitggsaktnssilerrREIE-- 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1676 mEMHNKVKEDALKhAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDE 1755
Cdd:TIGR02168 681 -ELEEKIEELEEK-IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1756 LAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLER 1835
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1836 QNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQM 1915
Cdd:TIGR02168 839 RLEDLEEQIEELS-EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1916 DKLNSRIKLLKRNLDETEEELQKEKTQKR-KYQRECEDMIE-------SQEAMNREINSLKTKLRRTGGIGLSS 1981
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEAlenkiedDEEEARRRLKRLENKIKELGPVNLAA 991
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
883-1655 |
1.60e-32 |
|
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: 138.65 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 883 KVKPLLEVTKQEEKLVQKEDELKQVreKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQE 962
Cdd:TIGR02168 201 QLKSLERQAEKAERYKELKAELREL--ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 963 LEDMMQELETrieeeeeRVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLK 1042
Cdd:TIGR02168 279 LEEEIEELQK-------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1043 EKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNER----- 1117
Cdd:TIGR02168 352 ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkle 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1118 RVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNE 1197
Cdd:TIGR02168 432 EAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1198 LL------DSLDTTAAQQELRSKREQEL-----------------------ATLKKSLEEETVNHEGVLADMRHKHSQEL 1248
Cdd:TIGR02168 512 LKnqsglsGILGVLSELISVDEGYEAAIeaalggrlqavvvenlnaakkaiAFLKQNELGRVTFLPLDSIKGTEIQGNDR 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1249 NSINDQ------LENLRKAKTVLEKA-----KGTLEAENADLATELR----------------------------SVNSS 1289
Cdd:TIGR02168 592 EILKNIegflgvAKDLVKFDPKLRKAlsyllGGVLVVDDLDNALELAkklrpgyrivtldgdlvrpggvitggsaKTNSS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1290 RQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMEsqlTEAQQLLEE 1369
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE---AEVEQLEER 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1370 ETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNK---DIEA 1446
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANlreRLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1447 LERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKET 1526
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1527 KVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAN--------TQGTADKNVHELEKAKRALESQLAELKAQNEELEddl 1598
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlseeyslTLEEAEALENKIEDDEEEARRRLKRLENKIKELG--- 985
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1599 qltedaklrlEVNMQAL---RSQFER--DLLAKEEGAEEKRrglvKQLRDLETELDEERKQR 1655
Cdd:TIGR02168 986 ----------PVNLAAIeeyEELKERydFLTAQKEDLTEAK----ETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1294-1956 |
3.66e-32 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 136.99 E-value: 3.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1294 DRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEnitnQLEEA-ELKAsaavksasnmesqlteaqqllEEETR 1372
Cdd:COG1196 171 KERKEEAERKLEATEENLERLEDILGELERQLEPLERQAE----KAERYrELKE---------------------ELKEL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1373 QKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVK 1452
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1453 ELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvlsvs 1532
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE------- 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1533 RELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEvnm 1612
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE--- 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1613 qalrsQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIEttmEMHNKVKEDALKHAKK 1692
Cdd:COG1196 456 -----EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK---AALLLAGLRGLAGAVA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1693 LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQ----LTEDLASSERARRAAETERDELAEEIANNANKGS 1768
Cdd:COG1196 528 VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAkagrATFLPLDKIRARAALAAALARGAIGAAVDLVASD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1769 LMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANE-KSNSQKNENGRALLERQNKELKAKLAEI 1847
Cdd:COG1196 608 LREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAgGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1848 ETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQH-------KEQMDKLNS 1920
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEaleelpePPDLEELER 767
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 62471805 1921 RIKLLKRNLDE-------TEEELQKEKTQKRKYQRECEDMIES 1956
Cdd:COG1196 768 ELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEA 810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1137-1958 |
9.70e-32 |
|
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: 136.34 E-value: 9.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1137 QTLLRIDEESA--TKATAQKaqRELESQLAEIQEDLEAEKAARAKaekVRRDL---------SEELEALKNELlDSLDTT 1205
Cdd:TIGR02168 155 EERRAIFEEAAgiSKYKERR--KETERKLERTRENLDRLEDILNE---LERQLkslerqaekAERYKELKAEL-RELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1206 AAQQELRSKREqELATLKKSLEEetvnhegvLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRS 1285
Cdd:TIGR02168 229 LLVLRLEELRE-ELEELQEELKE--------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1286 VNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1365
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1366 LLE-------EETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEvttqmQEIKKKAEEDADLAKELEEGKK 1438
Cdd:TIGR02168 380 QLEtlrskvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE-----AELKELQAELEELEEELEELQE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1439 RLNKDIEALERQVKELIAQNDRLDKSKKKIQS------ELEDATIELEAQRTKVLELEKKQKNFDKILAeekAISEQI-A 1511
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQlqarldSLERLQENLEGFSEGVKALLKNQSGLSGILG---VLSELIsV 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1512 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKR--KTLQNELDDLANTQ----------------GTADKNVHEL 1573
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQNElgRVTFLPLDSIKGTEiqgndreilkniegflGVAKDLVKFD 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1574 EKAKRALESQLAE----------LKAQNEELEDDLQLTEDAKL----------RLEVNMQAL-RSQFERDLLAKEEGAEE 1632
Cdd:TIGR02168 612 PKLRKALSYLLGGvlvvddldnaLELAKKLRPGYRIVTLDGDLvrpggvitggSAKTNSSILeRRREIEELEEKIEELEE 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1633 KRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKE 1712
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1713 ELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKgslmideKRRLEARIATLEEELEEEQ 1792
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER-------LESLERRIAATERRLEDLE 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1793 SNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRtKVKATIATLEAKIANLEEQ 1872
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR-ELESKRSELRRELEELREK 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1873 LEnegKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMD----KLNSRIKLLKRNLDE-------TEEELQKEKT 1941
Cdd:TIGR02168 924 LA---QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEddeeEARRRLKRLENKIKElgpvnlaAIEEYEELKE 1000
|
890
....*....|....*..
gi 62471805 1942 QKRKYQRECEDMIESQE 1958
Cdd:TIGR02168 1001 RYDFLTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1059-1847 |
4.77e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 130.56 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1059 AEEEEKAKHLAKLKAKheatisELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQT 1138
Cdd:TIGR02168 220 AELRELELALLVLRLE------ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1139 LLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELldsldttAAQQELRSKREQE 1218
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1219 LATLKKSLEEETVNHEGvLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLatelrsvnssrqendrRRK 1298
Cdd:TIGR02168 367 LEELESRLEELEEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL----------------LKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1299 QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAElkasAAVKSASNMESQLTEAQQLLEEETRQKLGLS 1378
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE----QALDAAERELAQLQARLDSLERLQENLEGFS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1379 SKLRQIESEKEA-------LQEQLEEDDEAKRNYERKLAEvttQMQEIKKKAEEDADLA----KELEEGK-------KRL 1440
Cdd:TIGR02168 506 EGVKALLKNQSGlsgilgvLSELISVDEGYEAAIEAALGG---RLQAVVVENLNAAKKAiaflKQNELGRvtflpldSIK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1441 NKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQ---------IA 1511
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvIT 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1512 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQN 1591
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1592 EELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEgAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKE 1671
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE-AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1672 IETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVlqltedlASSERARRAAET 1751
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER-------ASLEEALALLRS 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1752 ERDELAEEIANnankgslmiDEKRRLEARiatleEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANE--------KSNS 1823
Cdd:TIGR02168 895 ELEELSEELRE---------LESKRSELR-----RELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaEALE 960
|
810 820
....*....|....*....|....
gi 62471805 1824 QKNENGRALLERQNKELKAKLAEI 1847
Cdd:TIGR02168 961 NKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1251-1961 |
3.20e-28 |
|
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: 124.80 E-value: 3.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1251 INDQLENLRKAKTVLEKAKgTLEAENADLATELRSvnSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQ 1330
Cdd:TIGR02169 196 KRQQLERLRREREKAERYQ-ALLKEKREYEGYELL--KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1331 EAENITNQLEEAELKASAAVKSA--------SNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAK 1402
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKigeleaeiASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1403 RNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQ 1482
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1483 RTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANT 1562
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1563 QGTADKN-------VHELEKAKR----ALESQlAELKAQNEELEDDL--------------------------------- 1598
Cdd:TIGR02169 513 EEVLKASiqgvhgtVAQLGSVGEryatAIEVA-AGNRLNNVVVEDDAvakeaiellkrrkagratflplnkmrderrdls 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1599 QLTEDAKLRLEVNMQALRSQFE-------RDLLAKEEGAEEKRRGLVKQLRDLETELDEE--------RKQRTAAVASkK 1663
Cdd:TIGR02169 592 ILSEDGVIGFAVDLVEFDPKYEpafkyvfGDTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsRAPRGGILFS-R 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1664 KLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSE 1743
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1744 RARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQ-----IEQLTTELAN 1818
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLReieqkLNRLTLEKEY 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1819 EKSNSQKNENGRALLERQNKELKAKLAEIETAQRtKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELT 1898
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1899 MNIEDERRHVDQHKEQMDKLNSRIK----LLKRNLDETEEELQKEKTQKRKyqRECEDMIESQEAMN 1961
Cdd:TIGR02169 910 AQIEKKRKRLSELKAKLEALEEELSeiedPKGEDEEIPEEELSLEDVQAEL--QRVEEEIRALEPVN 974
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
983-1559 |
3.35e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 121.20 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 983 ALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEE 1062
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1063 EKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRI 1142
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1143 DEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATL 1222
Cdd:COG1196 403 EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1223 KKSLEEETVNHEgVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAES 1302
Cdd:COG1196 483 LEELAEAAARLL-LLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1303 QIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSasnmESQLTEAQQLLEEETRQKLGLSSKLR 1382
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREA----DARYYVLGDTLLGRTLVAARLEAALR 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1383 QIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD 1462
Cdd:COG1196 638 RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1463 KSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKI 1542
Cdd:COG1196 718 EEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEELEERY 797
|
570
....*....|....*..
gi 62471805 1543 EDLENKRKTLQNELDDL 1559
Cdd:COG1196 798 DFLSEQREDLEEARETL 814
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1007-1756 |
4.88e-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: 117.46 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1007 AARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERL 1086
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1087 HKDQQQRQESdrskrkiETEVADLKEQLNERRVQVDEMQAQLAKREEELtqtllrideesatkataqkaqRELESQLAEI 1166
Cdd:TIGR02168 326 EELESKLDEL-------AEELAELEEKLEELKEELESLEAELEELEAEL---------------------EELESRLEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1167 QEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVnheGVLADMRHKHSQ 1246
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL---EELEEELEELQE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1247 ELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQEND------RRRKQAESQIAELQVKLAEIERARSE 1320
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvKALLKNQSGLSGILGVLSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1321 ------------LQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESE- 1387
Cdd:TIGR02168 535 yeaaieaalggrLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKl 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1388 KEALQ---------EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAeedADLAKELEEGKKRLNKD--IEALERQVKELIA 1456
Cdd:TIGR02168 615 RKALSyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERRreIEELEEKIEELEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1457 QNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELD 1536
Cdd:TIGR02168 692 KIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1537 EAFDKIEDLENKRKTLQNELDDLANtqgtadkNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALR 1616
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKE-------ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1617 SQFERdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQ 1696
Cdd:TIGR02168 845 EQIEE-LSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1697 VKDA-LRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDEL 1756
Cdd:TIGR02168 924 LAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1296-1974 |
1.00e-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: 116.31 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1296 RRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAE------NITNQLEEAELKASAAvksasnmesQLTEAQQLLEE 1369
Cdd:TIGR02168 173 RRKETERKLERTRENLDRLEDILNELERQLKSLERQAEkaerykELKAELRELELALLVL---------RLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1370 ETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlakeLEEGKKRLNKDIEALER 1449
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLER 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1450 QVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVL 1529
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1530 SVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKraLESQLAELKAQNEELEDDLQLTEDAKLRLE 1609
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE--LEEELEELQEELERLEEALEELREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1610 VNMQALRSQFERdllakeegaeekRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGD---LKEIETTMEMHNKVKEDA 1686
Cdd:TIGR02168 475 QALDAAERELAQ------------LQARLDSLERLQENLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEGYEAAIEAA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1687 LkhAKKLQAQVKDALrdaeeaKAAKEELQALSKEAERKVKALEAEVLQLTEdLASSERARRAAETERDELAEEIANNANK 1766
Cdd:TIGR02168 543 L--GGRLQAVVVENL------NAAKKAIAFLKQNELGRVTFLPLDSIKGTE-IQGNDREILKNIEGFLGVAKDLVKFDPK 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1767 ----------GSLMIDE---------KRRLEARIATLEEELEEEQ--------SNSEVLLDRSR---KAQLQIEQLTTEL 1816
Cdd:TIGR02168 614 lrkalsyllgGVLVVDDldnalelakKLRPGYRIVTLDGDLVRPGgvitggsaKTNSSILERRReieELEEKIEELEEKI 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1817 ANEKSNSQKNENGRALLERQNKELKAKLAEIETaQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKE 1896
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSR-QISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1897 LTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRRT 1974
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
|
| MYSc_Myo33 |
cd14894 |
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ... |
269-755 |
4.34e-25 |
|
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.
Pssm-ID: 276859 [Multi-domain] Cd Length: 871 Bit Score: 114.07 E-value: 4.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 269 LLQANPILEAFGNAKTVKNDNSSRFGKF--IRINFDASGF---ISGANIETYLLEKSRAIRQA------KDERTFHIFYQ 337
Cdd:cd14894 249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAFGLHPWefqICGCHISPFLLEKSRVTSERgresgdQNELNFHILYA 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 338 LLAG--ATPEQR---EKFILD--DVKSYAFLSNGSLPVPGV--------DDYAEFQATVKSMNIMGMTSEDFNSIFRIVS 402
Cdd:cd14894 329 MVAGvnAFPFMRllaKELHLDgiDCSALTYLGRSDHKLAGFvskedtwkKDVERWQQVIDGLDELNVSPDEQKTIFKVLS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 403 AVLLFGSMKFRQERNNDQATLPDN---TVAQKIAHLLGL-SVTDMTRAFLTPRIKVGRDFVTKAQTKE--QVEFAVEAIA 476
Cdd:cd14894 409 AVLWLGNIELDYREVSGKLVMSSTgalNAPQKVVELLELgSVEKLERMLMTKSVSLQSTSETFEVTLEkgQVNHVRDTLA 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 477 KACYERMFKWLVNRINR-------SLDRTKRQ---------GASFIGILDMAGFEIFELNSFEQLCINYTNEKLqqlfnh 540
Cdd:cd14894 489 RLLYQLAFNYVVFVMNEatkmsalSTDGNKHQmdsnasapeAVSLLKIVDVFGFEDLTHNSLDQLCINYLSEKL------ 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 541 tmfileqeeYQREGiewKFIDFGLDLQP----------TIDLIDKPGGIMALLDEECWFPKAT----------DKTFVDK 600
Cdd:cd14894 563 ---------YAREE---QVIAVAYSSRPhltardsekdVLFIYEHPLGVFASLEELTILHQSEnmnaqqeekrNKLFVRN 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 601 LVSAHSMH----PKFMKTDFR------GVADFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQDPFVVNIWKDAE 670
Cdd:cd14894 631 IYDRNSSRlpepPRVLSNAKRhtpvllNVLPFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRMLNESS 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 671 IVGMAQQALTDTQFGARTRKGMFRTVSHLYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEG 750
Cdd:cd14894 711 QLGWSPNTNRSMLGSAESRLSGTKSFVGQFRSHVNVLTSQDDKNMPFYFHCIRPNAKKQPSLVNNDLVEQQCRSQRLIRQ 790
|
....*
gi 62471805 751 IRICR 755
Cdd:cd14894 791 MEICR 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1061-1865 |
2.70e-24 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 111.70 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1061 EEEKAKHLAKLKA------KHEATISELEERLHKDQQQRQESDR----SKRKIETEVADLKEQLNERRVQVDEMQAQLAK 1130
Cdd:TIGR02169 169 DRKKEKALEELEEveenieRLDLIIDEKRQQLERLRREREKAERyqalLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1131 REEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDleaekaaraKAEKVRRDLsEELEALKNELLDSLDTTAAQQE 1210
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE---------EQLRVKEKI-GELEAEIASLERSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1211 LRSKREQElatlkksLEEEtvnhegvladmRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSR 1290
Cdd:TIGR02169 319 DAEERLAK-------LEAE-----------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1291 QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLE--EAELKASAAVKSA-----SNMESQLTEA 1363
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgiEAKINELEEEKEDkaleiKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1364 QQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKD 1443
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1444 IE-ALERQVKELIAQND-------RLDKSKK----------KIQSELEDATIELEAQRT----KVLELEKKQKNFDKILA 1501
Cdd:TIGR02169 541 IEvAAGNRLNNVVVEDDavakeaiELLKRRKagratflplnKMRDERRDLSILSEDGVIgfavDLVEFDPKYEPAFKYVF 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1502 EEKAISEQIAQERD-----------------------------TAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTL 1552
Cdd:TIGR02169 621 GDTLVVEDIEAARRlmgkyrmvtlegelfeksgamtggsraprGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRI 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1553 QNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRS---QFERDLLA-KEE 1628
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEArieELEEDLHKlEEA 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1629 GAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAK 1708
Cdd:TIGR02169 781 LNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1709 AAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEEL 1788
Cdd:TIGR02169 861 GKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK 940
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1789 EEEQSNSEVLLDrSRKAQLQIEQLTTEL-ANEKSNSQKNENGRALLERQNkELKAKLAEIEtAQRTKVKATIATLEAK 1865
Cdd:TIGR02169 941 GEDEEIPEEELS-LEDVQAELQRVEEEIrALEPVNMLAIQEYEEVLKRLD-ELKEKRAKLE-EERKAILERIEEYEKK 1015
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
887-1499 |
3.71e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 111.18 E-value: 3.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 887 LLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDM 966
Cdd:COG1196 231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 967 MQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKL 1046
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1047 LEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA 1126
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1127 QLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaeKAARAKAEKVRRDLSEELEALknELLDSLDTTA 1206
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA-----ALLLAGLRGLAGAVAVLIGVE--AAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1207 AQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAkgTLEAENADLATELRSV 1286
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVA--SDLREADARYYVLGDT 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1287 NSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQL 1366
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1367 LEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADlakELEEGKKRLNKDIEA 1446
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE---ELERELERLEREIEA 778
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1447 LE----------RQVKE----LIAQNDRLDKSKKkiqsELEDATIELEAQRTKVLelekkQKNFDKI 1499
Cdd:COG1196 779 LGpvnllaieeyEELEErydfLSEQREDLEEARE----TLEEAIEEIDRETRERF-----LETFDAV 836
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1153-1974 |
5.71e-24 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 110.59 E-value: 5.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1153 QKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVN 1232
Cdd:pfam15921 102 EKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1233 HEGVLadmrhkhsQELNSIndqlenlrkaKTVLEKAKGTLEAENADLAT-ELRSVNSSrqendrrrkqaesqiaelqvkl 1311
Cdd:pfam15921 182 HEGVL--------QEIRSI----------LVDFEEASGKKIYEHDSMSTmHFRSLGSA---------------------- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1312 aeIERARSELQEKCTKLQQEAENITNQLEEaeLKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEAL 1391
Cdd:pfam15921 222 --ISKILRELDTEISYLKGRIFPVEDQLEA--LKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1392 QEQLEEDDEAKRN----YERKLAEVTTQMQEIKKkaeedadlakELEEGKKRLNKDIEALERQvkeLIAQNDRLDKSKKK 1467
Cdd:pfam15921 298 QSQLEIIQEQARNqnsmYMRQLSDLESTVSQLRS----------ELREAKRMYEDKIEELEKQ---LVLANSELTEARTE 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1468 iQSELEDATIELEAQRTKVL-ELEKKQKNfdkiLAEEKAISEQIaQERDTAereareKETKVLSVSRELDEAFDKIEDLE 1546
Cdd:pfam15921 365 -RDQFSQESGNLDDQLQKLLaDLHKREKE----LSLEKEQNKRL-WDRDTG------NSITIDHLRRELDDRNMEVQRLE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1547 NKRKTLQNElddlanTQGTADKNVHELEKAKRALE---SQLAELKAQNEELEDDLQLTEDAKLRLEvNMQALRSQFERDL 1623
Cdd:pfam15921 433 ALLKAMKSE------CQGQMERQMAAIQGKNESLEkvsSLTAQLESTKEMLRKVVEELTAKKMTLE-SSERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1624 LAKEEGAEEKRRGLVK----------QLRDLETELDEERKQRTAAVASKKKLEGDLK-------EIETTMEM---HNKVK 1683
Cdd:pfam15921 506 QEKERAIEATNAEITKlrsrvdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKvieilrqQIENMTQLvgqHGRTA 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1684 EDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANN 1763
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1764 ANKGSLMIDEKRRLEARIatleeeleeeQSNSEVLLDRSRKAQLQIEQLTTELANEKSN--SQKNENGRALlerqnkelk 1841
Cdd:pfam15921 666 RNELNSLSEDYEVLKRNF----------RNKSEEMETTTNKLKMQLKSAQSELEQTRNTlkSMEGSDGHAM--------- 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1842 aKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKelTMNIEDerrhvDQHKEQMDKLNSR 1921
Cdd:pfam15921 727 -KVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELS--TVATEK-----NKMAGELEVLRSQ 798
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1922 IKLLKRNLDETEEELQKEKTQKrkyqRECEDMIESQEAmnreiNSLKTKLRRT 1974
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQF----AECQDIIQRQEQ-----ESVRLKLQHT 842
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1357-1973 |
1.21e-23 |
|
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: 109.49 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLE-------EDDEAKRNYERKLAEVTTQMQEIKKKAEEDADL 1429
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1430 AKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQS---ELEDATIELEAQRtkvlelekkqknfDKILAEEKAI 1506
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkikKLEEDILLLEDQN-------------SKLSKERKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1507 SEQIAQERDTAEREarEKETKVLSVSRELDEAFdkIEDLENKRKTlqnelddlantqgtADKNVHELEKAKRALESQLAE 1586
Cdd:pfam01576 158 EERISEFTSNLAEE--EEKAKSLSKLKNKHEAM--ISDLEERLKK--------------EEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1587 LKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEgAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLE 1666
Cdd:pfam01576 220 LQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNN-ALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1667 GDLK----EIETTMEMHNKVKEDALKHAKKLqAQVKDALRDAEEAKAAKeeLQALSKEAERKVKALEAEVLQLTEDLASS 1742
Cdd:pfam01576 299 EELEalktELEDTLDTTAAQQELRSKREQEV-TELKKALEEETRSHEAQ--LQEMRQKHTQALEELTEQLEQAKRNKANL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1743 ERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSN 1822
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1823 SQKNENGRALLERQNKELKAKLAEiETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIE 1902
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQE-ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLE 534
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1903 DERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1973
Cdd:pfam01576 535 EDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1292-1974 |
2.08e-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: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1292 ENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEN------ITNQLEEAELKA-----SAAVKSASNMESQL 1360
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKaeryqaLLKEKREYEGYEllkekEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1361 TEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEE-DDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKR 1439
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1440 LNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKK-QKNFDKILAEEKAIsEQIAQERDTAE 1518
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEfAETRDELKDYREKL-EKLKREINELK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1519 REAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDL 1598
Cdd:TIGR02169 406 RELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1599 QLTEDAKLRLEVNMQALRSQfERDLLAKEEGAEEKRRGLVKQLRDLETEldEERKQRTAAVASKKKL-------EGDLKE 1671
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVAQLGSV--GERYATAIEVAAGNRLnnvvvedDAVAKE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1672 -IETTMEMH---------NKVKE------------------DALKHAKKLQAQVKDALRDAEEAKAAKEELQAL------ 1717
Cdd:TIGR02169 563 aIELLKRRKagratflplNKMRDerrdlsilsedgvigfavDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMgkyrmv 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1718 -------------------SKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIannANKGSLMIDEKRRLE 1778
Cdd:TIGR02169 643 tlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRL---DELSQELSDASRKIG 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1779 ARIATLEEELEEEQSNSEVLLDRSRKaqlqIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIE---------- 1848
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEELEED----LSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEarlshsripe 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1849 -TAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKR 1927
Cdd:TIGR02169 796 iQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 62471805 1928 NLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRRT 1974
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
887-1664 |
2.12e-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: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 887 LLEVTKQEEKLVQKEDELKQVREKL----------DTLAKNTQEYE-----RKYQQALVEKTTLAEQL---QAEIE-LCA 947
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLrrerekaeryQALLKEKREYEgyellKEKEALERQKEAIERQLaslEEELEkLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 948 EAEESRSRLMARKQELED----MMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKI 1023
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEElnkkIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1024 KKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAK----HLAKLKAKHEATISELEE---RLHKDQQQRQES 1096
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdELKDYREKLEKLKREINElkrELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1097 DRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAA 1176
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1177 RAKAEKVRRDLSEELEALKNELLDSLDTTAaqqELRSKREQELATLKKSL---------EEETVNHEGVLADMRHKHSQ- 1246
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQGVHGTVA---QLGSVGERYATAIEVAAgnrlnnvvvEDDAVAKEAIELLKRRKAGRa 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1247 ---ELNSINDQLENLRKAKT--VLEKA------------------KGTLEAENADLATEL----RSV---------NSSR 1290
Cdd:TIGR02169 576 tflPLNKMRDERRDLSILSEdgVIGFAvdlvefdpkyepafkyvfGDTLVVEDIEAARRLmgkyRMVtlegelfekSGAM 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1291 QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEE 1370
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1371 TRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKkkaeedadlAKELEEGKKRLNKDIEALERQ 1450
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE---------ARLSHSRIPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1451 VKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEkkqknfDKILAEEKAISEQIAQERDTaEREAREKETKVLS 1530
Cdd:TIGR02169 807 VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLK------EQIKSIEKEIENLNGKKEEL-EEELEELEAALRD 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1531 VSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLT---EDAKLR 1607
Cdd:TIGR02169 880 LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAE 959
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1608 LEVNMQALRSQFERDLLAKEEGAEEKRR--GLVKQLRDLETElDEERKQRTAAVASKKK 1664
Cdd:TIGR02169 960 LQRVEEEIRALEPVNMLAIQEYEEVLKRldELKEKRAKLEEE-RKAILERIEEYEKKKR 1017
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1154-1697 |
2.77e-23 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 108.23 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1154 KAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDsLDTTAAQQELRSKREQELATLKKSLEEETVNH 1233
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKE-LEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1234 EGVLADMRhKHSQELNSINDQLENLRKAKT---VLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAES---QIAEL 1307
Cdd:PRK03918 265 EERIEELK-KEIEELEEKVKELKELKEKAEeyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1308 QVKLAEIERARSELQEKcTKLQQEAENITNQLEEaeLKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESE 1387
Cdd:PRK03918 344 KKKLKELEKRLEELEER-HELYEEAKAKKEELER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1388 KEALQEQLEEDDEAKR------------NYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALER--QVKE 1453
Cdd:PRK03918 421 IKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1454 LIAQNDRLDKSKKKIQSE-LEDATIELEAQRTKVLELEKKQKNFDKILAEEKAI---SEQIAQERDTAEREAREKETKVL 1529
Cdd:PRK03918 501 LAEQLKELEEKLKKYNLEeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELkkkLAELEKKLDELEEELAELLKELE 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1530 SVS-----------RELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALEsqlaELKAQNEELEDDL 1598
Cdd:PRK03918 581 ELGfesveeleerlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLE----ELRKELEELEKKY 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1599 QLTEDAKLRLEvnMQALRSQFERdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEgDLKEI-ETTME 1677
Cdd:PRK03918 657 SEEEYEELREE--YLELSRELAG-LRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE-RVEELrEKVKK 732
|
570 580
....*....|....*....|
gi 62471805 1678 MHNKVKEDALKHAKKLQAQV 1697
Cdd:PRK03918 733 YKALLKERALSKVGEIASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1031-1595 |
5.92e-23 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 107.05 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1031 ALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADL 1110
Cdd:PRK02224 188 SLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETI 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1111 KEQLNER---RVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLeaekaarakaEKVRRDL 1187
Cdd:PRK02224 268 AETEREReelAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL----------EECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1188 SEelealKNELLDSLDTTAAQQELRSKREQELAtlkKSLEEETVNHEGVLADMRhkhsQELNSINDQLENLRKAKTVLEK 1267
Cdd:PRK02224 338 QA-----HNEEAESLREDADDLEERAEELREEA---AELESELEEAREAVEDRR----EEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1268 AKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQ--------------VKLAEIERARSELQEKCTKLQQEAE 1333
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEalleagkcpecgqpVEGSPHVETIEEDRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1334 NITNQLEEAELK---ASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEqLEEDDEAKRnyerklA 1410
Cdd:PRK02224 486 DLEEEVEEVEERlerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE-LEAEAEEKR------E 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1411 EVTTQMQEIKKKAEEDADLAKELEEGKKRLNK--DIEALERQVKELIAQNDRLdKSKKKIQSELEDATIE-LEAQRTKVL 1487
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERL-REKREALAELNDERRErLAEKRERKR 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1488 ELEKK-QKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAntqgTA 1566
Cdd:PRK02224 638 ELEAEfDEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALE----AL 713
|
570 580 590
....*....|....*....|....*....|
gi 62471805 1567 DKNVHELEKAKRALEsqlAELKAQN-EELE 1595
Cdd:PRK02224 714 YDEAEELESMYGDLR---AELRQRNvETLE 740
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1069-1955 |
1.13e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 106.76 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1069 AKLKAKHEATISE---LEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQvDEMQAQLAKREEEltqtllriDEE 1145
Cdd:PTZ00121 1083 AKEDNRADEATEEafgKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE-DARKAEEARKAED--------AKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1146 SATKATAQKAQRELESQLAEiqEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKS 1225
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAE--DAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1226 LEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIA 1305
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1306 ELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIE 1385
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1386 SEKEALQEQleEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlAKELEEGKKRLNKDIEALErqVKELIAQNDRLDKSK 1465
Cdd:PTZ00121 1392 KADEAKKKA--EEDKKKADELKKAAAAKKKADEAKKKAEE----KKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAK 1463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1466 KKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEE---KAISEQIAQERDTAEREAREKETKVLSVSRELDEAfdki 1542
Cdd:PTZ00121 1464 KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---- 1539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1543 EDLENKRKTlqnelddlantqgtadKNVHELEKAKRALESQLAELKAQNEELED-DLQLTEDAKLRLEVNMQALRSQFER 1621
Cdd:PTZ00121 1540 KKAEEKKKA----------------DELKKAEELKKAEEKKKAEEAKKAEEDKNmALRKAEEAKKAEEARIEEVMKLYEE 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1622 DLLAKEEGA--EEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEiettmEMHNKVKEDALKhaKKLQAQVKD 1699
Cdd:PTZ00121 1604 EKKMKAEEAkkAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-----EEENKIKAAEEA--KKAEEDKKK 1676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1700 ALRDAEEAKAAKEELQALSKEAERK-----VKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEK 1774
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEK 1756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1775 RRLEARIATLEEELEEEQSNSEVLL-----DRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELkaklaEIET 1849
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKEAVIeeeldEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM-----EDSA 1831
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1850 AQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKE-LTMNIEDERRHVDQHKEQMDKLNSRIKLLKRN 1928
Cdd:PTZ00121 1832 IKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEdDEEEIEEADEIEKIDKDDIEREIPNNNMAGKN 1911
|
890 900
....*....|....*....|....*..
gi 62471805 1929 LDETEEELQKEKTQKRKYQRECEDMIE 1955
Cdd:PTZ00121 1912 NDIIDDKLDKDEYIKRDAEETREEIIK 1938
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1056-1759 |
1.44e-22 |
|
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: 106.31 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1056 QTLAEEEEKAKHLAKLKAKHEATisELEERLHkdqqQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEEL 1135
Cdd:TIGR02169 201 ERLRREREKAERYQALLKEKREY--EGYELLK----EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1136 TQTLLRIDEESATKATAQKAQ-RELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELlDSLDTTAAQQELR-- 1212
Cdd:TIGR02169 275 EELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI-EELEREIEEERKRrd 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1213 ------SKREQELATLKKSLEEETVNHegvlADMRHKHSQ----------ELNSIND--------------QLENLRKAK 1262
Cdd:TIGR02169 354 klteeyAELKEELEDLRAELEEVDKEF----AETRDELKDyrekleklkrEINELKReldrlqeelqrlseELADLNAAI 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1263 TVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLqqEAENITNQLEEA 1342
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA--EAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1343 ELKASAAVKSASN-----MESQLTE---------------------------AQQLLEEETRQKLGLSS-----KLRQIE 1385
Cdd:TIGR02169 508 GGRAVEEVLKASIqgvhgTVAQLGSvgeryataievaagnrlnnvvveddavAKEAIELLKRRKAGRATflplnKMRDER 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1386 SEKEALQEQ----------------------------LEEDDEAKRNYERKLAEVTTQMQEIKK---------KAEEDAD 1428
Cdd:TIGR02169 588 RDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlVVEDIEAARRLMGKYRMVTLEGELFEKsgamtggsrAPRGGIL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1429 LAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISE 1508
Cdd:TIGR02169 668 FSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1509 QIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLEnkRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELK 1588
Cdd:TIGR02169 748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1589 AQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRgLVKQLRDLETELDEERKQRTAAVASKKKLEGD 1668
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-LEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1669 LKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEE------AKAAKEELQALSKEAERKVKALEAEVLQLTEDLASS 1742
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEdeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
|
810
....*....|....*..
gi 62471805 1743 ERARRAAETERDELAEE 1759
Cdd:TIGR02169 985 LKRLDELKEKRAKLEEE 1001
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1084-1684 |
3.10e-22 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 104.74 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1084 ERLHKDQQQRQESDRSKRKiETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRE---LE 1160
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIE-EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEletLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1161 SQLAEIQEDLEAEKAARAKAE---KVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEEtvnhegvL 1237
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAeevRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDR-------L 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1238 ADMRhkhsQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERA 1317
Cdd:PRK02224 331 EECR----VAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1318 RSELQEKCTKLQQEAENITNqlEEAELKASAavksaSNMESQLTEAQQLLEE----ETRQKLGLSSKLrqiesekealqE 1393
Cdd:PRK02224 407 LGNAEDFLEELREERDELRE--REAELEATL-----RTARERVEEAEALLEAgkcpECGQPVEGSPHV-----------E 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1394 QLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlAKELEEGKKRLnkdiealerqvkeliaqnDRLDKSKKKIQSELE 1473
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLER----AEDLVEAEDRI------------------ERLEERREDLEELIA 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1474 DATIELEAQRTKVLELEKKqknfdkilaeekaiseqiAQERDTAEREAREKETKVLSvsrELDEAFDKIEDLENKRKTLQ 1553
Cdd:PRK02224 527 ERRETIEEKRERAEELRER------------------AAELEAEAEEKREAAAEAEE---EAEEAREEVAELNSKLAELK 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1554 NELDDLANTQGTADKnVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKlrlevnmQALRSQFERDLLakeEGAEEK 1633
Cdd:PRK02224 586 ERIESLERIRTLLAA-IADAEDEIERLREKREALAELNDERRERLAEKRERK-------RELEAEFDEARI---EEARED 654
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1634 RRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKE 1684
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
858-1614 |
3.10e-21 |
|
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: 101.68 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 858 AIRIIQRNCAAYLKLRNWQwwrlyTKVKPLLEVTKQeekLVQKEDELKQVREKLDTLAKNTQEYERKYQQ--ALVEKTTL 935
Cdd:TIGR02169 215 ALLKEKREYEGYELLKEKE-----ALERQKEAIERQ---LASLEEELEKLTEEISELEKRLEEIEQLLEElnKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 936 AEQLQAEIELcAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLE 1015
Cdd:TIGR02169 287 EEQLRVKEKI-GELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1016 KVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQE 1095
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1096 SDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKA 1175
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHG 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1176 ARAKAEKVRRDLSEELE-ALKNELL-----DSLDTTAAQQELRSKR------------EQELATLKKSLEEETVNHEGVL 1237
Cdd:TIGR02169 526 TVAQLGSVGERYATAIEvAAGNRLNnvvveDDAVAKEAIELLKRRKagratflplnkmRDERRDLSILSEDGVIGFAVDL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1238 ADMRHKHSQELN-SINDQL--ENLRKAKTVLEKAKG-TLEAENAD---------LATELRSVNSSRQENDRRRKQA---- 1300
Cdd:TIGR02169 606 VEFDPKYEPAFKyVFGDTLvvEDIEAARRLMGKYRMvTLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRErleg 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1301 -ESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSS 1379
Cdd:TIGR02169 686 lKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1380 KLRQIESEKEALQEQLEE-----DDEAKRNYERKLAEVTTQMQEIKKKAEE-DADLAKE------LEEGKKRLNKDIEAL 1447
Cdd:TIGR02169 766 RIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLREiEQKLNRLtlekeyLEKEIQELQEQRIDL 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1448 ERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETK 1527
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1528 VLSVSRELDEAFDK-------------IEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEEL 1594
Cdd:TIGR02169 926 LEALEEELSEIEDPkgedeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
810 820
....*....|....*....|
gi 62471805 1595 EDDLQLTEdaKLRLEVNMQA 1614
Cdd:TIGR02169 1006 LERIEEYE--KKKREVFMEA 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
915-1767 |
4.07e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 101.76 E-value: 4.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 915 AKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKqeLEDMMQELETRIEEEEERVlalgGEKKKLEln 994
Cdd:PTZ00121 1096 AFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK--AEEARKAEDAKRVEIARKA----EDARKAE-- 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 995 IQDLEEQLEEEEAARQKLQLEKVqldakikkyeEDLALTDDQNQKLLKEKKLLEERANDLSQtlAEEEEKAKHLAK---L 1071
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKA----------EELRKAEDARKAEAARKAEEERKAEEARK--AEDAKKAEAVKKaeeA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1072 KAKHEATISELEERLHKDQQQRQESDRS--KRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTllridEESATK 1149
Cdd:PTZ00121 1236 KKDAEEAKKAEEERNNEEIRKFEEARMAhfARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKA-----DEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1150 ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEE 1229
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1230 TVnhegvlADMRHKHSQELNSINDQLENLRKAKTVLEKAKGtlEAENADLATELRSVNSSRQENDRRRKQA-ESQIAELQ 1308
Cdd:PTZ00121 1391 KK------ADEAKKKAEEDKKKADELKKAAAAKKKADEAKK--KAEEKKKADEAKKKAEEAKKADEAKKKAeEAKKAEEA 1462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1309 VKLAEIERARSELQEKCTKlQQEAENITNQLEEAELKASAAVKSASNMEsqltEAQQLLEEETRQKlglSSKLRQIESEK 1388
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKK----KADEAKKAEEAKK---ADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1389 EAlqeqleedDEAKRNYERKLAEVTTQMQEIKKKAE-EDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKK 1467
Cdd:PTZ00121 1535 KA--------DEAKKAEEKKKADELKKAEELKKAEEkKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1468 IQSE----LEDATIELEAQRtKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIE 1543
Cdd:PTZ00121 1607 MKAEeakkAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEE 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1544 DLENKRKTLQNELDDLANTQGTADKNVHELEKA---KRALESQLAELKAQNEELEDDLQLTEDAKLRLEvnmqalrsqfE 1620
Cdd:PTZ00121 1686 DEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE----------E 1755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1621 RDLLAKEEGAEEKRRGLVKQLRD--LETELDEERKQRTAAVASKKKLEGDLKE--IETTMEMH---NKVKEDALKHAKKL 1693
Cdd:PTZ00121 1756 KKKIAHLKKEEEKKAEEIRKEKEavIEEELDEEDEKRRMEVDKKIKDIFDNFAniIEGGKEGNlviNDSKEMEDSAIKEV 1835
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1694 QAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKG 1767
Cdd:PTZ00121 1836 ADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAG 1909
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
908-1673 |
7.29e-21 |
|
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: 100.53 E-value: 7.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 908 REKLDTLAkNTQEYERKYQQALVEKTTLAEQLQaeiELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGE 987
Cdd:TIGR02169 156 RKIIDEIA-GVAEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 988 KKKLELNIQDLEEQLEEEEAARQKLQlekVQLDAKIKKYEEdlaLTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKakh 1067
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLT---EEISELEKRLEE---IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE--- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1068 laklKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESA 1147
Cdd:TIGR02169 303 ----IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1148 TKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLE 1227
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1228 EetvnhegvLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAEL 1307
Cdd:TIGR02169 459 Q--------LAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1308 -QVK---LAEIERA---------------------------------------RSELQEKCTKLQQEAENITNQLEEAEL 1344
Cdd:TIGR02169 531 gSVGeryATAIEVAagnrlnnvvveddavakeaiellkrrkagratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDP 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1345 KASAAVKSA-------SNMES---QLTEAQQL-LEEETRQKLGL----SSKLRQIESEKEALQEQLEEDDEAKRNYERKL 1409
Cdd:TIGR02169 611 KYEPAFKYVfgdtlvvEDIEAarrLMGKYRMVtLEGELFEKSGAmtggSRAPRGGILFSRSEPAELQRLRERLEGLKREL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1410 AEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL 1489
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1490 EKKQKNFDKILAEEKA-----ISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQG 1564
Cdd:TIGR02169 771 EEDLHKLEEALNDLEArlshsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1565 TADKNVHELEKAKRALESQLAELKAQNEELEDDLQltedaklrlevnmqalrsqferDLLAKEEGAEEKRRGLVKQLRDL 1644
Cdd:TIGR02169 851 SIEKEIENLNGKKEELEEELEELEAALRDLESRLG----------------------DLKKERDELEAQLRELERKIEEL 908
|
810 820
....*....|....*....|....*....
gi 62471805 1645 ETELDEERKQRTAAVASKKKLEGDLKEIE 1673
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1058-1581 |
9.76e-21 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 99.75 E-value: 9.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1058 LAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIEtEVADLKEQLNERRVQVDEMQAQLAKREEELTQ 1137
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1138 TLLRIDEESATKATAQKAQRELESqLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELlDSLDTTAAQQELRSKREQ 1217
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI-NGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1218 ELATLKKSLEEETVNHEGvladmRHKHSQELNSINDQLENLRKAKTVLEKAKgtLEAENADLATELRSVNSSRQENDRRR 1297
Cdd:PRK03918 342 ELKKKLKELEKRLEELEE-----RHELYEEAKAKKEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1298 KQAESQIAELQVKLAEIERA---------------RSELQEKCTKlqqEAENITNQLEEAELKASAAVKSASNMESQLTE 1362
Cdd:PRK03918 415 GELKKEIKELKKAIEELKKAkgkcpvcgrelteehRKELLEEYTA---ELKRIEKELKEIEEKERKLRKELRELEKVLKK 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1363 AQQLLEEETrqklgLSSKLRQIESE-KEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEgkkrLN 1441
Cdd:PRK03918 492 ESELIKLKE-----LAEQLKELEEKlKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE----LE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1442 KDIEALERQVKELIAQNDRL-----DKSKKKIQS---------ELEDATIELEAQRTKV----LELEKKQKNFDKILAEE 1503
Cdd:PRK03918 563 KKLDELEEELAELLKELEELgfesvEELEERLKElepfyneylELKDAEKELEREEKELkkleEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1504 KAISEQIAQ-ERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALE 1581
Cdd:PRK03918 643 EELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
889-1618 |
1.25e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 889 EVTKQEEklVQKEDELKQVREKLDTLAKNTQEYERKYQQAL-VEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMM 967
Cdd:PTZ00121 1186 EVRKAEE--LRKAEDARKAEAARKAEEERKAEEARKAEDAKkAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 968 QELETRIEEEEERvlalggEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLL 1047
Cdd:PTZ00121 1264 HFARRQAAIKAEE------ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1048 EERANDLSQTLAEEEEKAKHLAKlKAKHEATISELeerlhKDQQQRQESDRSKRKIET--EVADLKEQLNERRVQVDEMQ 1125
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAE-AAEEKAEAAEK-----KKEEAKKKADAAKKKAEEkkKADEAKKKAEEDKKKADELK 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1126 --AQLAKREEELTQTL--LRIDEESATKATAQKAQRELESQLAEIQ--EDLEAEKAARAKAEKVRRDLSEELEAlknell 1199
Cdd:PTZ00121 1412 kaAAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKA------ 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1200 DSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQElnsinDQLENLRKAKTVlEKAKGTLEAENADL 1279
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEA-----KKADEAKKAEEK-KKADELKKAEELKK 1559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1280 ATELRSVNSSRQENDRRRKQAESqiAELqvkLAEIERARSElqekctklqqeaENITNQLEEAELKASAAVKSasnmESQ 1359
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRK--AEE---AKKAEEARIE------------EVMKLYEEEKKMKAEEAKKA----EEA 1618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1360 LTEAQQLLEEETRQKLGLSSKLRQIESEKEALQ-EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKK 1438
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEA 1698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1439 RLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKI---LAEEKAISEQIAQERD 1515
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlKKEEEKKAEEIRKEKE 1778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1516 TAEREA--REKETKVLSVSRELDEAFDKIEDLE-----------NKRKTLQNELDDLANTQGTADKNVHELEKAKRALES 1582
Cdd:PTZ00121 1779 AVIEEEldEEDEKRRMEVDKKIKDIFDNFANIIeggkegnlvinDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNN 1858
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 62471805 1583 QLAELKAQNEE-------LEDDLQLTEDAKLRLEVNMQALRSQ 1618
Cdd:PTZ00121 1859 ENGEDGNKEADfnkekdlKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1060-1895 |
2.94e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 99.06 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1060 EEEEKAKHLAKLKAKHEATISElEERLHKDQQQRQESDRskRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTL 1139
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAE-EARKAEEAKKKAEDAR--KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1140 LRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRdlseELEALKNELLDSLDTTAAQQELRSKREQel 1219
Cdd:PTZ00121 1168 EARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK----AEEARKAEDAKKAEAVKKAEEAKKDAEE-- 1241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1220 atlKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVlEKAKGTLEAENADLATELRSVNSSRQENDRRRK- 1298
Cdd:PTZ00121 1242 ---AKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADEL-KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKa 1317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1299 -QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEE-----ETR 1372
Cdd:PTZ00121 1318 dEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadEAK 1397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1373 QKLGLSSK----LRQIESEKEALQEQLEEDDEAKRNYE-RKLAEVTTQMQEIKKKAEE---------DADLAKELEEGKK 1438
Cdd:PTZ00121 1398 KKAEEDKKkadeLKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEakkaeeakkKAEEAKKADEAKK 1477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1439 RLN--KDIEALERQVKELIAQNDRLDKSK--KKIQSELEDATIELEAQRTKVLELEKKQKNFDKilAEEKAISEQI---- 1510
Cdd:PTZ00121 1478 KAEeaKKADEAKKKAEEAKKKADEAKKAAeaKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK--AEEKKKADELkkae 1555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1511 ----AQERDTAEREAREKETKVLSVSR---------ELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAK 1577
Cdd:PTZ00121 1556 elkkAEEKKKAEEAKKAEEDKNMALRKaeeakkaeeARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1578 RALESQLAELKAQNEELEDDlqlTEDAKLRLEvnmqalrsqferDLLAKEEgaEEKRRGlvKQLRDLETELDEERKQRTA 1657
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKA---EEENKIKAA------------EEAKKAE--EDKKKA--EEAKKAEEDEKKAAEALKK 1696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1658 AVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKA------AKEELQALSKEAERKVKALEAE 1731
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakkdeeEKKKIAHLKKEEEKKAEEIRKE 1776
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1732 VLQLTEDLASSERARRAAETERD-----ELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEvlldrsrKAQ 1806
Cdd:PTZ00121 1777 KEAVIEEELDEEDEKRRMEVDKKikdifDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEA-------DAF 1849
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1807 LQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKA 1886
Cdd:PTZ00121 1850 EKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDA 1929
|
....*....
gi 62471805 1887 NRKMDKKIK 1895
Cdd:PTZ00121 1930 EETREEIIK 1938
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1210-1684 |
5.80e-20 |
|
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: 97.01 E-value: 5.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1210 ELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSqELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSS 1289
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEK-ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1290 R----------QENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQ 1359
Cdd:TIGR04523 196 LlklelllsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1360 LTEAQQLLEEETRQKLGLSSKLRQIESEKEA-----LQEQLEEDDEAKRNYE---------------------------- 1406
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQnqisqnnkiisqlneqisqlkkeltnse 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1407 -------RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIEL 1479
Cdd:TIGR04523 356 sensekqRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETI 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1480 EAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1559
Cdd:TIGR04523 436 IKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDL 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1560 ANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQ----------ALRSQFERDLLAKEEg 1629
Cdd:TIGR04523 516 TKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieelkqtqksLKKKQEEKQELIDQK- 594
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 1630 aEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIEttmEMHNKVKE 1684
Cdd:TIGR04523 595 -EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK---SKKNKLKQ 645
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1350-1892 |
2.43e-19 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 95.13 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1350 VKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRnyerKLAEVTTQMQEIKKKAEEDADL 1429
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE----EIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1430 AKELEEGKKRLNKDIEALERQVKE-------------LIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNF 1496
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKElkelkekaeeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1497 DKILAEEKAISEQIA--QERDTAEREAREKETKVLSVSREL-----DEAFDKIEDLENKRKTLQNELDDLANTQGTADKN 1569
Cdd:PRK03918 341 EELKKKLKELEKRLEelEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1570 VHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNmqalrsqferDLLAKEEGAEEKRRGLVKQLRDLETELD 1649
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELK----------RIEKELKEIEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1650 EERKqrtaaVASKKKLEGDLKEIETTMEMHN--KVKEDA--LKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKV 1725
Cdd:PRK03918 491 KESE-----LIKLKELAEQLKELEEKLKKYNleELEKKAeeYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1726 KALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKA 1805
Cdd:PRK03918 566 DELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1806 QLQIEQLttelaNEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKvkatiATLEAKIANLEEQLENEGKERLLQQK 1885
Cdd:PRK03918 646 RKELEEL-----EKKYSEEEYEELREEYLELSRELAGLRAELEELEKRR-----EEIKKTLEKLKEELEEREKAKKELEK 715
|
....*..
gi 62471805 1886 ANRKMDK 1892
Cdd:PRK03918 716 LEKALER 722
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1390-1959 |
4.19e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 94.34 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1390 ALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlaKELEEGKKRLNkdieALERQVKELIAQNDRLDKSKKKIQ 1469
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEE-----KEEKDLHERLN----GLESELAELDEEIERYEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1470 SELEDATIELEAQRTKVLELEKKQKNFDKiLAEEKAISEQiaqERDTAEREAREKETKVLSVSRELDEAFDK-------- 1541
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELETLEAEIED-LRETIAETER---EREELAEEVRDLRERLEELEEERDDLLAEaglddada 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1542 ------IEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQAL 1615
Cdd:PRK02224 310 eavearREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1616 RSQFErDLLAKEEGAEEkrrglvkQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEmhnkvKEDALKHAKKLQA 1695
Cdd:PRK02224 390 EEEIE-ELRERFGDAPV-------DLGNAEDFLEELREERDELREREAELEATLRTARERVE-----EAEALLEAGKCPE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1696 ---QVKDALRDAEEAkaakeelqalskEAERKVKALEAEVLQLTEdlassERARRAAETERDELAEEIANNANKgslmID 1772
Cdd:PRK02224 457 cgqPVEGSPHVETIE------------EDRERVEELEAELEDLEE-----EVEEVEERLERAEDLVEAEDRIER----LE 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1773 EKR-RLEARIATLEEELEEEQSNSEVLldRSRKAQLQIEQLTTELANEKSNSQKNENGRALlerqnKELKAKLAEIetAQ 1851
Cdd:PRK02224 516 ERReDLEELIAERRETIEEKRERAEEL--RERAAELEAEAEEKREAAAEAEEEAEEAREEV-----AELNSKLAEL--KE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1852 RTKVKATIATLEAKIANLEEQLEnEGKERLLQQKAnrkmdkkikeltmnIEDERRhvdqhkEQMDKLNSRIKLLKRNLDE 1931
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIE-RLREKREALAE--------------LNDERR------ERLAEKRERKRELEAEFDE 645
|
570 580
....*....|....*....|....*....
gi 62471805 1932 TE-EELQKEKTQKRKYQRECEDMIESQEA 1959
Cdd:PRK02224 646 ARiEEAREDKERAEEYLEQVEEKLDELRE 674
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
883-1700 |
4.30e-18 |
|
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: 91.57 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 883 KVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIE-LCAEAEESRSRLMARKQ 961
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLkLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 962 ELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEA-ARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKL 1040
Cdd:pfam02463 251 EEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEeLKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1041 LKEKKLLEERANdlsqtlaEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQ 1120
Cdd:pfam02463 331 KKEKEEIEELEK-------ELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1121 VDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELL- 1199
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLq 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1200 --DSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQEL----------NSINDQLENLRKAKTVLEK 1267
Cdd:pfam02463 484 eqLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLgvavenykvaISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1268 AKGTL-EAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEI------ERARSELQEKCTKLQQEAENITNQLE 1340
Cdd:pfam02463 564 QKLVRaLTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKAtleadeDDKRAKVVEGILKDTELTKLKESAKA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1341 EAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYE---RKLAEVTTQMQ 1417
Cdd:pfam02463 644 KESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKeelKKLKLEAEELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1418 EIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFD 1497
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1498 KILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAK 1577
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1578 RALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTA 1657
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 62471805 1658 AVASKKKLEGdLKEIETTMEMHNKVKEDALKHAKKLQAQVKDA 1700
Cdd:pfam02463 964 RLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERLEEEKK 1005
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1339-1919 |
3.98e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 88.43 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1339 LEEAELKAsaAVKSASNMESQLTEAQQLLEEETRQKlglsSKLRQIESEKEALQEQLEEDDEAKrnYERKLAEV---TTQ 1415
Cdd:COG4913 218 LEEPDTFE--AADALVEHFDDLERAHEALEDAREQI----ELLEPIRELAERYAAARERLAELE--YLRAALRLwfaQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1416 MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD-KSKKKIQSELEDATIELEAQRTKVLELEKKQK 1494
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1495 NFD-KILAEEKAISEQIAQERDTAEREAREKEtkvlSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHEL 1573
Cdd:COG4913 370 ALGlPLPASAEEFAALRAEAAALLEALEEELE----ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1574 ekaKRALESQL----------AEL---KAQNEE----------------------LEDDLQLTEDAKLRLEVNMQ----- 1613
Cdd:COG4913 446 ---RDALAEALgldeaelpfvGELievRPEEERwrgaiervlggfaltllvppehYAAALRWVNRLHLRGRLVYErvrtg 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1614 ---ALRSQFERDLLAKE-------------------------EGAEEKRR--------GLVKQLRDLEtELDEERKQRTA 1657
Cdd:COG4913 523 lpdPERPRLDPDSLAGKldfkphpfrawleaelgrrfdyvcvDSPEELRRhpraitraGQVKGNGTRH-EKDDRRRIRSR 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1658 AV---ASKKKLEGDLKEIETTmemhnkvkEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALS------KEAERKVKAL 1728
Cdd:COG4913 602 YVlgfDNRAKLAALEAELAEL--------EEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAEL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1729 EAEVLQLTE---DLASSERARRAAETERDELAEEIAnnankgsLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKA 1805
Cdd:COG4913 674 EAELERLDAssdDLAALEEQLEELEAELEELEEELD-------ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1806 Q-LQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRT---KVKATIATLEAKIANLEE------QLEN 1875
Cdd:COG4913 747 LrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrEWPAETADLDADLESLPEylalldRLEE 826
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 62471805 1876 EG----KERLLQQKaNRKMDKKIKELTMNIEDERRHVdqhKEQMDKLN 1919
Cdd:COG4913 827 DGlpeyEERFKELL-NENSIEFVADLLSKLRRAIREI---KERIDPLN 870
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
908-1767 |
4.83e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 88.10 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 908 REKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLA-LGG 986
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDyLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 987 EKKKLELNIQDLEEQLEEEEAARQKLQLEK---VQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEE 1063
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1064 KAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRID 1143
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1144 EESATKATAQKAQR---ELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELA 1220
Cdd:pfam02463 395 EELELKSEEEKEAQlllELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1221 TLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEA---ENADLATELRSVNSSRQENDRRR 1297
Cdd:pfam02463 475 KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgrlGDLGVAVENYKVAISTAVIVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1298 KQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLL----EEETRQ 1373
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVvegiLKDTEL 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1374 KLGLSSKLRQIESEKEALQEQLEEDDEAKRNYE-RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDiEALERQVK 1452
Cdd:pfam02463 635 TKLKESAKAKESGLRKGVSLEEGLAEKSEVKASlSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE-QREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1453 ELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvlSVS 1532
Cdd:pfam02463 714 KLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL----KVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1533 RELDEAFDKIEDLENKRKTLQNELDDLANTQGtadknvhELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNM 1612
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQ-------LLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEE 862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1613 QALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKK 1692
Cdd:pfam02463 863 ITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLL 942
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1693 LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKAL--------EAEVLQLTEDLASSERARRAAETERDELAEEIANNA 1764
Cdd:pfam02463 943 EEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMaieefeekEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
...
gi 62471805 1765 NKG 1767
Cdd:pfam02463 1023 LEL 1025
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1319-1974 |
2.97e-16 |
|
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: 85.07 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1319 SELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEED 1398
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKND 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1399 DEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIE 1478
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1479 LEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLsvsrELDEAFDKIEDLENKRKTLQNELDD 1558
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT----EISNTQTQLNQLKDEQNKIKKQLSE 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1559 LANTQGTADKNVHELEKAKRALESQLAELKAQNEeleddlqltedaklrlevnmQALRSQFERDLLAKEegaeekrrglv 1638
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--------------------QDWNKELKSELKNQE----------- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1639 KQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTmemhNKVKEDALKhakKLQAQVKDALRDAEEAKAAKEELQALS 1718
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE----NSEKQRELE---EKQNEIEKLKKENQSYKQEIKNLESQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1719 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVL 1798
Cdd:TIGR04523 394 NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1799 LDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRtKVKATIATLEAKIANLEEQLE--NE 1876
Cdd:TIGR04523 474 SRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE-KLESEKKEKESKISDLEDELNkdDF 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1877 GKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNL-------DETEEELQKEKTQKRKYQRE 1949
Cdd:TIGR04523 553 ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIeekekkiSSLEKELEKAKKENEKLSSI 632
|
650 660
....*....|....*....|....*
gi 62471805 1950 CEDMIESQEAMNREINSLKTKLRRT 1974
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEI 657
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1184-1703 |
3.28e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.35 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1184 RRDLSEELEALKnELLDSLDttAAQQELRSKREQ--------ELATLKKSLEEETVNHEGVLADMRH-KHSQELNSINDQ 1254
Cdd:COG4913 220 EPDTFEAADALV-EHFDDLE--RAHEALEDAREQiellepirELAERYAAARERLAELEYLRAALRLwFAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1255 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQEND-RRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAE 1333
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1334 NITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQklgLSSKLRQIESEKEALQE-------------------- 1393
Cdd:COG4913 377 ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD---LRRELRELEAEIASLERrksniparllalrdalaeal 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1394 --------------QLEEDDEAKRN------------------YERKLAE---------------VTTQMQEIKKKAEED 1426
Cdd:COG4913 454 gldeaelpfvgeliEVRPEEERWRGaiervlggfaltllvppeHYAAALRwvnrlhlrgrlvyerVRTGLPDPERPRLDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1427 ADLAKELE--EG------KKRLNK--------DIEALER---------QVK---ELIAQNDRLDK---------SKKKI- 1468
Cdd:COG4913 534 DSLAGKLDfkPHpfrawlEAELGRrfdyvcvdSPEELRRhpraitragQVKgngTRHEKDDRRRIrsryvlgfdNRAKLa 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1469 --QSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDT--AEREAREKETKVlsvsRELDEAFDKIED 1544
Cdd:COG4913 614 alEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasAEREIAELEAEL----ERLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1545 LENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKL---RLEVNMQALRSQFER 1621
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerFAAALGDAVERELRE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1622 DLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASkkklegDLKEIETTMEMHNKVKEDALkhaKKLQAQVKDAL 1701
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDA------DLESLPEYLALLDRLEEDGL---PEYEERFKELL 840
|
..
gi 62471805 1702 RD 1703
Cdd:COG4913 841 NE 842
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1007-1659 |
4.52e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 84.97 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1007 AARQKLQLEkvQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAE--EEEKAKHLAKLkAKHEATISELEE 1084
Cdd:COG4913 247 AREQIELLE--PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEelRAELARLEAEL-ERLEARLDALRE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1085 RLHKDQQQRQESD-RSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTqtllrideesATKATAQKAQRELESQL 1163
Cdd:COG4913 324 ELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP----------ASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1164 AEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELldsldttaaqQELRSKR---EQELATLKKSLEEETVNH------- 1233
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEAEI----------ASLERRKsniPARLLALRDALAEALGLDeaelpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1234 -----------------EGVLADMR------HKHSQELNSINDQLE-----NLRKAKTVLEKAKgTLEAENADLATEL-- 1283
Cdd:COG4913 464 gelievrpeeerwrgaiERVLGGFAltllvpPEHYAAALRWVNRLHlrgrlVYERVRTGLPDPE-RPRLDPDSLAGKLdf 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1284 --------------------------------RSV--------NSSRQENDRRRK---------QAESQIAELQVKLAEI 1314
Cdd:COG4913 543 kphpfrawleaelgrrfdyvcvdspeelrrhpRAItragqvkgNGTRHEKDDRRRirsryvlgfDNRAKLAALEAELAEL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1315 ERARSELQEKCTKLQQEAENITNQLeeaelkasaavksasnmesqltEAQQLLEEETRQKLGLSSKLRQIEsEKEALQEQ 1394
Cdd:COG4913 623 EEELAEAEERLEALEAELDALQERR----------------------EALQRLAEYSWDEIDVASAEREIA-ELEAELER 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1395 LEEDDEakrnyerKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELED 1474
Cdd:COG4913 680 LDASSD-------DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1475 ATIELEAQRTKvlelekkqknfdkilaeEKAISEQIAQERDTAEREAREKETKVL-----------SVSRELDEAFDKIE 1543
Cdd:COG4913 753 ERFAAALGDAV-----------------ERELRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLP 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1544 DLENKRKTLQNE--------LDDLANTQGTADKN--VHELEKAKRALESQLAELkaqNEELEdDLQLTEDAKLRLEVNMQ 1613
Cdd:COG4913 816 EYLALLDRLEEDglpeyeerFKELLNENSIEFVAdlLSKLRRAIREIKERIDPL---NDSLK-RIPFGPGRYLRLEARPR 891
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1614 ALRS--QFERDLLAKEEGAE-------EKRRGLVKQLRD-LETELDEERKQRTAAV 1659
Cdd:COG4913 892 PDPEvrEFRQELRAVTSGASlfdeelsEARFAALKRLIErLRSEEEESDRRWRARV 947
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1277-1973 |
6.81e-16 |
|
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: 84.25 E-value: 6.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1277 ADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKlQQEAENITNQLEEAELKASAAVKSASNM 1356
Cdd:pfam02463 186 AELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNE-ERIDLLQELLRDEQEEIESSKQEIEKEE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEaQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1436
Cdd:pfam02463 265 EKLAQV-LKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1437 KKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQrTKVLELEKKQKNFDKILAEEKAISEQIAQERDT 1516
Cdd:pfam02463 344 LKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA-AKLKEEELELKSEEEKEAQLLLELARQLEDLLK 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1517 AEREAREKETKVLSVSRELDEAFDKI----EDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNE 1592
Cdd:pfam02463 423 EEKKEELEILEEEEESIELKQGKLTEekeeLEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1593 ELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEI 1672
Cdd:pfam02463 503 SKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1673 ETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETE 1752
Cdd:pfam02463 583 LIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKS 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1753 RDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNEngRAL 1832
Cdd:pfam02463 663 EVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEE--LKL 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1833 LERQNKELKAKLAEIETAQRTKvKATIATLEAKIANLEEQLENEGKERLLQQKanrkmDKKIKELTMNIEDERRHVDQHK 1912
Cdd:pfam02463 741 LKQKIDEEEEEEEKSRLKKEEK-EEEKSELSLKEKELAEEREKTEKLKVEEEK-----EEKLKAQEEELRALEEELKEEA 814
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1913 EQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1973
Cdd:pfam02463 815 ELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1377-1973 |
4.94e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 81.26 E-value: 4.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1377 LSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLnKDIEALERQVKELIA 1456
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV-KELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1457 QNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEqIAQERDTAEREAREKETKVLSVSRELD 1536
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1537 EAFDKIEDLENKrktlqnelddlantqgtadknvhelEKAKRALESQLAELKAQNEELEDDLQLTEDAKlRLEVNMQALR 1616
Cdd:PRK03918 325 GIEERIKELEEK-------------------------EERLEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1617 sqferdllaKEEGAEEKRRgLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEmhnkvkedALKHAKKLQAQ 1696
Cdd:PRK03918 379 ---------KRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIE--------ELKKAKGKCPV 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1697 VKDALRDAEEAKaakeelqaLSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNAnkgslMIDEKRR 1776
Cdd:PRK03918 441 CGRELTEEHRKE--------LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-----LAEQLKE 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1777 LEARIATLEEELEEEQSNS-EVLLDRSRKAQLQIEQLTTELanEKSNSQKNEngRALLERQNKELKAKLAEIETAQRTKV 1855
Cdd:PRK03918 508 LEEKLKKYNLEELEKKAEEyEKLKEKLIKLKGEIKSLKKEL--EKLEELKKK--LAELEKKLDELEEELAELLKELEELG 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1856 KATIATLEAKIANLEEqLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETE-E 1934
Cdd:PRK03918 584 FESVEELEERLKELEP-FYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEyE 662
|
570 580 590
....*....|....*....|....*....|....*....
gi 62471805 1935 ELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1973
Cdd:PRK03918 663 ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKE 701
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
958-1848 |
5.61e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.25 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 958 ARKQELEDMMQELETRIEEEEER--VLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAK---IKKYEEDLAL 1032
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETLRqvRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSreiVKSYENELDP 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1033 TDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKE 1112
Cdd:TIGR00606 250 LKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1113 QLNERRVQVDEMQAQLAKREEELTQTLLRIDEESaTKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELE 1192
Cdd:TIGR00606 330 KLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI-RARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAK 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1193 ALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHS--QELNSINDQL----ENLRKAKTVLE 1266
Cdd:TIGR00606 409 TAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKelQQLEGSSDRIleldQELRKAERELS 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1267 KAKgtleaENADLATELRSVNSSRQEN---DRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE-- 1341
Cdd:TIGR00606 489 KAE-----KNSLTETLKKEVKSLQNEKadlDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDElt 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1342 AELKASAAVKSASNMESQLTEAQQLLEEETRQklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVT------TQ 1415
Cdd:TIGR00606 564 SLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK---LNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCgsqdeeSD 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1416 MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKN 1495
Cdd:TIGR00606 641 LERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKK 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1496 FDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELD---DLANTQGTADKNVHE 1572
Cdd:TIGR00606 721 KEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsakVCLTDVTIMERFQME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1573 LEKAKRALESQLAELKAQ---------NEELEDDLQLTEDAKLRLEVNMQALRSQFERDL-------------------L 1624
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQGSdldrtvqqvNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlksktnelkseklqigtnL 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1625 AKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDA 1704
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1705 EEAkaakeelqaLSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATL 1784
Cdd:TIGR00606 961 ENK---------IQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELK 1031
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1785 EEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIE 1848
Cdd:TIGR00606 1032 EVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
900-1593 |
5.90e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.25 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 900 KEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQeletrieeeee 979
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD----------- 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 980 RVLALGGE--KKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQT 1057
Cdd:TIGR00606 472 RILELDQElrKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1058 LAEEEEKAKHLAKLKAKHEATiSELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQ 1137
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFD 630
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1138 TLLRIDEESAT---KATAQKAQREL----------ESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELL---DS 1201
Cdd:TIGR00606 631 VCGSQDEESDLerlKEEIEKSSKQRamlagatavySQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRlapDK 710
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1202 LDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENaDLAT 1281
Cdd:TIGR00606 711 LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLT 789
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1282 ELRSVNSSRQENDRRRKQAESQIAELQVklAEIERARSELQEKCTKLQQEAENITNQLEEAelkasaavksasnmesqlt 1361
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQG--SDLDRTVQQVNQEKQEKQHELDTVVSKIELN------------------- 848
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1362 eaQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELE------- 1434
Cdd:TIGR00606 849 --RKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEkdqqeke 926
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1435 -------EGKKRLNKDIEALERQVKELIAQNDRLDkskKKIQSELEDATIELEAQRTKVL----ELEKKQKNFDKIL-AE 1502
Cdd:TIGR00606 927 elisskeTSNKKAQDKVNDIKEKVKNIHGYMKDIE---NKIQDGKDDYLKQKETELNTVNaqleECEKHQEKINEDMrLM 1003
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1503 EKAISEQIAQER---DTAEREAREKETKVLSVSR-----ELDEafDKIEDLENKRKTLQNELDDLANTQGTADKNVHELE 1574
Cdd:TIGR00606 1004 RQDIDTQKIQERwlqDNLTLRKRENELKEVEEELkqhlkEMGQ--MQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYE 1081
|
730
....*....|....*....
gi 62471805 1575 KAKRALESQLAELKAQNEE 1593
Cdd:TIGR00606 1082 KEIKHFKKELREPQFRDAE 1100
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1073-1686 |
5.98e-15 |
|
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: 81.04 E-value: 5.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1073 AKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLlrideeSATKATA 1152
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGEL------SAADAAV 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1153 QKAQRELES----QLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEE 1228
Cdd:pfam12128 318 AKDRSELEAledqHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKD 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1229 ETVN---------------HEGVLADMRHKHSQELNSINDQ------------------------LENLRKAKTVLEKAK 1269
Cdd:pfam12128 398 KLAKireardrqlavaeddLQALESELREQLEAGKLEFNEEeyrlksrlgelklrlnqatatpelLLQLENFDERIERAR 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1270 GTLEAENA---DLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIE-----RARSELQEKCTKLQQEAENITNQLEE 1341
Cdd:pfam12128 478 EEQEAANAeveRLQSELRQARKRRDQASEALRQASRRLEERQSALDELElqlfpQAGTLLHFLRKEAPDWEQSIGKVISP 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1342 AEL--------KASAAVKSASNMESQLTEAQQL-------LEEETRQKLGLSSKLRQIESEKEALQEqlEEDDEAKRNYE 1406
Cdd:pfam12128 558 ELLhrtdldpeVWDGSVGGELNLYGVKLDLKRIdvpewaaSEEELRERLDKAEEALQSAREKQAAAE--EQLVQANGELE 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1407 RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQndrLDKSKKKIQSELEDAtieLEAQRTKV 1486
Cdd:pfam12128 636 KASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS---LEAQLKQLDKKHQAW---LEEQKEQK 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1487 LELEKKQKNFDKILAEEK-----AISEQIAQERDTAERE--AREKETKVLSVSRELDEafDKIEDLENKRKTLQNELDDL 1559
Cdd:pfam12128 710 REARTEKQAYWQVVEGALdaqlaLLKAAIAARRSGAKAElkALETWYKRDLASLGVDP--DVIAKLKREIRTLERKIERI 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1560 ANTQGTA----DKNVHELEKAKRALESQLAELKAQNEELEDDL-QLTEDAKLRlevnmqalRSQFERDLlakeegaeekr 1634
Cdd:pfam12128 788 AVRRQEVlryfDWYQETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKLR--------RAKLEMER----------- 848
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1635 rglvKQLRDLETELDEErkqrtaavaskkklegdLKEIETTMEMHNKVKEDA 1686
Cdd:pfam12128 849 ----KASEKQQVRLSEN-----------------LRGLRCEMSKLATLKEDA 879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1298-1942 |
7.73e-15 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 80.45 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1298 KQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQlleeetrQKLGL 1377
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKE-------QKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1378 SSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALErqvKELIAQ 1457
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK---NKLLKL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1458 NDRLDKSKKKIQ--SELEDATIELEAQRTKVLE-LEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLsvsrE 1534
Cdd:TIGR04523 200 ELLLSNLKKKIQknKSLESQISELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQK----E 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1535 LDEAFDKIEDLENKRKTLQNELDDLAN-TQGTADKNVHE----LEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLE 1609
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNqKEQDWNKELKSelknQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1610 VNMQALRSQFE------RDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQrtaavasKKKLEGDLKEIETTMEMHNKVK 1683
Cdd:TIGR04523 356 SENSEKQRELEekqneiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKL-------NQQKDEQIKKLQQEKELLEKEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1684 EDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVlqltedlasserarRAAETERDELAEEIANN 1763
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI--------------NKIKQNLEQKQKELKSK 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1764 ANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELaneksNSQKNENGRALLErqnKELKAK 1843
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL-----NKDDFELKKENLE---KEIDEK 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1844 LAEIEtaqrtKVKATIATLEAKianleeqleNEGKERLLQQKANRKMD--KKIKELTMNIEDERRHVDQHKEQMDKLNSR 1921
Cdd:TIGR04523 567 NKEIE-----ELKQTQKSLKKK---------QEEKQELIDQKEKEKKDliKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
650 660
....*....|....*....|.
gi 62471805 1922 IKLLKRNLDETEEELQKEKTQ 1942
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKET 653
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1382-1975 |
1.51e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.96 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1382 RQIESEKEALQEQLEEDDEAKRNYERKLAEVTT--QMQEIKKKAEEDADLAKELEEGKKRLnkDIEALERQVKELIAQND 1459
Cdd:COG4913 221 PDTFEAADALVEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1460 RLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDkilAEEKaisEQIAQERDTAEREAREKETKVLSVSRELD--- 1536
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNG---GDRL---EQLEREIERLERELEERERRRARLEALLAalg 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1537 -EAFDKIEDLENKRKTLQNELDDLANTQgtadknvHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQAL 1615
Cdd:COG4913 373 lPLPASAEEFAALRAEAAALLEALEEEL-------EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1616 RSQFERDLLAKE-------------------EGAEEK------------------------RRGLVKQLRDLETELDEER 1652
Cdd:COG4913 446 RDALAEALGLDEaelpfvgelievrpeeerwRGAIERvlggfaltllvppehyaaalrwvnRLHLRGRLVYERVRTGLPD 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1653 KQRTAAVASK--KKLEGDLKEIETTMEMH-----NKVK---EDALKHAKK---LQAQVKD--ALRDAEEAKAAKEELQaL 1717
Cdd:COG4913 526 PERPRLDPDSlaGKLDFKPHPFRAWLEAElgrrfDYVCvdsPEELRRHPRaitRAGQVKGngTRHEKDDRRRIRSRYV-L 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1718 SKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELaeeiannankgslmiDEKRRLEARIATLEEELEEEQSnsev 1797
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---------------QERREALQRLAEYSWDEIDVAS---- 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1798 lldrsrkAQLQIEQLTTELAN-EKSNSQKNEngralLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENe 1876
Cdd:COG4913 666 -------AEREIAELEAELERlDASSDDLAA-----LEEQLEELEAELEELE-EELDELKGEIGRLEKELEQAEEELDE- 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1877 gkerlLQQKANRKMDKKIKELTMNIEDERRHVDQ---HKEQMDKLNSRIKLLKRNLDETEEELQKEKTQ-KRKYQRECED 1952
Cdd:COG4913 732 -----LQDRLEAAEDLARLELRALLEERFAAALGdavERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETAD 806
|
650 660
....*....|....*....|...
gi 62471805 1953 MIESQEAmNREINSLKTKLRRTG 1975
Cdd:COG4913 807 LDADLES-LPEYLALLDRLEEDG 828
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
893-1635 |
1.72e-14 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 79.63 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 893 QEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELET 972
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 973 RIEEEEERVLALGGEKKKLELNIQ------DLEEQLEEEEAARQ-----KLQLEKVQLDAKIKKYEEDLALTD------- 1034
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREaeeeeeEELEKLQEKLEQLEeellaKKKLESERLSSAAKLKEEELELKSeeekeaq 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1035 DQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQ-RQESDRSKRKIETEVADLKEQ 1113
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELElKKSEDLLKETQLVKLQEQLEL 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1114 LNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEA 1193
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVR 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1194 LKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNH-----EGVLADMRHKHSQELNSINDQLENLRKAKTVLEKA 1268
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLdkatlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1269 KGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIeraRSELQEKCTKLQQEAENITNQLEEAELKASA 1348
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEI---LRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1349 AVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAD 1428
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1429 LAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSE----LEDATIELEAQRTKVL---ELEKKQKNFDKILA 1501
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLeklaEEELERLEEEITKEELlqeLLLKEEELEEQKLK 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1502 EEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKaKRALE 1581
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE-ERNKR 964
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1582 SQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRR 1635
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQR 1018
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1238-1453 |
2.54e-14 |
|
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: 77.11 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1238 ADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERA 1317
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1318 RSELQEKCTKLQQEAENITNQLEEAEL----KASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQE 1393
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLlspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1394 QLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKE 1453
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1056-1913 |
3.08e-14 |
|
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: 78.84 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1056 QTLAEEEEKAKHLAKLKAKHEATISELEERLH--KDQQQR-QESDRSKRKIE---TEVADLKEQLNERRVQVDEMQAQLA 1129
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQaaSDHLNLvQTALRQQEKIEryqEDLEELTERLEEQEEVVEEAAEQLA 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1130 KREEELTQTLLRIDEesatkataqkaqreLESQLAEIQEDLEAEKAARAKAEKVRRDLsEELEALKNelLDSLDTTAAQQ 1209
Cdd:COG3096 379 EAEARLEAAEEEVDS--------------LKSQLADYQQALDVQQTRAIQYQQAVQAL-EKARALCG--LPDLTPENAED 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1210 ELRSKREQElatlkKSLEEETVNHEGVLADMRHKHSQelnsindqlenLRKAKTVLEKAKGTLEAENA-DLATELRSVNS 1288
Cdd:COG3096 442 YLAAFRAKE-----QQATEEVLELEQKLSVADAARRQ-----------FEKAYELVCKIAGEVERSQAwQTARELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1289 SRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQE---AENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1365
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQldaAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1366 LLEEETRQKlglsSKLRQIESEKEALQEQL----EEDDEAKRNyerkLAEVTTQMQEIkkkaeedADLAKELEEGKKRLN 1441
Cdd:COG3096 586 QLEQLRARI----KELAARAPAWLAAQDALerlrEQSGEALAD----SQEVTAAMQQL-------LEREREATVERDELA 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1442 KDIEALERQVKELI----AQNDRLDKSKKKIQSEL-----EDATIE--------------------LEAQRTKVLELEKk 1492
Cdd:COG3096 651 ARKQALESQIERLSqpggAEDPRLLALAERLGGVLlseiyDDVTLEdapyfsalygparhaivvpdLSAVKEQLAGLED- 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1493 qknfdkiLAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDL--------ENKRKTLQNELDDLANTQG 1564
Cdd:COG3096 730 -------CPEDLYLIEGDPDSFDDSVFDAEELEDAVVVKLSDRQWRYSRFPEVplfgraarEKRLEELRAERDELAEQYA 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1565 TADKNVHELEKAKRAL----------------ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFerDLLakee 1628
Cdd:COG3096 803 KASFDVQKLQRLHQAFsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQL--QLL---- 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1629 gaeekrRGLVKQL-----RDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKkLQAQVKDAlrd 1703
Cdd:COG3096 877 ------NKLLPQAnlladETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQ-LQADYLQA--- 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1704 aeeakaakeelQALSKEAERKVKALEaEVLQLTEDLASSERARRAAETErdELAEEIannanKGSLMIDEKRRLEARIAT 1783
Cdd:COG3096 947 -----------KEQQRRLKQQIFALS-EVVQRRPHFSYEDAVGLLGENS--DLNEKL-----RARLEQAEEARREAREQL 1007
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1784 LEEELEEEQSNSEVL-LDRSRKAQLQIEQ-LTTELANEKSNSQKNENGRALLERQnkELKAKLAEiETAQRTKVKATIAT 1861
Cdd:COG3096 1008 RQAQAQYSQYNQVLAsLKSSRDAKQQTLQeLEQELEELGVQADAEAEERARIRRD--ELHEELSQ-NRSRRSQLEKQLTR 1084
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1862 LEAKIANLEEQLenegkerllqqkanRKMDKKIKeltmnieDERRHVDQHKE 1913
Cdd:COG3096 1085 CEAEMDSLQKRL--------------RKAERDYK-------QEREQVVQAKA 1115
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
892-1530 |
3.72e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.57 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 892 KQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEdmmqELE 971
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE----ELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 972 TRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQlEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERA 1051
Cdd:PRK03918 238 EEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE-EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1052 NDLSQTLAEEEEKAKHLAKLKAKHEAT---ISELEERLHKDQQQRQESDRSKRKiETEVADLKEQLNERRVQ-VDEMQAQ 1127
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELkkkLKELEKRLEELEERHELYEEAKAK-KEELERLKKRLTGLTPEkLEKELEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1128 LAKREEELTQTLLRIDEESAtkataqkaqrELESQLAEIQEDLEAEKAARAKAEKVRRDLSEE-----LEALKNELLDSL 1202
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIG----------ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1203 DTTAAQQELRSKREQELATLKKSLEEE-TVNHEGVLADMRHKHSQELNSINdqLENLRKAKTVLEKAKGTLeaenADLAT 1281
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKVLKKEsELIKLKELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKL----IKLKG 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1282 ELRSVNSSRQEndrrrkqaesqIAELQVKLAEIERARSELQEKCTKLQQEAENItnqleeaelkasaAVKSASNMESQLT 1361
Cdd:PRK03918 540 EIKSLKKELEK-----------LEELKKKLAELEKKLDELEEELAELLKELEEL-------------GFESVEELEERLK 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1362 EaqqlLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAkrnyERKLAEVTTQMQEIKKKAEEdadLAKEL-EEGKKRL 1440
Cdd:PRK03918 596 E----LEPFYNEYLELKDAEKELEREEKELKKLEEELDKA----FEELAETEKRLEELRKELEE---LEKKYsEEEYEEL 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1441 NKDIEALERQVKELIAQNDRLDKSKKKIQSELEDatieLEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAERE 1520
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEK----LKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
650
....*....|
gi 62471805 1521 AREKETKVLS 1530
Cdd:PRK03918 741 ALSKVGEIAS 750
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
889-1453 |
4.19e-14 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 78.18 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 889 EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYER---KYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELED 965
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEElkeEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 966 MMQeLETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEdlalTDDQNQKLLKEKK 1045
Cdd:PRK03918 281 KVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1046 LLEERANDLSQTLAEEEEKAKHLAKLKAKheaTISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQ 1125
Cdd:PRK03918 356 ELEERHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1126 AQLAK------------REEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKaekvrRDLSEELEA 1193
Cdd:PRK03918 433 KAKGKcpvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKL-----KELAEQLKE 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1194 LKNEL--LDSLDTTAAQQELRSKREqELATLKKSLEeetvnhegvladmrhkhsqELNSINDQLENLRKAKTVLEKAKGT 1271
Cdd:PRK03918 508 LEEKLkkYNLEELEKKAEEYEKLKE-KLIKLKGEIK-------------------SLKKELEKLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1272 LEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAElkasaavK 1351
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE-------K 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1352 SASNMESQLTEAQQLLEEETRQKlgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAK 1431
Cdd:PRK03918 641 RLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEK 718
|
570 580
....*....|....*....|..
gi 62471805 1432 ELEEgKKRLNKDIEALERQVKE 1453
Cdd:PRK03918 719 ALER-VEELREKVKKYKALLKE 739
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1098-1499 |
1.16e-13 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 77.03 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1098 RSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAAR 1177
Cdd:TIGR02169 660 RAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1178 AKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEEtvnhegvladmrhkhsqELNSINDQLEN 1257
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS-----------------RIPEIQAELSK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1258 LrkaktvlekakgtlEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN 1337
Cdd:TIGR02169 803 L--------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1338 QLEEAELKASAAVKSASNMESQLTEAQQLLEEetrqklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQ 1417
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRE-------LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKG 941
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1418 EIKKKAEEDADLAKeLEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKN-- 1495
Cdd:TIGR02169 942 EDEEIPEEELSLED-VQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREvf 1020
|
....*..
gi 62471805 1496 ---FDKI 1499
Cdd:TIGR02169 1021 meaFEAI 1027
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1019-1619 |
1.81e-13 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 75.83 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1019 LDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKheatISELEERLHKDQQQRQESDR 1098
Cdd:TIGR04523 164 LKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQ----ISELKKQNNQLKDNIEKKQQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1099 SKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEesatkataqkaqreLESQLAEIQEDLEAEKAARA 1178
Cdd:TIGR04523 240 EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE--------------LEKQLNQLKSEISDLNNQKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1179 KAEKvrRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHegvladmrhkhsqelNSINDQLENL 1258
Cdd:TIGR04523 306 QDWN--KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESEN---------------SEKQRELEEK 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1259 RKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQ 1338
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQ 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1339 LEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQ- 1417
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEk 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1418 ---EIKKKAEEDADLAKELEEGKKRLNKD-----IEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL 1489
Cdd:TIGR04523 529 lesEKKEKESKISDLEDELNKDDFELKKEnlekeIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1490 EKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADK- 1568
Cdd:TIGR04523 609 EKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKe 688
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1569 -NVHELEKAKRALESQ-LAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQF 1619
Cdd:TIGR04523 689 lSLHYKKYITRMIRIKdLPKLEEKYKEIEKELKKLDEFSKELENIIKNFNKKF 741
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1246-1640 |
2.21e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1246 QELNSINDQLENLRKAKTVLEKAKGTLEA--ENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQE 1323
Cdd:COG4717 95 EELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1324 KCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEEtrqklglsskLRQIESEKEALQEQLEEDDEAKR 1403
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE----------LEELEEELEQLENELEAAALEER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1404 NYERK--------LAEVTTQMQEIKKKAEEDADLAKELEE----GKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSE 1471
Cdd:COG4717 245 LKEARlllliaaaLLALLGLGGSLLSLILTIAGVLFLVLGllalLFLLLAREKASLGKEAEELQALPALEELEEEELEEL 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1472 LEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVlsvsrELDEAFDKIEDLENKRKT 1551
Cdd:COG4717 325 LAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-----EDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1552 LQNELDDLANTQGTADKNVHELEKA--KRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFE-RDLLAKEE 1628
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGElAELLQELE 479
|
410
....*....|..
gi 62471805 1629 GAEEKRRGLVKQ 1640
Cdd:COG4717 480 ELKAELRELAEE 491
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1295-1781 |
2.31e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 75.85 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1295 RRRKQAESQIAELQVKLAEIERArsELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEetrqk 1374
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREE----- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1375 lglsskLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIkkkAEEDADLAKELEEGkkrlNKDIEALERQVKEL 1454
Cdd:PRK02224 253 ------LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL---EEERDDLLAEAGLD----DADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1455 IAQN----DRLDKSKKKIQ---SELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETK 1527
Cdd:PRK02224 320 EDRDeelrDRLEECRVAAQahnEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1528 VLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEK----------------------------AKRA 1579
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvegsphvetieedreRVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1580 LESQLAELKAQNEELEDDLQLTEDAKlRLEVNMQALRSQFER--DLLA-KEEGAEEKR---RGLVKQLRDLETELDEERK 1653
Cdd:PRK02224 480 LEAELEDLEEEVEEVEERLERAEDLV-EAEDRIERLEERREDleELIAeRRETIEEKReraEELRERAAELEAEAEEKRE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1654 QRTAAVASKKKLEGDLKEIETTMEmHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVL 1733
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLA-ELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKR 637
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 62471805 1734 QLTEDLasSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARI 1781
Cdd:PRK02224 638 ELEAEF--DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
959-1829 |
5.63e-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: 74.62 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 959 RKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQ 1038
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1039 KLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEE-RLHKDQQQRQESDRSKRKIETEVADLKEQLNER 1117
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEkKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1118 RVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELE-SQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKN 1196
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1197 ELLDSLDTTAAQQELRSKREQELATLKKSLEEETVnhEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAEN 1276
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL--EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSED 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1277 ADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNM 1356
Cdd:pfam02463 473 LLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ES----QLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIK-----KKAEEDA 1427
Cdd:pfam02463 553 VSatadEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvvEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1428 DLAKELEEGKKRLNKDIEAleRQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAIS 1507
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKG--VSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1508 EQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAEL 1587
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1588 KAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEG 1667
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1668 DLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARR 1747
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1748 AAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNE 1827
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSIN 1030
|
..
gi 62471805 1828 NG 1829
Cdd:pfam02463 1031 KG 1032
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
887-1459 |
7.69e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.92 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 887 LLEVTKQEEKLVQKE--DELKQVREKLDTLAKNTQEYERKYQQAlvekttlAEQLQAEIELCAEAEESRSRLMARKQELE 964
Cdd:PRK02224 189 LDQLKAQIEEKEEKDlhERLNGLESELAELDEEIERYEEQREQA-------RETRDEADEVLEEHEERREELETLEAEIE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 965 DMMQELETRIEeeeervlalggEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYE---EDLALTDDQNQKLL 1041
Cdd:PRK02224 262 DLRETIAETER-----------EREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEarrEELEDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1042 KEKKLLEERANDLSQTLAEEEEKAKHLAKlKAKHEAtiSELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQV 1121
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAE-ELREEA--AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1122 DEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLA-----EIQEDLEAEKAARAKAEkvRRDLSEELEALKN 1196
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEagkcpECGQPVEGSPHVETIEE--DRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1197 ELLDSLDTTAAQQElRSKREQELATLKKSLEEETVNHEGVLADmrhkHSQELNSINDQLENLRKAKTVLE-------KAK 1269
Cdd:PRK02224 486 DLEEEVEEVEERLE-RAEDLVEAEDRIERLEERREDLEELIAE----RRETIEEKRERAEELRERAAELEaeaeekrEAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1270 GTLEAENADLATELRSVNSSRQENDRRRKQAEsQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE-----AEL 1344
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLE-RIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEkrerkREL 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1345 KAS---AAVKSASNMESQLTEAQQLLEEETR----QKLGLSSKLRQIESEKEALQEQLEEDD--EAKRNYERKLAEVTTQ 1415
Cdd:PRK02224 640 EAEfdeARIEEAREDKERAEEYLEQVEEKLDelreERDDLQAEIGAVENELEELEELRERREalENRVEALEALYDEAEE 719
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 62471805 1416 MQEIKkkaeedADLAKELEegkkrlNKDIEALER---QVKELIAQND 1459
Cdd:PRK02224 720 LESMY------GDLRAELR------QRNVETLERmlnETFDLVYQND 754
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1300-1532 |
1.13e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1300 AESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSs 1379
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1380 klRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQND 1459
Cdd:COG4942 97 --AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1460 RLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVS 1532
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1064-1480 |
2.30e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.79 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1064 KAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEV-------ADLKEQLNERRVQVDEMQAQLAKREEELT 1136
Cdd:TIGR02169 661 APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsqelSDASRKIGEIEKEIEQLEQEEEKLKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1137 QTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAekaarakaekvrrdLSEELEALKNELLDSldttaaqqelrskRE 1216
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHK--------------LEEALNDLEARLSHS-------------RI 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1217 QELATLKKSLEEETVNHEGVLADMrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRR 1296
Cdd:TIGR02169 794 PEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1297 RKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLG 1376
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1377 LSSkLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEedadlakELEEGKKRLNKDIEALERQVKELIA 1456
Cdd:TIGR02169 950 ELS-LEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA-------KLEEERKAILERIEEYEKKKREVFM 1021
|
410 420
....*....|....*....|....*
gi 62471805 1457 QN-DRLDKSKKKIQSELEDATIELE 1480
Cdd:TIGR02169 1022 EAfEAINENFNEIFAELSGGTGELI 1046
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1255-1753 |
4.10e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 71.34 E-value: 4.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1255 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEN 1334
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1335 ITNQLEEAELKASAAvksasNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNyerklaevtt 1414
Cdd:COG4717 128 LPLYQELEALEAELA-----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1415 QMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKsKKKIQSELedATIELEAQRTKVLELEKKQK 1494
Cdd:COG4717 193 ELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL-EERLKEAR--LLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1495 NFDKILAEEKAISEQIAqerdTAEREAREKETKVLSVSRELDEAFDKIEDLENKRktLQNELDDLANTQGTADKNVHELE 1574
Cdd:COG4717 270 SLILTIAGVLFLVLGLL----ALLFLLLAREKASLGKEAEELQALPALEELEEEE--LEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1575 KAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQAlrsqfERDLLAKEEGAEEKRRgLVKQLRDLETELDEERKQ 1654
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED-----EEELRAALEQAEEYQE-LKEELEELEEQLEELLGE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1655 RTAAVA--SKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKeelQALSKEAERKVKALEAEV 1732
Cdd:COG4717 418 LEELLEalDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQ---ELEELKAELRELAEEWAA 494
|
490 500
....*....|....*....|.
gi 62471805 1733 LQLTEDLAssERARRAAETER 1753
Cdd:COG4717 495 LKLALELL--EEAREEYREER 513
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
885-1659 |
8.15e-12 |
|
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: 70.85 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 885 KPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAE------------QLQAEIELCAEAEES 952
Cdd:TIGR00606 326 RELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpfserQIKNFHTLVIERQED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 953 RSRLMARK-QELEDMMQELETRIEEEEERVLALGG----EKKKLELNIQDLEEQLEEEEAARQKLQlEKVQLDAKIKKYE 1027
Cdd:TIGR00606 406 EAKTAAQLcADLQSKERLKQEQADEIRDEKKGLGRtielKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAE 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1028 EDLALTDDQNQKLLKEKKLLEERAN--DLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIET 1105
Cdd:TIGR00606 485 RELSKAEKNSLTETLKKEVKSLQNEkaDLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1106 EVAD------LKEQLNERRVQVDEMQAQLAKREEELTQTllrideeSATKATAQKAQRELESQLAEIQEDLEAEKAArak 1179
Cdd:TIGR00606 565 LLGYfpnkkqLEDWLHSKSKEINQTRDRLAKLNKELASL-------EQNKNHINNELESKEEQLSSYEDKLFDVCGS--- 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1180 aekvrRDLSEELEALKNELLDS---LDTTAAQQELRSKREQELATLKKS---LEEETVNHEGVLADMRHKHSQELNSIND 1253
Cdd:TIGR00606 635 -----QDEESDLERLKEEIEKSskqRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPD 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1254 QLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIER------ARSELQEKCTK 1327
Cdd:TIGR00606 710 KLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimPEEESAKVCLT 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1328 LQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKlglssKLRQIESEKEALQEQLEEDDEAKRNYER 1407
Cdd:TIGR00606 790 DVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQH-----ELDTVVSKIELNRKLIQDQQEQIQHLKS 864
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1408 KLAEVTTQMQEIKKKAEEDADLAKELEEgkkrLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKV- 1486
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVE----LSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAq 940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1487 LELEKKQKNFDKILAEEKAISEQIaqeRDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDD------LA 1560
Cdd:TIGR00606 941 DKVNDIKEKVKNIHGYMKDIENKI---QDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkiqerWL 1017
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1561 NTQGTADKNVHELEKAKRAL--------ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQ---FERDLLAKE-E 1628
Cdd:TIGR00606 1018 QDNLTLRKRENELKEVEEELkqhlkemgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEikhFKKELREPQfR 1097
|
810 820 830
....*....|....*....|....*....|....
gi 62471805 1629 GAEEKRRGLVKQLRDLE---TELDEERKQRTAAV 1659
Cdd:TIGR00606 1098 DAEEKYREMMIVMRTTElvnKDLDIYYKTLDQAI 1131
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
879-1613 |
8.18e-12 |
|
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: 70.52 E-value: 8.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 879 RLYTKVKPLLEVTKQ-----EEKLVQKEDELKQVREKLDTLAKNTQEYE-------RKYQQALVEKTTLAEQLQAEIELC 946
Cdd:pfam05483 78 RLYSKLYKEAEKIKKwkvsiEAELKQKENKLQENRKIIEAQRKAIQELQfenekvsLKLEEEIQENKDLIKENNATRHLC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 947 AEAEESRSRLMARKQELEdmmqeleTRIEEEEERVLALGGEKKKLELNIQDLeeqleeeeaarqKLQLEKVQLDAKIKkY 1026
Cdd:pfam05483 158 NLLKETCARSAEKTKKYE-------YEREETRQVYMDLNNNIEKMILAFEEL------------RVQAENARLEMHFK-L 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1027 EEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETE 1106
Cdd:pfam05483 218 KEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1107 VADLKEQLnERRVQVdemQAQLAKREEELTQTLLRIDEESAT--------KATAQKAQRELESQLAEIQEDLEAEKAARA 1178
Cdd:pfam05483 298 LEDIKMSL-QRSMST---QKALEEDLQIATKTICQLTEEKEAqmeelnkaKAAHSFVVTEFEATTCSLEELLRTEQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1179 KAEKVRRDLSEELEALKNELLDsldttaaQQELRSKREQELATLKKSL-EEETVNHEgvladmrhkhSQELNSINDQLEN 1257
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEE-------MTKFKNNKEVELEELKKILaEDEKLLDE----------KKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1258 LRKAKTVLEKAKgtlEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN 1337
Cdd:pfam05483 437 KEQELIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1338 QLEEAELKASAAVKSASNMESQLteaQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQ 1417
Cdd:pfam05483 514 ELKKHQEDIINCKKQEERMLKQI---ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1418 EIKKKAEedaDLAKELEEGkkrlNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL-EKKQKNF 1496
Cdd:pfam05483 591 ILENKCN---NLKKQIENK----NKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIiDNYQKEI 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1497 DKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDdlaNTQGTADKNVHELEKA 1576
Cdd:pfam05483 664 EDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERD---SELGLYKNKEQEQSSA 740
|
730 740 750
....*....|....*....|....*....|....*..
gi 62471805 1577 KRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQ 1613
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
887-1944 |
1.85e-11 |
|
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: 69.76 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 887 LLEVTKQEEKLVQKEDELKQVREKLD-TLAKNTQEYERKYQQALVEKTTLAE----QLQAEIELCAEAEESRSRLMARKQ 961
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKfYLRQSVIDLQTKLQEMQMERDAMADirrrESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 962 ELEDMMQELETRIEEEEERVLALGG---EKKKLELNIQDLEEQLEEEEAARQKLQLEKV---------QLDAKIKKYEED 1029
Cdd:pfam15921 160 LKEDMLEDSNTQIEQLRKMMLSHEGvlqEIRSILVDFEEASGKKIYEHDSMSTMHFRSLgsaiskilrELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1030 LALTDDQ-----NQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESD----RSK 1100
Cdd:pfam15921 240 IFPVEDQlealkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNsmymRQL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1101 RKIETEVADLKEQLNERRV----QVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAA 1176
Cdd:pfam15921 320 SDLESTVSQLRSELREAKRmyedKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1177 RAKAEKVRRDLSEELEALKNELLDsldttaaqqelRSKREQELATLKKSLEEETVNH-EGVLADMRHKHS--QELNSIND 1253
Cdd:pfam15921 400 NKRLWDRDTGNSITIDHLRRELDD-----------RNMEVQRLEALLKAMKSECQGQmERQMAAIQGKNEslEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1254 QLENlrkAKTVLEKAKGTLEAENADLATELRSVN---SSRQENDRRRKQAESQIAELQ----VKLAEIERARSElQEKCT 1326
Cdd:pfam15921 469 QLES---TKEMLRKVVEELTAKKMTLESSERTVSdltASLQEKERAIEATNAEITKLRsrvdLKLQELQHLKNE-GDHLR 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1327 KLQQEAENITNQLEEAElkasaavKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYE 1406
Cdd:pfam15921 545 NVQTECEALKLQMAEKD-------KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKD 617
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1407 RKLAEVTTQMQEIkkkaeeDADLAKELEEGKKRLnkdiealeRQVKELIAQNDRLDKSKKKIQSELEDATIELEA-QRTK 1485
Cdd:pfam15921 618 AKIRELEARVSDL------ELEKVKLVNAGSERL--------RAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVlKRNF 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1486 VLELEKKQKNFDKILAEEKAISEQIAQERDTAeREAREKETKVLSVSRELDEafdKIEDLENKRKTLQNELDDLANTQGT 1565
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQLKSAQSELEQTRNTL-KSMEGSDGHAMKVAMGMQK---QITAKRGQIDALQSKIQFLEEAMTN 759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1566 ADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRL-------EVNMQALRSQFE--RDLLAKEEgAEEKRRG 1636
Cdd:pfam15921 760 ANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLkekvanmEVALDKASLQFAecQDIIQRQE-QESVRLK 838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1637 L-----VKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEM--HNKVKEDALKhakklqaqvKDALRDaeeaka 1709
Cdd:pfam15921 839 LqhtldVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlsHHSRKTNALK---------EDPTRD------ 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1710 akeeLQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEiannankgSLMIDEKRRLEARIATLEEELE 1789
Cdd:pfam15921 904 ----LKQLLQELRSVINEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIES--------SLRSDICHSSSNSLQTEGSKSS 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1790 EEQSNSEVLLdrsRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNK----ELKAKLAE--IETAQRTKVKATIATLE 1863
Cdd:pfam15921 972 ETCSREPVLL---HAGELEDPSSCFTFPSTASPSVKNSASRSFHSSPKKspvhSLLTSSAEgsIGSSSQYRSAKTIHSPD 1048
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1864 AKIANLEEQLENEGkerllqqKANRKMDKKIKELTMNIEDerrhvdqhkeqMDKLNSRIKLLKRNldeTEEELQKEKTQK 1943
Cdd:pfam15921 1049 SVKDSQSLPIETTG-------KTCRKLQNRLESLQTLVED-----------LQLKNQAMSSMIRN---QEKRIQKVKDQE 1107
|
.
gi 62471805 1944 R 1944
Cdd:pfam15921 1108 K 1108
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1104-1845 |
2.06e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 69.48 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1104 ETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATA-------QKAQRELESQLAEIQEDLeaekaa 1176
Cdd:pfam12128 208 DDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAelrlshlHFGYKSDETLIASRQEER------ 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1177 rakaekvrrdlsEELEALKNELLDSLDttAAQQELRSKREQELATLKKSLEEEtvNHEGVLADMRHKHSQElnsinDQLE 1256
Cdd:pfam12128 282 ------------QETSAELNQLLRTLD--DQWKEKRDELNGELSAADAAVAKD--RSELEALEDQHGAFLD-----ADIE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1257 NLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAElqvKLAEIERARSELQEKCTKLQQEAENIT 1336
Cdd:pfam12128 341 TAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNR---DIAGIKDKLAKIREARDRQLAVAEDDL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1337 NQLEeAELKasaavksaSNMESQLTEAQQlleeetrQKLGLSSKLrqieSEKEALQEQLEEDDEAKRNYERKLAEVTTQM 1416
Cdd:pfam12128 418 QALE-SELR--------EQLEAGKLEFNE-------EEYRLKSRL----GELKLRLNQATATPELLLQLENFDERIERAR 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1417 QEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQndrldkskkkiQSELEDATIELEAQRTKVLELEKKQ--- 1493
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER-----------QSALDELELQLFPQAGTLLHFLRKEapd 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1494 --KNFDKILAEEKAISEQIAQERDTAereAREKETKVLSVSRELDEAfdKIEDLENKRKTLQNELDDLANTQGTADKNVH 1571
Cdd:pfam12128 547 weQSIGKVISPELLHRTDLDPEVWDG---SVGGELNLYGVKLDLKRI--DVPEWAASEEELRERLDKAEEALQSAREKQA 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1572 ELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETEL--- 1648
Cdd:pfam12128 622 AAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHqaw 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1649 -----DEERKQRTAAVASKKKLEGDLKeiettmemhnkVKEDALKHAKkLQAQVKDALRDAEEAKAAKEELQALSKEAER 1723
Cdd:pfam12128 702 leeqkEQKREARTEKQAYWQVVEGALD-----------AQLALLKAAI-AARRSGAKAELKALETWYKRDLASLGVDPDV 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1724 KVKaLEAEVLQLTEDLASSERARRAA-----------ETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQ 1792
Cdd:pfam12128 770 IAK-LKREIRTLERKIERIAVRRQEVlryfdwyqetwLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMER 848
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1793 SNSEVLLDRS----RKAQLQIEQLTTelANEKSNSQKNENGRALLERQNKELKAKLA 1845
Cdd:pfam12128 849 KASEKQQVRLsenlRGLRCEMSKLAT--LKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
|
| Myosin_N |
pfam02736 |
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the ... |
79-122 |
3.42e-11 |
|
Myosin N-terminal SH3-like domain; This domain has an SH3-like fold. It is found at the N-terminus of many but not all myosins. The function of this domain is unknown.
Pssm-ID: 460670 Cd Length: 45 Bit Score: 59.75 E-value: 3.42e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 62471805 79 KRLVWVPHENQGFVAASIKREHGDEVEVELaETGKRVMILRDDI 122
Cdd:pfam02736 3 KKLVWVPDPKEGFVKGEIKEEEGDKVTVET-EDGKTVTVKKDDV 45
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1075-1555 |
4.08e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1075 HEATISELEERLHKDQQQRQ-ESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEeltqtllrideesatkatAQ 1153
Cdd:COG4717 40 LAFIRAMLLERLEKEADELFkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE------------------LE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1154 KAQRELESQLAEIQEDLEAEKAARAKAEKVRRdlSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNH 1233
Cdd:COG4717 102 EELEELEAELEELREELEKLEKLLQLLPLYQE--LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1234 EGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSV-NSSRQENDRRRKQAESQIAELQVKLA 1312
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLeNELEAAALEERLKEARLLLLIAAALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1313 EIERARSELQEKCTKLqqeAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQ 1392
Cdd:COG4717 260 ALLGLGGSLLSLILTI---AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1393 EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSEL 1472
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1473 EDATIELEAQRTKVLELEKKQKNfdkilAEEKAISEQIAQERdtAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTL 1552
Cdd:COG4717 416 GELEELLEALDEEELEEELEELE-----EELEELEEELEELR--EELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
...
gi 62471805 1553 QNE 1555
Cdd:COG4717 489 AEE 491
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1691-1973 |
4.44e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 4.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1691 KKLQAQVKDALRdaeeakaakeeLQALSKEA-ERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANkgsl 1769
Cdd:COG1196 203 EPLERQAEKAER-----------YRELKEELkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA---- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1770 midEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIET 1849
Cdd:COG1196 268 ---ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1850 -------------AQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMD 1916
Cdd:COG1196 345 eleeaeeeleeaeAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1917 KLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1973
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1129-1897 |
5.51e-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: 68.07 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1129 AKREEELTQTLLRIDEESATK---------ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELl 1199
Cdd:TIGR00618 125 KSETEEVIHDLLKLDYKTFTRvvllpqgefAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRS- 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1200 dSLDTTAAQQelrskREQELATLKKSLEEETVNHEGVLADMRHKHSQElnsinDQLENLRKAKTVLEKAKGTLEAENADL 1279
Cdd:TIGR00618 204 -QLLTLCTPC-----MPDTYHERKQVLEKELKHLREALQQTQQSHAYL-----TQKREAQEEQLKKQQLLKQLRARIEEL 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1280 ATELRSVNSSRQENDRRRKQAesQIAELQVKLAEIERAR----SELQEKCTKLQQEAENITNQLE-----EAELKASAAV 1350
Cdd:TIGR00618 273 RAQEAVLEETQERINRARKAA--PLAAHIKAVTQIEQQAqrihTELQSKMRSRAKLLMKRAAHVKqqssiEEQRRLLQTL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1351 KSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLA 1430
Cdd:TIGR00618 351 HSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAK 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1431 KELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSEledatieleaqrtkvLELEKKQKNFDKILAEEKAISEQI 1510
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER---------------EQQLQTKEQIHLQETRKKAVVLAR 495
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1511 AQERDTAEREAREKEtkvlsvsRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEkakrALESQLAELKAQ 1590
Cdd:TIGR00618 496 LLELQEEPCPLCGSC-------IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT----SERKQRASLKEQ 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1591 NEELEDDLQLTEDAKLRLEVNMQALRSqferdllakeegaeekrrgLVKQLRDLETELDEERKQ-RTAAVASKKKLEGDL 1669
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRSKEDIPNLQN-------------------ITVRLQDLTEKLSEAEDMlACEQHALLRKLQPEQ 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1670 KEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEA-ERKVKALEAEVLQLT---EDLASSERA 1745
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASrQLALQKMQSEKEQLTywkEMLAQCQTL 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1746 RRAAETERDELAEEIANNANKGSLMIDE-------------KRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQieQL 1812
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDlaaredalnqslkELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS--HL 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1813 TTELANEKSNSQKNENGRALLERQNKE-----LKAKLAEIETAQ--RTKVKATIATLEAKIANLEEQLENEGkERLLQQK 1885
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQeipsdEDILNLQCETLVqeEEQFLSRLEEKSATLGEITHQLLKYE-ECSKQLA 862
|
810
....*....|..
gi 62471805 1886 ANRKMDKKIKEL 1897
Cdd:TIGR00618 863 QLTQEQAKIIQL 874
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1140-1912 |
7.24e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 7.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1140 LRIDEESATkaTAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKnELLDSLDTTAAQQELRSKREQEL 1219
Cdd:PRK04863 281 RRVHLEEAL--ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS-DHLNLVQTALRQQEKIERYQADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1220 ATLKKSLEEETV----NHEGVLADMRHKHS--QELNSINDQLENL--------------RKAKTVLEKAKGTLEAenADL 1279
Cdd:PRK04863 358 EELEERLEEQNEvveeADEQQEENEARAEAaeEEVDELKSQLADYqqaldvqqtraiqyQQAVQALERAKQLCGL--PDL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1280 ATElrsvnssrqendrrrkQAESQIAELQVKLAEIERARSELQEKCtklqQEAENITNQLEEA---------ELKASAAV 1350
Cdd:PRK04863 436 TAD----------------NAEDWLEEFQAKEQEATEELLSLEQKL----SVAQAAHSQFEQAyqlvrkiagEVSRSEAW 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1351 KSASNMESQLTEAQQLLE--EETRQKLG-LSSKLRQIESEKEALQE-----QLEEDDEAkrNYERKLAEVTTQMQEIKKK 1422
Cdd:PRK04863 496 DVARELLRRLREQRHLAEqlQQLRMRLSeLEQRLRQQQRAERLLAEfckrlGKNLDDED--ELEQLQEELEARLESLSES 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1423 AEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATiELEAQRTKVLELEKK-QKNFDKILA 1501
Cdd:PRK04863 574 VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQ-DVTEYMQQLLERERElTVERDELAA 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1502 EEKAISEQIA--QERDTAE--REAREKET--KVLsvsreLDEAFDKIE---------------------DLENKRKTLQN 1554
Cdd:PRK04863 653 RKQALDEEIErlSQPGGSEdpRLNALAERfgGVL-----LSEIYDDVSledapyfsalygparhaivvpDLSDAAEQLAG 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1555 E---LDDLANTQGTADK------NVHELEKA----------------------KRALESQLAELKAQNEELEddlqlTED 1603
Cdd:PRK04863 728 LedcPEDLYLIEGDPDSfddsvfSVEELEKAvvvkiadrqwrysrfpevplfgRAAREKRIEQLRAEREELA-----ERY 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1604 AKLRLEVN-MQALRSQFERDL-----LAKEEGAEEKRRGLVKQLRDLETEL----DEERKQRTAAVASKKKLEGdLKEIE 1673
Cdd:PRK04863 803 ATLSFDVQkLQRLHQAFSRFIgshlaVAFEADPEAELRQLNRRRVELERALadheSQEQQQRSQLEQAKEGLSA-LNRLL 881
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1674 TTMemhNKVKEDAL-KHAKKLQAQVKDALRDAEEAKAAKEELQALSKEA------ERKVKALEAEVLQLTEDLA------ 1740
Cdd:PRK04863 882 PRL---NLLADETLaDRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQRdakqqa 958
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1741 ---SSERARRAA---ETERDELAEEIANN-ANKGSLMIDEKRRLEARIATLEEELEEEQsNSEVL--LDRSRKAQlqiEQ 1811
Cdd:PRK04863 959 falTEVVQRRAHfsyEDAAEMLAKNSDLNeKLRQRLEQAEQERTRAREQLRQAQAQLAQ-YNQVLasLKSSYDAK---RQ 1034
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1812 LTTELANEKSN--SQKNENGRALLERQNKELKAKLaeieTAQRTKVKAtiatLEAKIANLEEQLENegkerllqqkanrk 1889
Cdd:PRK04863 1035 MLQELKQELQDlgVPADSGAEERARARRDELHARL----SANRSRRNQ----LEKQLTFCEAEMDN-------------- 1092
|
890 900
....*....|....*....|...
gi 62471805 1890 MDKKIKELTMNIEDERRHVDQHK 1912
Cdd:PRK04863 1093 LTKKLRKLERDYHEMREQVVNAK 1115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1517-1732 |
1.54e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1517 AEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELED 1596
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1597 DLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLV----------KQLRDLETELDEERKQRTAAVASKKKLE 1666
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylaparrEQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1667 GDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEV 1732
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1106-1349 |
1.58e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1106 EVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAArakaekvRR 1185
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1186 DLSEELEALKNELLDSLDttAAQQELRSKREQELATLKKSLEeetvnhegvLADMRHKHSQELNSINDQLENLRKAKTVL 1265
Cdd:COG4942 94 ELRAELEAQKEELAELLR--ALYRLGRQPPLALLLSPEDFLD---------AVRRLQYLKYLAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1266 EKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELK 1345
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....
gi 62471805 1346 ASAA 1349
Cdd:COG4942 243 TPAA 246
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1066-1778 |
1.80e-10 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 66.28 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1066 KHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIEtevadlKEQLNERRVQVdemqaqlaKREEELTQTLLRIDEE 1145
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQ------ELQFENEKVSL--------KLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1146 SATKATAQKaqreLESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALK---NELLDSLDTTAAQQELRSKREQE-LAT 1221
Cdd:pfam05483 151 NATRHLCNL----LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMIlafEELRVQAENARLEMHFKLKEDHEkIQH 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1222 LKKSLEEETVNHEGVLADMRHKHSQELNSINDQ---LENLRKAKTVLEKaKGTLEAENadlatelrsVNSSRQENDRRRK 1298
Cdd:pfam05483 227 LEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEE-KTKLQDEN---------LKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1299 QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLS 1378
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1379 SKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAD---LAKELEEGKKRLNKDIEALERQVKELI 1455
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekIAEELKGKEQELIFLLQAREKEIHDLE 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1456 AQNDRLDKSKKKIQSELEDATIELEAQRTKVLELekkQKNFDKILAEEKaiseQIAQERDTAEREAREKETKVLSVSREL 1535
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL---TAHCDKLLLENK----ELTQEASDMTLELKKHQEDIINCKKQE 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1536 DEAFDKIEDLENKRKTLQNELDDLANT-QGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQA 1614
Cdd:pfam05483 530 ERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKN 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1615 LRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELD-EERKQRTAAVASKKKLEGDLKEI--ETTMEMHNKVKEDAlKHAK 1691
Cdd:pfam05483 610 IEELHQENKALKKKGSAENKQLNAYEIKVNKLELElASAKQKFEEIIDNYQKEIEDKKIseEKLLEEVEKAKAIA-DEAV 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1692 KLQAQVKdaLRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMI 1771
Cdd:pfam05483 689 KLQKEID--KRCQHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
....*..
gi 62471805 1772 DEKRRLE 1778
Cdd:pfam05483 767 EEKEKLK 773
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1130-1972 |
2.06e-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: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1130 KREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQ 1209
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1210 ELRS------KREQELATLKKSLEEETVN----HEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADL 1279
Cdd:TIGR00606 266 KLDNeikalkSRKKQMEKDNSELELKMEKvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTEL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1280 ATEL--RSVNSSRQENDRRRKQAESQIAELQVKLAEIER-ARSELQEKctklqqeaENITNQLEEAELKASAAVKSASNM 1356
Cdd:TIGR00606 346 LVEQgrLQLQADRHQEHIRARDSLIQSLATRLELDGFERgPFSERQIK--------NFHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEAQQLLEEETRQKLGLSsklRQIESEKEALQEQLEEddeaKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1436
Cdd:TIGR00606 418 QSKERLKQEQADEIRDEKKGLG---RTIELKKEILEKKQEE----LKFVIKELQQLEGSSDRILELDQELRKAERELSKA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1437 KKrlNKDIEALERQVKELIAQNDRLDKSKKKIQSELEdatieleaqrtkvlelekkQKNFDKilaEEKAISEQIAQERDT 1516
Cdd:TIGR00606 491 EK--NSLTETLKKEVKSLQNEKADLDRKLRKLDQEME-------------------QLNHHT---TTRTQMEMLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1517 AEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELED 1596
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1597 dlqltedaKLRLEVNMQALRSQFERdllakeegaeekrrglvkqlrdLETELDEERKQRTAAVASKKKLEGDLKEIETTM 1676
Cdd:TIGR00606 627 --------KLFDVCGSQDEESDLER----------------------LKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1677 EMHNKVKEDALKHAKKLQAQVKDalrdaeeakaakeeLQALSKEAERKVKALEAEVLQLtedlasserarraaETERDEL 1756
Cdd:TIGR00606 677 QSCCPVCQRVFQTEAELQEFISD--------------LQSKLRLAPDKLKSTESELKKK--------------EKRRDEM 728
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1757 AEEIANNANKGSLMIDEKRRLEARIatleeeleeeqsnsevlldrsrkaqlqiEQLTTELANEKSNSQKNENgraLLERQ 1836
Cdd:TIGR00606 729 LGLAPGRQSIIDLKEKEIPELRNKL----------------------------QKVNRDIQRLKNDIEEQET---LLGTI 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1837 NKELK-AKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDK--KIKELTMNIEDERRHVDQHKE 1913
Cdd:TIGR00606 778 MPEEEsAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKqhELDTVVSKIELNRKLIQDQQE 857
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1914 QMDKLNSRIKllkrnldeteeELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLR 1972
Cdd:TIGR00606 858 QIQHLKSKTN-----------ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1587-1977 |
2.85e-10 |
|
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: 65.85 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1587 LKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERdlLAKEEGAEEKRRGLVKQLRDLE-----TELDEERKQRTAAVAS 1661
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDILNELERQLKS--LERQAEKAERYKELKAELRELElallvLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1662 KKKLEGDLKEIETTMemhnkvkedalkhaKKLQAQVkDALRDAEEAkaakeeLQALSKEAERKVKALEAEVLQLTEDLAS 1741
Cdd:TIGR02168 248 LKEAEEELEELTAEL--------------QELEEKL-EELRLEVSE------LEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1742 SERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATleeeleeeqsnsevlldrsrkAQLQIEQLTTELANEKS 1821
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE---------------------LKEELESLEAELEELEA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1822 NSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKanRKMDKKIKELTMNI 1901
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLE-LQIASLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAEL 442
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1902 EDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRE---CEDMIESQEAMNREINSLKTKLRRTGGI 1977
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARldsLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1053-1487 |
4.42e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1053 DLSQTLAEEEEKAKHLAKLKAKheatISELEERLHKDQQQRQESDRSKRKIET---------EVADLKEQLNERRVQVDE 1123
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEE----LEELEEELEELEAELEELREELEKLEKllqllplyqELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1124 MQAQLAKREEeltqtllrideesatkatAQKAQRELESQLAEIQEDLEAEKAARAKAEKVR-RDLSEELEALKNELLDSL 1202
Cdd:COG4717 151 LEERLEELRE------------------LEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1203 DTTAAQQELRSKREQELATLKKSLEEETVNHE-----------GVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGT 1271
Cdd:COG4717 213 EELEEAQEELEELEEELEQLENELEAAALEERlkearlllliaAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1272 LEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAvk 1351
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ-- 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1352 sasNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEvttqmQEIKKKAEEDADLAK 1431
Cdd:COG4717 371 ---EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE-----EELEEELEELEEELE 442
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1432 ELEEGKKRLNKDIEALERQVKELiAQNDRLDKSKKKIQSELEDATIELEAQRTKVL 1487
Cdd:COG4717 443 ELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1400-1664 |
5.12e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1400 EAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIEL 1479
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1480 EAQRtkvlelekkqknfdkilaeekaisEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1559
Cdd:COG4942 100 EAQK------------------------EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1560 ANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQferdllAKEEGAEEKRrgLVK 1639
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE------LAELQQEAEE--LEA 227
|
250 260
....*....|....*....|....*
gi 62471805 1640 QLRDLETELDEERKQRTAAVASKKK 1664
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALK 252
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1488-1940 |
7.01e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.02 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1488 ELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAntqgtAD 1567
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-----KL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1568 KNVHELEKAKRALESQLAELKAQNEELEDDLQL---TEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDL 1644
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1645 ETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEdaLKHAK----------KLQAQVKDALRDAEEAKAAKEEL 1714
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER--LKEARlllliaaallALLGLGGSLLSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1715 QALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEI-ANNANKGSLMIDEKRRLEARIATLEEELEEEQS 1793
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1794 NSEVLLDRSRKAQLQIEQLTTE-----LANEKSNSQKNENGRALLERQ-NKELKAKLAEIETAQRTKVKATIATLEAKIA 1867
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEeelraALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1868 NLEEQLENEGKERLLQQKANRKMDKkiKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEK 1940
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEE--DGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1542-1973 |
7.39e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1542 IEDLENKRKTLQNELDdlANTQGTADKNVHElekAKRALESQLAELKAQNEELEDD----LQLTEDAKLRLEVNMQALRS 1617
Cdd:PRK02224 178 VERVLSDQRGSLDQLK--AQIEEKEEKDLHE---RLNGLESELAELDEEIERYEEQreqaRETRDEADEVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1618 QFE-----RDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKK 1692
Cdd:PRK02224 253 LETleaeiEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1693 LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEvlqltedLASSERARRAAETERDELAEEIannankgslmid 1772
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE-------LEEAREAVEDRREEIEELEEEI------------ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1773 ekRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNEngrALLERQN-KELKAKLAEIETAQ 1851
Cdd:PRK02224 394 --EELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE---ALLEAGKcPECGQPVEGSPHVE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1852 RTKVK-ATIATLEAKIANLEEQLEnEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLD 1930
Cdd:PRK02224 469 TIEEDrERVEELEAELEDLEEEVE-EVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 62471805 1931 ETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1973
Cdd:PRK02224 548 ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIES 590
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1299-1525 |
7.74e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 63.31 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1299 QAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEeTRQKLGLS 1378
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE-RREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1379 SKLRQIESEKEALQEQLEEDDEakrnyerkLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQN 1458
Cdd:COG3883 92 ARALYRSGGSVSYLDVLLGSES--------FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1459 DRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKE 1525
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1303-1479 |
8.23e-10 |
|
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: 61.09 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1303 QIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLeEETRQKLGLSSKLR 1382
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1383 QIesekEALQEQLEEDDEAKRNYERKLAEVttqMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD 1462
Cdd:COG1579 90 EY----EALQKEIESLKRRISDLEDEILEL---MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|....*..
gi 62471805 1463 KSKKKIQSELEDATIEL 1479
Cdd:COG1579 163 AEREELAAKIPPELLAL 179
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1090-1347 |
1.10e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1090 QQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQED 1169
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1170 LEAEkaarakaekvRRDLSEELEAL-KNELLDSLDTTAAQQELrskreqelatlkksleEETVNHEGVLADMRHKHSQEL 1248
Cdd:COG4942 99 LEAQ----------KEELAELLRALyRLGRQPPLALLLSPEDF----------------LDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1249 NSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKL 1328
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
250
....*....|....*....
gi 62471805 1329 QQEAENITNQLEEAELKAS 1347
Cdd:COG4942 233 EAEAAAAAERTPAAGFAAL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1358-1568 |
1.18e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.47 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1358 SQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQM----QEIKKKAEEDADLAKEL 1433
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaaleAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1434 EEGKKRLNKDIEALERQ-----VKELIAQND--RLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAI 1506
Cdd:COG4942 100 EAQKEELAELLRALYRLgrqppLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1507 SEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADK 1568
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1271-1513 |
1.19e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 63.50 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1271 TLEAENADLATEL----------RSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKctklqqeaenitNQLE 1340
Cdd:COG3206 141 SYTSPDPELAAAVanalaeayleQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLV 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1341 EAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQE--QLEEDDEAKRNYERKLAEVTT---- 1414
Cdd:COG3206 209 DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSArytp 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1415 ---QMQEIKKK-AEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLdKSKKKIQSELEDATIELEAqrtkvlELE 1490
Cdd:COG3206 289 nhpDVIALRAQiAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQL-EARLAELPELEAELRRLER------EVE 361
|
250 260
....*....|....*....|...
gi 62471805 1491 KKQKNFDKILAEEKAISEQIAQE 1513
Cdd:COG3206 362 VARELYESLLQRLEEARLAEALT 384
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1062-1414 |
1.20e-09 |
|
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: 62.99 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1062 EEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLR 1141
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1142 IDEESATKATAQKAQRELE-------SQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLdsldttAAQQELRSk 1214
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEediktltQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ------QTEEELRS- 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1215 REQELATLKKSLEE---------ETVNHEGVLADMRHKHSQELNSIndqLENLRKAKTVLEKAKGTLEAenadLATELRS 1285
Cdd:pfam07888 190 LSKEFQELRNSLAQrdtqvlqlqDTITTLTQKLTTAHRKEAENEAL---LEELRSLQERLNASERKVEG----LGEELSS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1286 VNSSRQENDRRRKQAESQIAELQVKLAEIERA----RSELQEKCTKLQQEAENITNQLEE--AELKASAAVKSASNMESQ 1359
Cdd:pfam07888 263 MAAQRDRTQAELHQARLQAAQLTLQLADASLAlregRARWAQERETLQQSAEADKDRIEKlsAELQRLEERLQEERMERE 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1360 LTEAQ---------QLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTT 1414
Cdd:pfam07888 343 KLEVElgrekdcnrVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
928-1651 |
1.29e-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: 63.70 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 928 ALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIeeeeerVLALGGEKKKLELNIQDLEEQLEEEEA 1007
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEK------RDELNGELSAADAAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1008 ---ARQKLQLEKVQLDA--------KIKKYEEDL-ALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKH 1075
Cdd:pfam12128 330 qhgAFLDADIETAAADQeqlpswqsELENLEERLkALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1076 EATISELEERLhkDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA------QLAKREEELTQTLLRIDEESATK 1149
Cdd:pfam12128 410 LAVAEDDLQAL--ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATAtpelllQLENFDERIERAREEQEAANAEV 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1150 ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKR----EQELAT-LKK 1224
Cdd:pfam12128 488 ERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKvispELLHRTdLDP 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1225 SLEEETVNHEGVLADMR-HKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNssrqendrrrKQAESQ 1303
Cdd:pfam12128 568 EVWDGSVGGELNLYGVKlDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQAN----------GELEKA 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1304 IAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKL-------- 1375
Cdd:pfam12128 638 SREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKreartekq 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1376 --------GLSSKLRQIESEKEALQEQLE-EDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEA 1446
Cdd:pfam12128 718 aywqvvegALDAQLALLKAAIAARRSGAKaELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRY 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1447 LERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQ----RTKVLELEKKQKNFDKILAEekaISEQIAQERDTAEREAR 1522
Cdd:pfam12128 798 FDWYQETWLQRRPRLATQLSNIERAISELQQQLARLiadtKLRRAKLEMERKASEKQQVR---LSENLRGLRCEMSKLAT 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1523 EKE-TKVLSVSRELDEAFDKIEDLENKRKTL----QNELDDLANTqgTADKNVHELEKAKRALESQLAELKAQNEELEDD 1597
Cdd:pfam12128 875 LKEdANSEQAQGSIGERLAQLEDLKLKRDYLsesvKKYVEHFKNV--IADHSGSGLAETWESLREEDHYQNDKGIRLLDY 952
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1598 LQ----LTEDAKLRLEVNMQALRSQ---FERDLLAKEEGAEEKRRGLVKQLRDLETELDEE 1651
Cdd:pfam12128 953 RKlvpyLEQWFDVRVPQSIMVLREQvsiLGVDLTEFYDVLADFDRRIASFSRELQREVGEE 1013
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1195-1553 |
2.47e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 62.45 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1195 KNELLDSLDTTAAQQELRSKREQELATLKksLEEETVNHEgvladmRHKHSQELNSiNDQLENLRKAKTVLEKAKGTLEA 1274
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEK--MEQERLRQE------KEEKAREVER-RRKLEEAEKARQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1275 ENADLATEL-RSVNSSRQENDRRRKQA--ESQIAELQVKLAEIERARSELQEKCTKLQQE---AENITNQLEEAELKASA 1348
Cdd:pfam17380 338 EQERMAMEReRELERIRQEERKRELERirQEEIAMEISRMRELERLQMERQQKNERVRQEleaARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1349 AVKSASNMESQLTEAQQL----LEEETRQKLglsSKLRQIESEKEALQEQLEEDDEAKRnyeRKLAEvttqmqeiKKKAE 1424
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQRevrrLEEERAREM---ERVRLEEQERQQQVERLRQQEEERK---RKKLE--------LEKEK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1425 EDADLAKelEEGKKRLNKDIEALERQVKEliaqndrlDKSKKKI-QSELED--ATIELEAQRTKVLELEKKQKNFDkila 1501
Cdd:pfam17380 484 RDRKRAE--EQRRKILEKELEERKQAMIE--------EERKRKLlEKEMEErqKAIYEEERRREAEEERRKQQEME---- 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1502 EEKAISEQIaqerdtaeREAREKETKVLSVSRElDEAFDKIEDLENKRKTLQ 1553
Cdd:pfam17380 550 ERRRIQEQM--------RKATEERSRLEAMERE-REMMRQIVESEKARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1146-1354 |
2.79e-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: 61.32 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1146 SATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKS 1225
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1226 ---LEEETVNHEGVLADM--------RHKHSQELNSINDQLENLRKAK-------------TVLEKAKGTLEAENADLAT 1281
Cdd:COG4942 92 iaeLRAELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQylkylaparreqaEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1282 ELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSAS 1354
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1246-1731 |
3.53e-09 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 62.07 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1246 QELNSINDQLEN-LRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKL-AEIERARSELQE 1323
Cdd:pfam05557 5 IESKARLSQLQNeKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1324 KCTKLQQEAENITNQLEEAELKasaavksaSNMESQLTEAQQLLEeetRQKLGLSSKlrqiESEKEALQEQLEEDDEAKR 1403
Cdd:pfam05557 85 LEALNKKLNEKESQLADAREVI--------SCLKNELSELRRQIQ---RAELELQST----NSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1404 NYERKLAEVTTQMQEIKKKAEEDADLAKELE--EGKKRLNKDIEA-------LERQVKELIAQNDRLDKSK--------- 1465
Cdd:pfam05557 150 EAEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqEQDSEIVKNSKSelaripeLEKELERLREHNKHLNENIenklllkee 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1466 -----------KKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQ----------ERDTAEREAREK 1524
Cdd:pfam05557 230 vedlkrklereEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQlqqreivlkeENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1525 ETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL---------------------------ANTQGTADKNVHELEKAK 1577
Cdd:pfam05557 310 EKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLqrrvllltkerdgyrailesydkeltmSNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1578 RALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQferDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRta 1657
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQ---ESLADPSYSKEEVDSLRRKLETLELERQRLREQK-- 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1658 avaskkklegdlKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAE 1731
Cdd:pfam05557 465 ------------NELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRLLKKLEDD 526
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
857-1598 |
6.49e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 857 NAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVE-KTTL 935
Cdd:TIGR00618 145 RVVLLPQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHErKQVL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 936 AEQLQAEIELCAEAEESRSRLmARKQELEDMMQELETRIEEEEERVLALGGEKKKLE-----LNIQDLEEQLEEEEAARQ 1010
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEetqerINRARKAAPLAAHIKAVT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1011 KLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQ 1090
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1091 QQRQesdrskrkIETevadLKEQLNERRVQVDEMQAQLAKRE-EELTQTLLRIDEESAtKATAQKAQRELESQLAEIQED 1169
Cdd:TIGR00618 384 LQQQ--------KTT----LTQKLQSLCKELDILQREQATIDtRTSAFRDLQGQLAHA-KKQQELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1170 LEAEKAARAKAEKVRRDLSEELEALKNeLLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADM--------- 1240
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQT-KEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdnpgpltrr 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1241 -------RHKHSQELNSINDQLENLRKAKTVLeKAKGTLEAENADLATELRsvNSSRQENDRRRKQAESQIAELQVKLAE 1313
Cdd:TIGR00618 530 mqrgeqtYAQLETSEEDVYHQLTSERKQRASL-KEQMQEIQQSFSILTQCD--NRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1314 IERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTeaqqLLEEETRQKLGLSSKLRQIESEKEALQE 1393
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLT----LTQERVREHALSIRVLPKELLASRQLAL 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1394 QLEEDDEAKRNYERK-LAEVTTQMQEIKKKAEEDADLAKELEEG----KKRLNKDIEALERQVKELIAQNDRLDKSKKKI 1468
Cdd:TIGR00618 683 QKMQSEKEQLTYWKEmLAQCQTLLRELETHIEEYDREFNEIENAssslGSDLAAREDALNQSLKELMHQARTVLKARTEA 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1469 QSELEDATIELEAQRTKVLELEKKQKNFDKILAEE----KAISEQIAQERDTAEREareketkvLSVSRELdeafdkied 1544
Cdd:TIGR00618 763 HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDthllKTLEAEIGQEIPSDEDI--------LNLQCET--------- 825
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1545 LENKRKTLQNELDDLANTQGTADKNVHELEKAKRALEsQLAELKAQNEELEDDL 1598
Cdd:TIGR00618 826 LVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLA-QLTQEQAKIIQLSDKL 878
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1367-1968 |
7.05e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 60.89 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1367 LEEETRQKLG-LSSKLRQIESEKEALQEQLEEDDEAkrnyERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIE 1445
Cdd:pfam05483 97 IEAELKQKENkLQENRKIIEAQRKAIQELQFENEKV----SLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1446 ALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRtkvLELEKKQK-NFDKILAEEKAISEQIAQERDTAER---EA 1521
Cdd:pfam05483 173 KYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENAR---LEMHFKLKeDHEKIQHLEEEYKKEINDKEKQVSLlliQI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1522 REKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQgtaDKNVHELEKAKRALESQLAELKAqneeLEDDLQLT 1601
Cdd:pfam05483 250 TEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKK---DHLTKELEDIKMSLQRSMSTQKA----LEEDLQIA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1602 EDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNK 1681
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1682 vKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEV----LQLTEDLASSERARRAAETERDELA 1757
Cdd:pfam05483 403 -KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIhdleIQLTAIKTSEEHYLKEVEDLKTELE 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1758 EEIANN----ANKGSLMIDEKRRLEAriatLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALL 1833
Cdd:pfam05483 482 KEKLKNieltAHCDKLLLENKELTQE----ASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEF 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1834 ERQNKELKAKLAEIETAQRT------KVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKEltmniedERRH 1907
Cdd:pfam05483 558 IQKGDEVKCKLDKSEENARSieyevlKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSA-------ENKQ 630
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1908 VDQHKEQMDKLNSRIKLLKRNLDETEEelqkektqkrKYQRECEDMIESQEAMNREINSLK 1968
Cdd:pfam05483 631 LNAYEIKVNKLELELASAKQKFEEIID----------NYQKEIEDKKISEEKLLEEVEKAK 681
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
812-1441 |
8.26e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 812 FFRAGVLahleEERDF--KISDLIVNFQAFCRgflARRNYQKRLQQLNAIRIIQRNCAAYLKLRN-----------WQWW 878
Cdd:COG4913 212 FVREYML----EEPDTfeAADALVEHFDDLER---AHEALEDAREQIELLEPIRELAERYAAARErlaeleylraaLRLW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 879 RLYTKVKpLL--EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQA-LVEKTTLAEQLQAEIELCAEAEESRSR 955
Cdd:COG4913 285 FAQRRLE-LLeaELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRAR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 956 LMAR----KQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLA 1031
Cdd:COG4913 364 LEALlaalGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1032 LTDDQNQKLLKEKKLLEERANDLSQTLAEEE------EKA------------KHLAK-------LKAKHEATISELEERL 1086
Cdd:COG4913 444 ALRDALAEALGLDEAELPFVGELIEVRPEEErwrgaiERVlggfaltllvppEHYAAalrwvnrLHLRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1087 HKDQQQRQESDRSKRKIETEVAD----LKEQLNER--RVQVDEmQAQLAKREEELTQTLL--------------RIDEES 1146
Cdd:COG4913 524 PDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRRfdYVCVDS-PEELRRHPRAITRAGQvkgngtrhekddrrRIRSRY 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1147 ATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEA---LKNELLDSLDTTAAQQELRSKrEQELATLK 1223
Cdd:COG4913 603 VLGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrLAEYSWDEIDVASAEREIAEL-EAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1224 KSleeetvnhegvladmrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQ 1303
Cdd:COG4913 682 AS-------------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1304 IAELQVKLAEiERARSELQEKctKLQQEAENITNQLEEAELKASAAvksASNMESQLTEAQQLLEEETRqklGLSSKLRQ 1383
Cdd:COG4913 743 ARLELRALLE-ERFAAALGDA--VERELRENLEERIDALRARLNRA---EEELERAMRAFNREWPAETA---DLDADLES 813
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1384 IEsEKEALQEQLEEDDEAKrnYERKLAEVTTQmQEIKKKAEEDADLAKELEEGKKRLN 1441
Cdd:COG4913 814 LP-EYLALLDRLEEDGLPE--YEERFKELLNE-NSIEFVADLLSKLRRAIREIKERID 867
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1478-1949 |
1.26e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.17 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1478 ELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQerdtAEREAREKETKVLSVSRELDeafdkIEDLENKRKTLQNELD 1557
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEE----LEAELEELREELEKLEKLLQ-----LLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1558 DlantqgtadknvhelekakraLESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEkrrgL 1637
Cdd:COG4717 143 E---------------------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD----L 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1638 VKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEdalkhakklqaqvKDALRDAEEAKAAKEELQAL 1717
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER-------------LKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1718 SKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLmidEKRRLEARIATLEEELEEEQSNSEV 1797
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL---EEEELEELLAALGLPPDLSPEELLE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1798 LLDRSRKAQLQIEQLtTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKatiatLEAKIANLEEQLENEG 1877
Cdd:COG4717 342 LLDRIEELQELLREA-EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE-----LKEELEELEEQLEELL 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1878 KERLLQQKANRK--MDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRN--LDETEEELQKEKTQKRKYQRE 1949
Cdd:COG4717 416 GELEELLEALDEeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDgeLAELLQELEELKAELRELAEE 491
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1279-1881 |
1.46e-08 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 60.48 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1279 LATELRSVNSSRQeNDRRRKQAESQIAELQVKLaEIERARSELQEKCTKLqqEAENITNQLEEA---------ELKASAA 1349
Cdd:COG5022 795 LFIKLQPLLSLLG-SRKEYRSYLACIIKLQKTI-KREKKLRETEEVEFSL--KAEVLIQKFGRSlkakkrfslLKKETIY 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1350 VKSASNMESQLTEAQQLLEE-ETRQKLGLSS------------------------KLRQIESEKEALQE-QLEEDDEAKR 1403
Cdd:COG5022 871 LQSAQRVELAERQLQELKIDvKSISSLKLVNleleseiielkkslssdlienlefKTELIARLKKLLNNiDLEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1404 NYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELiaqndrldKSKKKIQSELEDATIELEAQR 1483
Cdd:COG5022 951 VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKEL--------AELSKQYGALQESTKQLKELP 1022
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1484 TKVLELEKKQKNFDKILAEEKAISEQIAQERD-TAEREAREKETKVLSVSRELDEAFDK----IEDLENKRKTLQNELDD 1558
Cdd:COG5022 1023 VEVAELQSASKIISSESTELSILKPLQKLKGLlLLENNQLQARYKALKLRRENSLLDDKqlyqLESTENLLKTINVKDLE 1102
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1559 LANTQGTADKNVhelEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFerDLLAKEEGAEEKRRGLV 1638
Cdd:COG5022 1103 VTNRNLVKPANV---LQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLF--WEANLEALPSPPPFAAL 1177
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1639 KQLRDLETELDEERKqrTAAVASKKKLEGDLKEIETtmemhnKVKEDALKhakklQAQVKDALRDAEEAKAAKEELQALS 1718
Cdd:COG5022 1178 SEKRLYQSALYDEKS--KLSSSEVNDLKNELIALFS------KIFSGWPR-----GDKLKKLISEGWVPTEYSTSLKGFN 1244
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1719 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIAN-----NANKGSLMIDEKRRLEARIATLEEELEEEQS 1793
Cdd:COG5022 1245 NLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSllqyiNVGLFNALRTKASSLRWKSATEVNYNSEELD 1324
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1794 NSEVLLDRSRkAQLQIEQL-----TTELANEKSNSQKNENG--RAL--LERQNKELKAKLAEIETAQRTKVKATIatlEA 1864
Cdd:COG5022 1325 DWCREFEISD-VDEELEELiqavkVLQLLKDDLNKLDELLDacYSLnpAEIQNLKSRYDPADKENNLPKEILKKI---EA 1400
|
650
....*....|....*..
gi 62471805 1865 KIANLEEQLENEGKERL 1881
Cdd:COG5022 1401 LLIKQELQLSLEGKDET 1417
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1109-1672 |
1.95e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 59.53 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1109 DLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaekaarakaekvrrdLS 1188
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS------------------LE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1189 EELEALKNELldsldttaAQQELRSKREQELATLKKSLEEEtvnHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKA 1268
Cdd:PRK01156 249 DMKNRYESEI--------KTAESDLSMELEKNNYYKELEER---HMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNI 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1269 KGTLEA--ENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKA 1346
Cdd:PRK01156 318 DAEINKyhAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1347 SAAVKSASNMESQLTEAQQLLEEetrqklgLSSKLRQIESEKEALQEQLeedDEAKRNYERKLAEVTTQMQEIKKKAEED 1426
Cdd:PRK01156 398 KIQEIDPDAIKKELNEINVKLQD-------ISSKVSSLNQRIRALRENL---DELSRNMEMLNGQSVCPVCGTTLGEEKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1427 ADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSE-----------LEDATIELEAQRTKVLELEKKQKN 1495
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEeinksineynkIESARADLEDIKIKINELKDKHDK 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1496 FDKILAEEKAISEQIAQER----------------DTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1559
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKrtswlnalavislidiETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1560 ANTQGTADKNVHELEKAKRALESQLAELK---AQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEgaeekRRG 1636
Cdd:PRK01156 628 ANNLNNKYNEIQENKILIEKLRGKIDNYKkqiAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRAR-----LES 702
|
570 580 590
....*....|....*....|....*....|....*....
gi 62471805 1637 LVKQLRDLETELDEERKQRTAAVASKKKLE---GDLKEI 1672
Cdd:PRK01156 703 TIEILRTRINELSDRINDINETLESMKKIKkaiGDLKRL 741
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1255-1952 |
1.98e-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: 59.85 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1255 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVkLAEIERARSELqekcTKLQQEaen 1334
Cdd:pfam12128 178 LRHIDKIAKAMHSKEGKFRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQA-IAGIMKIRPEF----TKLQQE--- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1335 iTNQLEEAELKASA---AVKSASNMESQLTEAQQLLEEETRQKLglSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAE 1411
Cdd:pfam12128 250 -FNTLESAELRLSHlhfGYKSDETLIASRQEERQETSAELNQLL--RTLDDQWKEKRDELNGELSAADAAVAKDRSELEA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1412 VTTQ----MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLD-KSKKKIQSELEDATIELEAQR-TK 1485
Cdd:pfam12128 327 LEDQhgafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRsKIKEQNNRDIAGIKDKLAKIReAR 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1486 VLELEKKQKNFDKIlaeEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTlQNELDDLANTQGT 1565
Cdd:pfam12128 407 DRQLAVAEDDLQAL---ESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENF-DERIERAREEQEA 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1566 ADKNVHELEKAKRALESQLAElkaQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDL--LAKEEGAEEKRRGLV---KQ 1640
Cdd:pfam12128 483 ANAEVERLQSELRQARKRRDQ---ASEALRQASRRLEERQSALDELELQLFPQAGTLLhfLRKEAPDWEQSIGKVispEL 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1641 L--RDLETELDEERKQRTAAVASkkkLEGDLKEIE--TTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQA 1716
Cdd:pfam12128 560 LhrTDLDPEVWDGSVGGELNLYG---VKLDLKRIDvpEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1717 LSKEAERKVKAL--------------EAEVLQLTEdlaSSERARRAAETERDELAEEIANNANKGSLMIDEKRR--LEAR 1780
Cdd:pfam12128 637 ASREETFARTALknarldlrrlfdekQSEKDKKNK---ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqkREAR 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1781 IAtleeeleEEQSNSEVLLDRSrkaqLQIEQLTTELANEKSNsqknengrallerqnkeLKAKLAEIETAQRTKVKA--- 1857
Cdd:pfam12128 714 TE-------KQAYWQVVEGALD----AQLALLKAAIAARRSG-----------------AKAELKALETWYKRDLASlgv 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1858 ---TIATLEAKIANLEEQLENEGK-------------ERLLQQKANRKMDK-KIKELTMNIEDE-RRHVDQHKEQMDKLN 1919
Cdd:pfam12128 766 dpdVIAKLKREIRTLERKIERIAVrrqevlryfdwyqETWLQRRPRLATQLsNIERAISELQQQlARLIADTKLRRAKLE 845
|
730 740 750
....*....|....*....|....*....|...
gi 62471805 1920 SRIKLLKRNLDETEEELQKEKTQKRKYQRECED 1952
Cdd:pfam12128 846 MERKASEKQQVRLSENLRGLRCEMSKLATLKED 878
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1322-1675 |
2.03e-08 |
|
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: 59.20 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1322 QEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEA--------QQLLEEETRQKLGLSSKLRQIESEKEALQ- 1392
Cdd:COG5185 158 TGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEpsgtvnsiKESETGNLGSESTLLEKAKEIINIEEALKg 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1393 -EQLEEDDEAKRNYERKLAEVTTQMQEIK-KKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQND---RLDKSKKK 1467
Cdd:COG5185 238 fQDPESELEDLAQTSDKLEKLVEQNTDLRlEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkATESLEEQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1468 IQSELEDATIE--LEAQRTKVLEL-EKKQKNFDKILAEEKAISEQIaqERDTAEREAREKETKVLSVSRELDEAFDKI-E 1543
Cdd:COG5185 318 LAAAEAEQELEesKRETETGIQNLtAEIEQGQESLTENLEAIKEEI--ENIVGEVELSKSSEELDSFKDTIESTKESLdE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1544 DLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTE-DAKLRLEVNMQALRSQFERD 1622
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMrEADEESQSRLEEAYDEINRS 475
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1623 LLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETT 1675
Cdd:COG5185 476 VRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKD 528
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1208-1575 |
2.81e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 59.07 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1208 QQELRSKREQeLATLK---KSLEEETVNHEGVLADMRHKHSQELNSIndqlENLRKAKTVLEKAKgtleaenadlateLR 1284
Cdd:pfam10174 407 QEQLRDKDKQ-LAGLKervKSLQTDSSNTDTALTTLEEALSEKERII----ERLKEQREREDRER-------------LE 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1285 SVNSSRQENdrrrKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQ 1364
Cdd:pfam10174 469 ELESLKKEN----KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1365 QlLEEETRQKLGLSSKLRQIE--------------SEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLA 1430
Cdd:pfam10174 545 N-AEEAVRTNPEINDRIRLLEqevarykeesgkaqAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1431 KELEEGKKRlnKDIEALERQVKEliaQNDRLDKSKkkiQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQI 1510
Cdd:pfam10174 624 KHGQQEMKK--KGAQLLEEARRR---EDNLADNSQ---QLQLEELMGALEKTRQELDATKARLSSTQQSLAEKDGHLTNL 695
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1511 AQERDTAEREARE-KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQgtaDKNVHELEK 1575
Cdd:pfam10174 696 RAERRKQLEEILEmKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKREK---DRLVHQLKQ 758
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1203-1644 |
2.82e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1203 DTTAAQQELRSKRE-----QELATLKKSLEEETVNHegVLAD-MRHkhSQELNSINDQLENLRKAktvLEKAKGTLEAEN 1276
Cdd:PRK04863 234 DMEAALRENRMTLEairvtQSDRDLFKHLITESTNY--VAADyMRH--ANERRVHLEEALELRRE---LYTSRRQLAAEQ 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1277 ADL---ATELRSVNSSRQENDRRRKQAESQIAELQVKLA---EIERARSELQEKCTKL--QQEA-ENITNQLEEAELKAS 1347
Cdd:PRK04863 307 YRLvemARELAELNEAESDLEQDYQAASDHLNLVQTALRqqeKIERYQADLEELEERLeeQNEVvEEADEQQEENEARAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1348 AAVKSASNMESQLTEAQQLLE----------------EETRQKLGLSS-KLRQIESEKEALQEQLEEDDEAKRNYERKLA 1410
Cdd:PRK04863 387 AAEEEVDELKSQLADYQQALDvqqtraiqyqqavqalERAKQLCGLPDlTADNAEDWLEEFQAKEQEATEELLSLEQKLS 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1411 EVttqmQEIKKKAEEDADLAKeleegkkRLNKDIEALE--RQVKELIAQNdrldkSKKKIQSEledatiELEAQRTKVLE 1488
Cdd:PRK04863 467 VA----QAAHSQFEQAYQLVR-------KIAGEVSRSEawDVARELLRRL-----REQRHLAE------QLQQLRMRLSE 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1489 LEK---KQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLAntqgt 1565
Cdd:PRK04863 525 LEQrlrQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLA----- 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1566 adknvhELEKAKRALESQLAELKAQ-NEELEDDLQLTEdaklrlevNMQALRSQfERDLLAKEEGAEEKRRGLVKQLRDL 1644
Cdd:PRK04863 600 ------ARAPAWLAAQDALARLREQsGEEFEDSQDVTE--------YMQQLLER-ERELTVERDELAARKQALDEEIERL 664
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1407-1818 |
3.34e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.63 E-value: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1407 RKLAEVTTQMQEIKKKAEEDADLAKELEEgkkrLNKDIEALERQVKELIAQNDRLDKSKK--KIQSELEDATIELEAQRT 1484
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE----LEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1485 KVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQG 1564
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS---LATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1565 TADKNVHELEKAKR--ALESQLAELKAqneeleddLQLTEDAKLRLEVNMQALRSQFER----------------DLLAK 1626
Cdd:COG4717 224 ELEEELEQLENELEaaALEERLKEARL--------LLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallfLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1627 EEGAEEKRRGLVKQLRDLEtELDEERKQRTAAV------ASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDA 1700
Cdd:COG4717 296 EKASLGKEAEELQALPALE-ELEEEELEELLAAlglppdLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1701 LRDAEEAKAAKEELQALskEAERKVKALEAEVLQLTEDLAS--SERARRAAETERDELAEEIANNANKGSLMIDEKRRLE 1778
Cdd:COG4717 375 LLAEAGVEDEEELRAAL--EQAEEYQELKEELEELEEQLEEllGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 62471805 1779 ARIATLEEELEEEQSNSEVlldrsRKAQLQIEQLTTELAN 1818
Cdd:COG4717 453 EELAELEAELEQLEEDGEL-----AELLQELEELKAELRE 487
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1184-1462 |
3.36e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 59.15 E-value: 3.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1184 RRDLSEELEALKNELLDSLDTTAAQQelrsKREQELATLKKSLEEETvnhegvladmrhkhsQELNSINDQLENLRKAKT 1263
Cdd:PRK11281 51 QKLLEAEDKLVQQDLEQTLALLDKID----RQKEETEQLKQQLAQAP---------------AKLRQAQAELEALKDDND 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1264 vlEKAKGTLEA-ENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLaeiERARSELQEKCTKLQQeaenITNQLeeA 1342
Cdd:PRK11281 112 --EETRETLSTlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQP---ERAQAALYANSQRLQQ----IRNLL--K 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1343 ELKASAAVKSAS-----NMESQLTEAQ-----QLLEEETR-QKLG------LSSKLRQIESEKEALQEQLEEddeaKRny 1405
Cdd:PRK11281 181 GGKVGGKALRPSqrvllQAEQALLNAQndlqrKSLEGNTQlQDLLqkqrdyLTARIQRLEHQLQLLQEAINS----KR-- 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1406 eRKLAEVT-TQMQEIKKKAEEDAD--LAKELEegkkrLNKDIEalerqvKELIAQNDRLD 1462
Cdd:PRK11281 255 -LTLSEKTvQEAQSQDEAARIQANplVAQELE-----INLQLS------QRLLKATEKLN 302
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1096-1359 |
4.13e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1096 SDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEesatkatAQKAQRELESQLAEIQEDLEAEka 1175
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEA-------LQAEIDKLQAEIAEAEAEIEER-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1176 arakaekvRRDLSEELEALKNE--LLDSLDTTAAQQELrskreqelatlkksleEETVNHEGVLADMRHKHSQELNSIND 1253
Cdd:COG3883 85 --------REELGERARALYRSggSVSYLDVLLGSESF----------------SDFLDRLSALSKIADADADLLEELKA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1254 QLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAE 1333
Cdd:COG3883 141 DKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAA 220
|
250 260
....*....|....*....|....*.
gi 62471805 1334 NITNQLEEAELKASAAVKSASNMESQ 1359
Cdd:COG3883 221 AAAAAAAAAAAAAAAAAAAAAAAASA 246
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1390-1599 |
4.19e-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: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1390 ALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQ 1469
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1470 SELEDATIELEAQ--------RTKVLELEKKQKNFDKILAEEKAIsEQIAQERDTAEREAREKETKVLSVSRELDEAFDK 1541
Cdd:COG4942 97 AELEAQKEELAELlralyrlgRQPPLALLLSPEDFLDAVRRLQYL-KYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1542 IEDLENKRKTLQNELDDLANTQgtaDKNVHELEKAKRALESQLAELKAQNEELEDDLQ 1599
Cdd:COG4942 176 LEALLAELEEERAALEALKAER---QKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1050-1290 |
5.21e-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: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1050 RANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLA 1129
Cdd:COG4942 35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1130 KREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLeaekaarakaekvrRDLSEELEALKNELldsldttAAQQ 1209
Cdd:COG4942 115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL--------------RADLAELAALRAEL-------EAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1210 ELRSKREQELATLKKSLEEETVNHEGVLAdmrhKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSS 1289
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLA----RLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
.
gi 62471805 1290 R 1290
Cdd:COG4942 250 A 250
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
885-1541 |
5.87e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 57.99 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 885 KPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLqaeielcAEAEESRSRLMARKQELE 964
Cdd:PRK01156 152 KKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQI-------ADDEKSHSITLKEIERLS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 965 DMMQELETRI---EEEEERVLALGGEKKKLELNIQdleeqleeeeaarqKLQLEKVQLDAKIKKYEEdlaLTDDQNQKLL 1041
Cdd:PRK01156 225 IEYNNAMDDYnnlKSALNELSSLEDMKNRYESEIK--------------TAESDLSMELEKNNYYKE---LEERHMKIIN 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1042 KEKKLLEERANDLSQTLAEEEEKAKHLAKLKA---KHEATISELEErLHKDQQQRQESDRSKRKIETEVADLKEQLNERR 1118
Cdd:PRK01156 288 DPVYKNRNYINDYFKYKNDIENKKQILSNIDAeinKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILELEGYEMDYN 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1119 VQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNel 1198
Cdd:PRK01156 367 SYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR-- 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1199 ldsldtTAAQQELRSKreqeLATLKKSLEEETVNHegvladMRHKHSQELNSINDQLENL-RKAKTVLEKAKgtleaena 1277
Cdd:PRK01156 445 ------NMEMLNGQSV----CPVCGTTLGEEKSNH------IINHYNEKKSRLEEKIREIeIEVKDIDEKIV-------- 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1278 DLATELRSVNSsrqENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN-QLEEAELKASAAVKSASNM 1356
Cdd:PRK01156 501 DLKKRKEYLES---EEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVI 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEAQQLLEEETRQKLG-LSSKLRQIESE----KEALQEQLEEDDEAKRNYERKLAEVttqmQEIKKKAEEdadLAK 1431
Cdd:PRK01156 578 SLIDIETNRSRSNEIKKQLNdLESRLQEIEIGfpddKSYIDKSIREIENEANNLNNKYNEI----QENKILIEK---LRG 650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1432 ELEEGKKRLNKdIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVlelekkqknfDKILAEEKAISEQIA 1511
Cdd:PRK01156 651 KIDNYKKQIAE-IDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTI----------EILRTRINELSDRIN 719
|
650 660 670
....*....|....*....|....*....|
gi 62471805 1512 QERDTAEReaREKETKVLSVSRELDEAFDK 1541
Cdd:PRK01156 720 DINETLES--MKKIKKAIGDLKRLREAFDK 747
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1540-1783 |
6.05e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1540 DKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQF 1619
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1620 ErdllakeegaeEKRRGLVKQLRDLETEldeERKQRTAAVASKKklegDLKEIETTMEMHNKVKEDALKHAKKLQAQVKD 1699
Cdd:COG4942 100 E-----------AQKEELAELLRALYRL---GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1700 ALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEA 1779
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
....
gi 62471805 1780 RIAT 1783
Cdd:COG4942 242 RTPA 245
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1414-1631 |
6.23e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1414 TQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL---- 1489
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaral 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1490 --EKKQKNFDKILAEEKAISEQIaqerdtaerearekeTKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTAD 1567
Cdd:COG3883 96 yrSGGSVSYLDVLLGSESFSDFL---------------DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1568 KNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAE 1631
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1050-1662 |
8.15e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.66 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1050 RANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKI------ETEVADLKEQLNERRVQVDE 1123
Cdd:PRK04863 493 EAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLgknlddEDELEQLQEELEARLESLSE 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1124 MQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNElldSLD 1203
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVE---RDE 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1204 TTAAQQELRSKREQ-------ELATLKKSLE----------------EETVNHEGVLADMRHK-HSQELNSINDQLENLR 1259
Cdd:PRK04863 650 LAARKQALDEEIERlsqpggsEDPRLNALAErfggvllseiyddvslEDAPYFSALYGPARHAiVVPDLSDAAEQLAGLE 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1260 KAKTVLEKAKGTLEA-ENADLATELRSVNSSRQENDRR-------------RKQAESQIAELQVKLAEIERARSELQEKC 1325
Cdd:PRK04863 730 DCPEDLYLIEGDPDSfDDSVFSVEELEKAVVVKIADRQwrysrfpevplfgRAAREKRIEQLRAEREELAERYATLSFDV 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1326 TKLQQeaeniTNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLeeDDEAKRNY 1405
Cdd:PRK04863 810 QKLQR-----LHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGL--SALNRLLP 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1406 ERKLAEVTTQMQEIKKkAEEDADLAKELEEGKKRLNKDIEALERQVKELiaQNDRLDKSKKKIQSELEDATIELEAQRTK 1485
Cdd:PRK04863 883 RLNLLADETLADRVEE-IREQLDEAEEAKRFVQQHGNALAQLEPIVSVL--QSDPEQFEQLKQDYQQAQQTQRDAKQQAF 959
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1486 VL-ELEKKQKNFD-----KILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL 1559
Cdd:PRK04863 960 ALtEVVQRRAHFSyedaaEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL 1039
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1560 ANtqgtadknvhELEK-AKRALESQLAELKAQNEELEDDLqltedaklrleVNMQALRSQFERDLLAKEEGAEEkrrgLV 1638
Cdd:PRK04863 1040 KQ----------ELQDlGVPADSGAEERARARRDELHARL-----------SANRSRRNQLEKQLTFCEAEMDN----LT 1094
|
650 660
....*....|....*....|....
gi 62471805 1639 KQLRDLETELDEERKQRTAAVASK 1662
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAKAGW 1118
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1692-1973 |
1.35e-07 |
|
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: 56.99 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1692 KLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVlQLTEDLASSERARRAAE-----TERDELAEEIANNANK 1766
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQA-EKAERYKELKAELRELElallvLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1767 GSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAE 1846
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1847 IEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLK 1926
Cdd:TIGR02168 328 LE-SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1927 RNLDETEEELQKEKTQKRKYQRECE-----DMIESQEAMNREINSLKTKLRR 1973
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELER 458
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1735-1973 |
1.65e-07 |
|
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: 56.61 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1735 LTEDLASSERARRAAETERDELaEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSE--------VLLDRSRKAQ 1806
Cdd:TIGR02169 158 IIDEIAGVAEFDRKKEKALEEL-EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKekreyegyELLKEKEALE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1807 LQIEQLTTELAN-----EKSNSQKNENGRAL--LERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENegKE 1879
Cdd:TIGR02169 237 RQKEAIERQLASleeelEKLTEEISELEKRLeeIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE--KE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1880 RLLQQKANR--KMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQ 1957
Cdd:TIGR02169 315 RELEDAEERlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394
|
250
....*....|....*.
gi 62471805 1958 EAMNREINSLKTKLRR 1973
Cdd:TIGR02169 395 EKLKREINELKRELDR 410
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1719-1945 |
1.86e-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: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1719 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQsnsEVL 1798
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---EEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1799 LDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGK 1878
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR-ADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1879 ERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRK 1945
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
889-1420 |
4.32e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.11 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 889 EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQ-AEIELCAEAEESRSRLMARKQELEDMM 967
Cdd:pfam05483 269 KANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiATKTICQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 968 QELETRIEEEEERVLALGGEKKKLELNiqdleeqleeeeaaRQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLL 1047
Cdd:pfam05483 349 FVVTEFEATTCSLEELLRTEQQRLEKN--------------EDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1048 EERandlsQTLAEEEEKAKHLA-KLKAKHEATISELEER---LHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDE 1123
Cdd:pfam05483 415 AED-----EKLLDEKKQFEKIAeELKGKEQELIFLLQARekeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1124 MQA---QLAKREEELTQ----TLLRIDEESATKATAQKAQRELESQLAEIQEdleAEKAARAKAEKVRRDLSEELEALKN 1196
Cdd:pfam05483 490 LTAhcdKLLLENKELTQeasdMTLELKKHQEDIINCKKQEERMLKQIENLEE---KEMNLRDELESVREEFIQKGDEVKC 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1197 ELLDSLDTTAAQQELRSKREQELATLkksleEETVNHEGVLADMRHKHSQELNSINdqlENLRKAKTVLEKAKGTLEAEN 1276
Cdd:pfam05483 567 KLDKSEENARSIEYEVLKKEKQMKIL-----ENKCNNLKKQIENKNKNIEELHQEN---KALKKKGSAENKQLNAYEIKV 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1277 ADLATELRSVNSSRQE-NDRRRKQAESQIAELQVKLAEIERARSELQEkCTKLQQEAE-----NITNQLEEAELKASAAV 1350
Cdd:pfam05483 639 NKLELELASAKQKFEEiIDNYQKEIEDKKISEEKLLEEVEKAKAIADE-AVKLQKEIDkrcqhKIAEMVALMEKHKHQYD 717
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1351 KSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIK 1420
Cdd:pfam05483 718 KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDKK 787
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1297-1480 |
4.78e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.22 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1297 RKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENItnqLEEAELKASAAVKSASNmesqltEAQQLLEE--ETRQK 1374
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL---LEEAEKEAQQAIKEAKK------EADEIIKElrQLQKG 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1375 LGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVT----------TQMQEIKKKAEEDAdlAKELEEGKK-RLN-K 1442
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKvgdevkylslGQKGEVLSIPDDKE--AIVQAGIMKmKVPlS 677
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 62471805 1443 DIEALERQVKELIAQNDRLDKSKKKIQSEL-------EDATIELE 1480
Cdd:PRK00409 678 DLEKIQKPKKKKKKKPKTVKPKPRTVSLELdlrgmryEEALERLD 722
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1289-1760 |
5.85e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1289 SRQENDRRRKQAESqiAELQVKLAEIERARSELQEKCTKLQQEAEnitnQLEEAELKASAAVKSASnmesqltEAQQLLE 1368
Cdd:PRK04863 275 MRHANERRVHLEEA--LELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAAS-------DHLNLVQ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1369 EETRQKlglsSKLRQIESEKEALQEQLEEDdeakrnyerklAEVTTQMQEIKKKAEEDADLA-KELEEGKKRLNKDIEAL 1447
Cdd:PRK04863 342 TALRQQ----EKIERYQADLEELEERLEEQ-----------NEVVEEADEQQEENEARAEAAeEEVDELKSQLADYQQAL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1448 ERQVKELIAQND---RLDKSKKkiQSELEDATIEleaqrtkvlelekkqkNFDKILAEEKAISEQIAQERDTAEREarek 1524
Cdd:PRK04863 407 DVQQTRAIQYQQavqALERAKQ--LCGLPDLTAD----------------NAEDWLEEFQAKEQEATEELLSLEQK---- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1525 etkvLSVSRELDEAFDKIEDLenkrktLQNELDDLANTQgtADKNVHELEKA---KRALESQLAELKAQNEELEDDLQLT 1601
Cdd:PRK04863 465 ----LSVAQAAHSQFEQAYQL------VRKIAGEVSRSE--AWDVARELLRRlreQRHLAEQLQQLRMRLSELEQRLRQQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1602 EDAklrlevnmQALRSQFERDL---LAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTM-E 1677
Cdd:PRK04863 533 QRA--------ERLLAEFCKRLgknLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARApA 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1678 MHNKvkEDALKhakKLQAQVKDALRDAEEAKAAKEELQALSKEA-------ERKVKALEAEVLQLTE-DLASSERARRAA 1749
Cdd:PRK04863 605 WLAA--QDALA---RLREQSGEEFEDSQDVTEYMQQLLERERELtverdelAARKQALDEEIERLSQpGGSEDPRLNALA 679
|
490
....*....|.
gi 62471805 1750 ETERDELAEEI 1760
Cdd:PRK04863 680 ERFGGVLLSEI 690
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1090-1350 |
6.46e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1090 QQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQ--LAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQ 1167
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1168 EDLeaekaarakaekvrrdlseeleALKNELLDSLDTTAAQQELRSKR---EQELATLKKSLeeeTVNHEGVLAdmrhkh 1244
Cdd:COG3206 247 AQL----------------------GSGPDALPELLQSPVIQQLRAQLaelEAELAELSARY---TPNHPDVIA------ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1245 sqelnsINDQLENLRKAktvlekakgtLEAENADLATELRsvnSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEk 1324
Cdd:COG3206 296 ------LRAQIAALRAQ----------LQQEAQRILASLE---AELEALQAREASLQAQLAQLEARLAELPELEAELRR- 355
|
250 260 270
....*....|....*....|....*....|...
gi 62471805 1325 ctkLQQEAEN-------ITNQLEEAELKASAAV 1350
Cdd:COG3206 356 ---LEREVEVarelyesLLQRLEEARLAEALTV 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1443-1661 |
7.08e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 7.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1443 DIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTkvlELEKKQKNFDKILAEEKAISEQIAQERDTAEREAR 1522
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1523 E--------KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEEL 1594
Cdd:COG3883 94 AlyrsggsvSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1595 EDDLQLTEDAKLRLEVNMQALRSQFERdlLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVAS 1661
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAE--LEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1146-1365 |
7.21e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1146 SATKATAQKAQRELESQLAEIQEDLEAEKAARAkaekvrrDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKS 1225
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELD-------ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1226 LEEETVNHEGVLADMRHK-----------HSQELNSINDQLENLRK-----AKTV--LEKAKGTLEAENADLATELRSVN 1287
Cdd:COG3883 81 IEERREELGERARALYRSggsvsyldvllGSESFSDFLDRLSALSKiadadADLLeeLKADKAELEAKKAELEAKLAELE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1288 SSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1365
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1373-1619 |
1.09e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 53.78 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1373 QKLGLSsklrQIESEKEALQ-EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLA-KELEEGKKRLNKDIEALERQ 1450
Cdd:PRK05771 26 HELGVV----HIEDLKEELSnERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSvKSLEELIKDVEEELEKIEKE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1451 VKELIAQNDRLDKSKKKIQSELEDAT----IELEaqrtkvLELEKKQKNFDKILAE--EKAISEQIAQERDTAEREAREK 1524
Cdd:PRK05771 102 IKELEEEISELENEIKELEQEIERLEpwgnFDLD------LSLLLGFKYVSVFVGTvpEDKLEELKLESDVENVEYISTD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1525 ETKVLSV----SRELDEAFDKIEDLENKRKTLQNElddlantqGTADKNVHELEKAKRALESQL----AELKAQNEELED 1596
Cdd:PRK05771 176 KGYVYVVvvvlKELSDEVEEELKKLGFERLELEEE--------GTPSELIREIKEELEEIEKEResllEELKELAKKYLE 247
|
250 260
....*....|....*....|...
gi 62471805 1597 DLQLTEDaKLRLEVNMQALRSQF 1619
Cdd:PRK05771 248 ELLALYE-YLEIELERAEALSKF 269
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1358-1635 |
1.50e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 52.22 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1358 SQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGK 1437
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1438 KRLNKDIEALERQVKELiaqndrldkskKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTA 1517
Cdd:COG1340 81 DELNEKLNELREELDEL-----------RKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1518 E--REAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELE 1595
Cdd:COG1340 150 EkaKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELH 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 62471805 1596 DDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRR 1635
Cdd:COG1340 230 EEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1008-1427 |
1.61e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1008 ARQKLQLEKVQLDAKIKKYEEDLALTDD--QNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLkakhEATISELEER 1085
Cdd:COG4717 96 ELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAE 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1086 LHKDQQQ-RQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLA 1164
Cdd:COG4717 172 LAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1165 EIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEE-ETVNHEGVLADMRHK 1243
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEElEEEELEELLAALGLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1244 HSQELNSINDQLENLRKAKTVLEKAkgtleaenadlatelrsvnsSRQENDRRRKQAESQIAEL----QVKLAEIERARS 1319
Cdd:COG4717 332 PDLSPEELLELLDRIEELQELLREA--------------------EELEEELQLEELEQEIAALlaeaGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1320 ELQEKCTKLQQEAENITNQLEEA--ELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKealqEQLEE 1397
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELlgELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL----EQLEE 467
|
410 420 430
....*....|....*....|....*....|
gi 62471805 1398 DDEakrnYERKLAEVTTQMQEIKKKAEEDA 1427
Cdd:COG4717 468 DGE----LAELLQELEELKAELRELAEEWA 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1432-1598 |
1.71e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.46 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1432 ELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKilAEE-KAISEQI 1510
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN--NKEyEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1511 aqerDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANtqgtadknvhELEKAKRALESQLAELKAQ 1590
Cdd:COG1579 99 ----ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA----------ELDEELAELEAELEELEAE 164
|
....*...
gi 62471805 1591 NEELEDDL 1598
Cdd:COG1579 165 REELAAKI 172
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1208-1474 |
2.27e-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: 52.72 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1208 QQELRSKREQELATLKKSLEEETVNHEGVLADmrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATEL---- 1283
Cdd:pfam05667 242 KRKRTKLLKRIAEQLRSAALAGTEATSGASRS-----AQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEApaat 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1284 RSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE-----AELKASAAVKS-----A 1353
Cdd:pfam05667 317 SSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEElkeqnEELEKQYKVKKktldlL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1354 SNMESQLTEAQQLLEEETRQKLGLSsklRQIESEKEALQEQLEEDDEAKRN----YERKLAEVT---TQMQEIKKKAEED 1426
Cdd:pfam05667 397 PDAEENIAKLQALVDASAQRLVELA---GQWEKHRVPLIEEYRALKEAKSNkedeSQRKLEEIKelrEKIKEVAEEAKQK 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 62471805 1427 ADLAKELEEGKKRLNKDI--EALERQVKELIAQndrLDKSKKKIQSELED 1474
Cdd:pfam05667 474 EELYKQLVAEYERLPKDVsrSAYTRRILEIVKN---IKKQKEEITKILSD 520
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1063-1367 |
3.33e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 51.07 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1063 EKAKHLAKLKAKHEATISELEerlhkdQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRI 1142
Cdd:pfam00038 18 DKVRFLEQQNKLLETKISELR------QKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1143 DEESATKataqkaqRELESQLAEIQEDLEAEKAArakaekvRRDLSEELEALKNELLdsldttaaqqELRSKREQELATL 1222
Cdd:pfam00038 92 EDELNLR-------TSAENDLVGLRKDLDEATLA-------RVDLEAKIESLKEELA----------FLKKNHEEEVREL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1223 KKSLEEETVNHE----------GVLADMRHKHSQELNSINDQLENLRKAKTvlekAKGTLEAE-NADlatELRSVNSSRQ 1291
Cdd:pfam00038 148 QAQVSDTQVNVEmdaarkldltSALAEIRAQYEEIAAKNREEAEEWYQSKL----EELQQAAArNGD---ALRSAKEEIT 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1292 ENDRRRKQAESQIAELQVKLAEIERARSELQEkctKLQQEAENITNQLEEAElkaSAAVKSASNMESQLTEAQQLL 1367
Cdd:pfam00038 221 ELRRTIQSLEIELQSLKKQKASLERQLAETEE---RYELQLADYQELISELE---AELQETRQEMARQLREYQELL 290
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
910-1309 |
3.80e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.15 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 910 KLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKK 989
Cdd:pfam12128 584 KLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 990 KLELNIQdleeqlEEEEAARQKLQLEKVQLDAKIKKYEEDL--ALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKH 1067
Cdd:pfam12128 664 SEKDKKN------KALAERKDSANERLNSLEAQLKQLDKKHqaWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAA 737
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1068 LAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLnerrvqvdemqAQLAKREEELTQT--------L 1139
Cdd:pfam12128 738 IAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKI-----------ERIAVRRQEVLRYfdwyqetwL 806
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1140 LRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAekvrRDLSEELEALKNELLDSLDTtaaqqelrskREQEL 1219
Cdd:pfam12128 807 QRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEME----RKASEKQQVRLSENLRGLRC----------EMSKL 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1220 ATLKKSLEEETVNHE-----GVLADMRHKHSQELNSINDQLENLrkaKTVLEKAKGTLEAEN-ADLATELRSVNSSRQEN 1293
Cdd:pfam12128 873 ATLKEDANSEQAQGSigerlAQLEDLKLKRDYLSESVKKYVEHF---KNVIADHSGSGLAETwESLREEDHYQNDKGIRL 949
|
410
....*....|....*...
gi 62471805 1294 DRRRK--QAESQIAELQV 1309
Cdd:pfam12128 950 LDYRKlvPYLEQWFDVRV 967
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1540-1703 |
5.60e-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: 51.57 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1540 DKIEDLENKRK----TLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRL---EVNM 1612
Cdd:pfam05667 324 ETEEELQQQREeeleELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLpdaEENI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1613 QALRSQFE---RDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQrtaavaSKKKLEgDLKEIETTM---EMHNKVKEDA 1686
Cdd:pfam05667 404 AKLQALVDasaQRLVELAGQWEKHRVPLIEEYRALKEAKSNKEDE------SQRKLE-EIKELREKIkevAEEAKQKEEL 476
|
170
....*....|....*..
gi 62471805 1687 LKHakkLQAQVKDALRD 1703
Cdd:pfam05667 477 YKQ---LVAEYERLPKD 490
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1351-1569 |
6.05e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1351 KSASNMESQLTEAQQLLEEETRQK-LGLSSKLRQIESEKEALQEQLEEDDEAKRnyerklaevttQMQEIKKKAEEDAdl 1429
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKqAAEQERLKQLEKERLAAQEQKKQAEEAAK-----------QAALKQKQAEEAA-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1430 AKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSElEDATIELEAQRTKVLELEKKQKnfdkilAEEKAISEQ 1509
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAA-AEAKKKAEAEAAAKAAAEAKKK------AEAEAKKKA 211
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1510 IAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLEN-KRKTLQNELDDLANtQGTADKN 1569
Cdd:PRK09510 212 AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKaAAAKAAAEVDDLFG-GLDSGKN 271
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1247-1426 |
6.66e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.54 E-value: 6.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1247 ELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQvklAEIERARSELQEkcT 1326
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGN--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1327 KLQQEAENITNQLEEAELKASAAvksasnmESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLeedDEAKRNYE 1406
Cdd:COG1579 86 RNNKEYEALQKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAEL---DEELAELE 155
|
170 180
....*....|....*....|
gi 62471805 1407 RKLAEVTTQMQEIKKKAEED 1426
Cdd:COG1579 156 AELEELEAEREELAAKIPPE 175
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1239-1960 |
6.69e-06 |
|
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: 51.36 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1239 DMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRrkqAESQIAELQVKLAEIERAR 1318
Cdd:pfam10174 88 DLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLRKTLEEMELR---IETQKQTLGARDESIKKLL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1319 SELQEK--CTKLQQEAENITNQLEEAELKASaavksasNMESQL----TEAQQLLEEETRQklglsSKLRQIESEKEALQ 1392
Cdd:pfam10174 165 EMLQSKglPKKSGEEDWERTRRIAEAEMQLG-------HLEVLLdqkeKENIHLREELHRR-----NQLQPDPAKTKALQ 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1393 EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEedadlakeleegkkrLNKDIEALERQVKELIAQNDRLDKSK-KKIQSE 1471
Cdd:pfam10174 233 TVIEMKDTKISSLERNIRDLEDEVQMLKTNGL---------------LHTEDREEEIKQMEVYKSHSKFMKNKiDQLKQE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1472 LEDATIELEAQRTKVLELEKKQ---KNFDKILAEEKAISEQIAQ----ERDTAEREAREKETKvlsvsreLDEAFDKIED 1544
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQNsdcKQHIEVLKESLTAKEQRAAilqtEVDALRLRLEEKESF-------LNKKTKQLQD 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1545 LENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQltedaklrlevNMQALRSQFERDLL 1624
Cdd:pfam10174 371 LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVK-----------SLQTDSSNTDTALT 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1625 AKEEGAEEKRRgLVKQLRDletELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAK-KLQAQVKDALRd 1703
Cdd:pfam10174 440 TLEEALSEKER-IIERLKE---QREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKeHASSLASSGLK- 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1704 aeeakaakeelqalskeAERKVKALEAEVLQLTEDLASSERARRAaeterdelAEEIANNANKGSLMIDEKRRLEARIAT 1783
Cdd:pfam10174 515 -----------------KDSKLKSLEIAVEQKKEECSKLENQLKK--------AHNAEEAVRTNPEINDRIRLLEQEVAR 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1784 LEEELEEEQSNSEVLLDRSRKAQlqieqlttelaNEKSN-SQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATL 1862
Cdd:pfam10174 570 YKEESGKAQAEVERLLGILREVE-----------NEKNDkDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1863 EAKIANLEEQLENEGKerllqqkanrkmdKKIKELTMNIEDERRHVDQHKEqmdklnsRIKLLKRNLDETEEELQKEKTQ 1942
Cdd:pfam10174 639 EEARRREDNLADNSQQ-------------LQLEELMGALEKTRQELDATKA-------RLSSTQQSLAEKDGHLTNLRAE 698
|
730
....*....|....*...
gi 62471805 1943 KRKYQRECEDMieSQEAM 1960
Cdd:pfam10174 699 RRKQLEEILEM--KQEAL 714
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1052-1974 |
6.73e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.59 E-value: 6.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1052 NDLSQTLAEEEEKAKHL-------AKLK---AKHEATISELEERLH--------KDQQQRQESDRSKRKIETevADLKEq 1113
Cdd:TIGR01612 751 KDLNKILEDFKNKEKELsnkindyAKEKdelNKYKSKISEIKNHYNdqinidniKDEDAKQNYDKSKEYIKT--ISIKE- 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1114 lNERRVQVDEMQAQlakREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEaekaarakaekvrrdlSEELEA 1193
Cdd:TIGR01612 828 -DEIFKIINEMKFM---KDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEIS----------------DDKLND 887
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1194 LKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETV--NHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGT 1271
Cdd:TIGR01612 888 YEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKIceNTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDK 967
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1272 LEAENADLATELR------SVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTK-LQQEAENITNQLEEAEL 1344
Cdd:TIGR01612 968 FDNTLIDKINELDkafkdaSLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNdIEQKIEDANKNIPNIEI 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1345 KASAAVKSASN-MESQLTEAQQLLEEETRQKLGLS--------SKLRQIESEKEALQEQLEEDDEAKR------NYERKL 1409
Cdd:TIGR01612 1048 AIHTSIYNIIDeIEKEIGKNIELLNKEILEEAEINitnfneikEKLKHYNFDDFGKEENIKYADEINKikddikNLDQKI 1127
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1410 AEVTTQMQEIKKKAEEDADLAK----ELEE--GKKRLNKDIEALERQVKELIAQNDR----LDKSKKKIQ--SELEDATI 1477
Cdd:TIGR01612 1128 DHHIKALEEIKKKSENYIDEIKaqinDLEDvaDKAISNDDPEEIEKKIENIVTKIDKkkniYDEIKKLLNeiAEIEKDKT 1207
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1478 ELE---------AQRTKVLELEK----KQKNFDKILAEEKAISE--QIAQERDTAEREAR-----EKETKVLSVSRELDE 1537
Cdd:TIGR01612 1208 SLEevkginlsyGKNLGKLFLEKideeKKKSEHMIKAMEAYIEDldEIKEKSPEIENEMGiemdiKAEMETFNISHDDDK 1287
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1538 AF--------DKIEDLENK-----------------RKTLQNELDDLANTQGTADK---------NVHELEKAKRALE-- 1581
Cdd:TIGR01612 1288 DHhiiskkhdENISDIREKslkiiedfseesdindiKKELQKNLLDAQKHNSDINLylneianiyNILKLNKIKKIIDev 1367
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1582 -SQLAELKAQNEELEDDLQLTED--AKLRLEVNMQALRSQFERDLLAKEegaeekRRGLVKQLRDLETELDEERKQRTAA 1658
Cdd:TIGR01612 1368 kEYTKEIEENNKNIKDELDKSEKliKKIKDDINLEECKSKIESTLDDKD------IDECIKKIKELKNHILSEESNIDTY 1441
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1659 VASKKKLEGDLKEIETTMEMHNKVKEDALKHAKklQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVL---QL 1735
Cdd:TIGR01612 1442 FKNADENNENVLLLFKNIEMADNKSQHILKIKK--DNATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKElfeQY 1519
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1736 TEDLasSERARRAAETErdeLAEEIANNANKGSLMIDEKRRLEARIATLEeeleeeqSNSEVLLDRSRKAQLQIEQLTTE 1815
Cdd:TIGR01612 1520 KKDV--TELLNKYSALA---IKNKFAKTKKDSEIIIKEIKDAHKKFILEA-------EKSEQKIKEIKKEKFRIEDDAAK 1587
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1816 laNEKSNSQKNENGRALLERQNKELKakLAEIETAQRTKVKATiATLEAKIANLEEQLENEgkerllQQKANRKMDKKIK 1895
Cdd:TIGR01612 1588 --NDKSNKAAIDIQLSLENFENKFLK--ISDIKKKINDCLKET-ESIEKKISSFSIDSQDT------ELKENGDNLNSLQ 1656
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1896 ELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDEteeelqkektQKRKYQRE-CEDMIESQEAMNREINSLKTKLRRT 1974
Cdd:TIGR01612 1657 EFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQ----------HKKNYEIGiIEKIKEIAIANKEEIESIKELIEPT 1726
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1283-1476 |
1.11e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 49.76 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1283 LRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE----LKASAAVKSASNMES 1358
Cdd:pfam09787 39 LDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEeqlaTERSARREAEAELER 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1359 QLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLeeddeakrnyerklaevTTQMQEIKKKAEEDADLaKELEEGKK 1438
Cdd:pfam09787 119 LQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQL-----------------TSKSQSSSSQSELENRL-HQLTETLI 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 62471805 1439 RLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDAT 1476
Cdd:pfam09787 181 QKQTMLEALSTEKNSLVLQLERMEQQIKELQGEGSNGT 218
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1477-1661 |
1.19e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1477 IELEAQRTKVLELEKKQKNFDKILAEekaiseqIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNEL 1556
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1557 DDLantqgtadKNVHELEkakrALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFErdllAKEEGAEEKRRG 1636
Cdd:COG1579 83 GNV--------RNNKEYE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA----ELEAELEEKKAE 146
|
170 180
....*....|....*....|....*
gi 62471805 1637 LVKQLRDLETELDEERKQRTAAVAS 1661
Cdd:COG1579 147 LDEELAELEAELEELEAEREELAAK 171
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1184-1938 |
1.33e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 50.73 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1184 RRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEG-------VLADMRH-----KHSQELNSI 1251
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAasdhlnlVQTALRQqekieRYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1252 NDQLEnlrKAKTVLEKAKGTLEaenadlatelrsvnssrqENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQ- 1330
Cdd:PRK04863 361 EERLE---EQNEVVEEADEQQE------------------ENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1331 ----------------EAENITNQLEEAELKASAA----------VKSASNMESQLTEAQQLLE------------EETR 1372
Cdd:PRK04863 420 vqalerakqlcglpdlTADNAEDWLEEFQAKEQEAteellsleqkLSVAQAAHSQFEQAYQLVRkiagevsrseawDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1373 QKLGLSSKLRQIESEKEALQEQ---LEEDDEAKRNYERKLaevttqmQEIKKKAEEDADLAKELEEGKKRLNKDIEALER 1449
Cdd:PRK04863 500 ELLRRLREQRHLAEQLQQLRMRlseLEQRLRQQQRAERLL-------AEFCKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1450 QVKELIAQNDRLDKSKKKIQSELEdatiELEAQRTKVLE----LEKKQKNFDKILAEEKAISEQIAQ--ERdtaEREARE 1523
Cdd:PRK04863 573 SVSEARERRMALRQQLEQLQARIQ----RLAARAPAWLAaqdaLARLREQSGEEFEDSQDVTEYMQQllER---ERELTV 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1524 KETKVLSVSRELDEafdKIEDLENKRKTLQNELDDLANTQGT-------ADKNVHE-------------------LEKAK 1577
Cdd:PRK04863 646 ERDELAARKQALDE---EIERLSQPGGSEDPRLNALAERFGGvllseiyDDVSLEDapyfsalygparhaivvpdLSDAA 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1578 RALESQlaelkaqnEELEDDLQLTEDaklrlevNMQALRS------QFERDLLAKEEGAEEK-----------RRGLVKQ 1640
Cdd:PRK04863 723 EQLAGL--------EDCPEDLYLIEG-------DPDSFDDsvfsveELEKAVVVKIADRQWRysrfpevplfgRAAREKR 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1641 LRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKedalkhakkLQAQVKDALRDaeeakaakeeLQALSKE 1720
Cdd:PRK04863 788 IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVA---------FEADPEAELRQ----------LNRRRVE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1721 AERKVKALEAEVLQLTEDLASSErarraaetERDELAEEIANNANkgsLMIDEkrRLEARIATLEEELEEEQSnSEVLLD 1800
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAK--------EGLSALNRLLPRLN---LLADE--TLADRVEEIREQLDEAEE-AKRFVQ 914
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1801 RSRKAQLQIEQLTTELANEKSNSqknengrALLERQNKELKAKLaeietaQRTKVKA-TIATLEAKIANL--EEQLENEG 1877
Cdd:PRK04863 915 QHGNALAQLEPIVSVLQSDPEQF-------EQLKQDYQQAQQTQ------RDAKQQAfALTEVVQRRAHFsyEDAAEMLA 981
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1878 KERLLQQKANRKMDKKIKELTMNIEDERRHVDQH---KEQMDKLNSRIKLLKRNLDETEEELQK 1938
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaqyNQVLASLKSSYDAKRQMLQELKQELQD 1045
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1073-1226 |
1.40e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1073 AKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATK--A 1150
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKeiE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1151 TAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSL-DTTAAQQELRSKREQELATLKKSL 1226
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELaELEAELEELEAEREELAAKIPPEL 176
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1104-1365 |
1.51e-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: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1104 ETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEkaarakaekv 1183
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1184 RRDLSEELEALKNellDSLDTTAAQQELRSKreqelatlkkSLEEetvnhegvLADMRHKHSQELNSINDQLENLRKAKT 1263
Cdd:COG3883 85 REELGERARALYR---SGGSVSYLDVLLGSE----------SFSD--------FLDRLSALSKIADADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1264 VLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE 1343
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260
....*....|....*....|..
gi 62471805 1344 LKASAAVKSASNMESQLTEAQQ 1365
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAAS 245
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1068-1538 |
1.53e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 50.14 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1068 LAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADL-KEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEES 1146
Cdd:pfam07111 106 LAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1147 ATK----ATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDL------SEELEALKNELLDSL-------DTTAAQQ 1209
Cdd:pfam07111 186 AGEakqlAEAQKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppevhSQTWELERQELLDTMqhlqedrADLQATV 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1210 ELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSIndqLENLRKAKTVLEKAKGTLEAENADLATELRSVNSS 1289
Cdd:pfam07111 266 ELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEFPKKCRSL---LNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1290 RQENDRRRKQAESQIAE-LQVKLAEIERAR---SELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQ 1365
Cdd:pfam07111 343 LQEQVTSQSQEQAILQRaLQDKAAEVEVERmsaKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMT 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1366 LLEEETRQKLGLSSKL----------RQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE-DADLAKELE 1434
Cdd:pfam07111 423 RVEQAVARIPSLSNRLsyavrkvhtiKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRlDAELQLSAH 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1435 EGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQER 1514
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEK 582
|
490 500
....*....|....*....|....
gi 62471805 1515 dTAEREAREKEtKVLSVSRELDEA 1538
Cdd:pfam07111 583 -VAEVETRLRE-QLSDTKRRLNEA 604
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1284-1611 |
1.56e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1284 RSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEA 1363
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1364 QQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKD 1443
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1444 IEALERQVKELIAQndRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREARE 1523
Cdd:COG4372 166 LAALEQELQALSEA--EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1524 KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTED 1603
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
....*...
gi 62471805 1604 AKLRLEVN 1611
Cdd:COG4372 324 LAKKLELA 331
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1338-1488 |
1.57e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1338 QLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTT--Q 1415
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1416 MQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLE 1488
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1051-1605 |
1.58e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.34 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1051 ANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQR----QESDRSKRKIE-------------TEVADLKEQ 1113
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRselrQQLEQLRARIKelaarapawlaaqDALERLREQ 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1114 LNER---RVQVDEMQAQLAKREEELTQTLlriDEESATKATAQKAQRELeSQ--------------------LAEIQEDL 1170
Cdd:COG3096 618 SGEAladSQEVTAAMQQLLEREREATVER---DELAARKQALESQIERL-SQpggaedprllalaerlggvlLSEIYDDV 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1171 EAEKAAR-------AKAEKVRRDLS---EELEALKNELLDSL----------DTTAAQQEL------------------- 1211
Cdd:COG3096 694 TLEDAPYfsalygpARHAIVVPDLSavkEQLAGLEDCPEDLYliegdpdsfdDSVFDAEELedavvvklsdrqwrysrfp 773
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1212 ------RSKREQELATLKKSLEEETVNHEGVLADmrhkhSQELNSINDQLENLrkaktvleKAKGTLEAENADLATELRS 1285
Cdd:COG3096 774 evplfgRAAREKRLEELRAERDELAEQYAKASFD-----VQKLQRLHQAFSQF--------VGGHLAVAFAPDPEAELAA 840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1286 VNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQekctKLQQEA-----ENITNQLEEAELKASAAvKSASNMESQL 1360
Cdd:COG3096 841 LRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLN----KLLPQAnlladETLADRLEELREELDAA-QEAQAFIQQH 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1361 TEAQQLLEEetrqklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdlAKELEEGKKrL 1440
Cdd:COG3096 916 GKALAQLEP-------LVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHFSYEDA--VGLLGENSD-L 985
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1441 NkdiEALERQVKELIAQNDRLDKSKKKIQSELEDATIELE----AQRTKVLELEKKQKNFDKI------LAEEKAISE-Q 1509
Cdd:COG3096 986 N---EKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLAslksSRDAKQQTLQELEQELEELgvqadaEAEERARIRrD 1062
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1510 IAQERDTAEREAR-EKETKVLSVSRELDEAFDKIEDLENKRKTL-------------------QNELDDLANTQGTADKN 1569
Cdd:COG3096 1063 ELHEELSQNRSRRsQLEKQLTRCEAEMDSLQKRLRKAERDYKQEreqvvqakagwcavlrlarDNDVERRLHRRELAYLS 1142
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 62471805 1570 VHEL----EKAKRALesQLAElkAQNEELEDDLQLTEDAK 1605
Cdd:COG3096 1143 ADELrsmsDKALGAL--RLAV--ADNEHLRDALRLSEDPR 1178
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1714-1889 |
1.67e-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: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1714 LQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKgslmIDEKRRLEARIATLEEELEEEQS 1793
Cdd:COG3883 28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE----IEERREELGERARALYRSGGSVS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1794 NSEVLL-------------------DRSRKAQLQIEQLTTELANEKSnsqKNENGRALLERQNKELKAKLAEIEtAQRTK 1854
Cdd:COG3883 104 YLDVLLgsesfsdfldrlsalskiaDADADLLEELKADKAELEAKKA---ELEAKLAELEALKAELEAAKAELE-AQQAE 179
|
170 180 190
....*....|....*....|....*....|....*
gi 62471805 1855 VKATIATLEAKIANLEEQLENEGKERLLQQKANRK 1889
Cdd:COG3883 180 QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1391-1683 |
1.79e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1391 LQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADlakeleegkkRLNKDIEALERQVKELIAQNDRLDKSKKKIQS 1470
Cdd:PHA02562 179 LNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIA----------RKQNKYDELVEEAKTIKAEIEELTDELLNLVM 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1471 ELEDATIELEAQRTKVLELEKKQKNFDKILaeekaiseqiaqerdtaerEAREKETKVLSVSRELDEAFDKIEDLENKRK 1550
Cdd:PHA02562 249 DIEDPSAALNKLNTAAAKIKSKIEQFQKVI-------------------KMYEKGGVCPTCTQQISEGPDRITKIKDKLK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1551 TLQNELDDLANTQGTADKNVHELEKAKRALEsqlaELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDllaKEEga 1630
Cdd:PHA02562 310 ELQHSLEKLDTAIDELEEIMDEFNEQSKKLL----ELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN---AEE-- 380
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1631 eekrrglVKQLRDLETELDEERkqrtaavaSKKKLEGDLKEIETTMEMHNKVK 1683
Cdd:PHA02562 381 -------LAKLQDELDKIVKTK--------SELVKEKYHRGIVTDLLKDSGIK 418
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1393-1695 |
1.80e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.75 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1393 EQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSEL 1472
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1473 EDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERdtaereaREKETKVLSVSRElDEAFDKIEDLENKRKTL 1552
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLE-------WRQQTEVLSPEEE-KELVEKIKELEKELEKA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1553 QNElddlantqgtadknvHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSqfERDLLAKEegaee 1632
Cdd:COG1340 153 KKA---------------LEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYK--EADELRKE----- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1633 kRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQA 1695
Cdd:COG1340 211 -ADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEI 272
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1259-1433 |
1.83e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.78 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1259 RKAKTVLEKAKGTLEAENADLATElrsvnsSRQENDRRRKQAEsqiaelqvklAEIERARSELQEKCTKLQQEAENITNQ 1338
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALLE------AKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1339 LEEAELKASAAVKSASNMESQLTEAQQL------LEEETRQKLGLSSKLRQiESEKEALQEQLEEddEAKrnyerklAEV 1412
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKeeeleeLIEEQLQELERISGLTA-EEAKEILLEKVEE--EAR-------HEA 171
|
170 180
....*....|....*....|..
gi 62471805 1413 TTQMQEIKKKAEEDAD-LAKEL 1433
Cdd:PRK12704 172 AVLIKEIEEEAKEEADkKAKEI 193
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1074-1685 |
1.87e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.96 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1074 KHEATISELEERLHKDQQ-------QRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA-----QLAKREEELTQTLLR 1141
Cdd:PRK04863 352 RYQADLEELEERLEEQNEvveeadeQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTraiqyQQAVQALERAKQLCG 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1142 IDEESATKAtaQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNeLLDSLDTTAAQQELRSK------- 1214
Cdd:PRK04863 432 LPDLTADNA--EDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRK-IAGEVSRSEAWDVARELlrrlreq 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1215 ---------REQELATLKKSLEEETvNHEGVLADMRHKHSQELNSiNDQLENLRKAktvlekakgtLEAENADLATELRS 1285
Cdd:PRK04863 509 rhlaeqlqqLRMRLSELEQRLRQQQ-RAERLLAEFCKRLGKNLDD-EDELEQLQEE----------LEARLESLSESVSE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1286 VNSSRQENDRRRKQAESQIAELqvklAEIERARSELQEKCTKLQQEAenitnqleeaelkaSAAVKSASNMESQLteaQQ 1365
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRL----AARAPAWLAAQDALARLREQS--------------GEEFEDSQDVTEYM---QQ 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1366 LLEEETrqklGLSSKLRQIESEKEALQEQLE--------EDDEAKRNYER----KLAE---------------------- 1411
Cdd:PRK04863 636 LLERER----ELTVERDELAARKQALDEEIErlsqpggsEDPRLNALAERfggvLLSEiyddvsledapyfsalygparh 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1412 --VTTQMQEIKKKAEEDADL--------------------AKELEE----------------------GKKRLNKDIEAL 1447
Cdd:PRK04863 712 aiVVPDLSDAAEQLAGLEDCpedlyliegdpdsfddsvfsVEELEKavvvkiadrqwrysrfpevplfGRAAREKRIEQL 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1448 ERQVKELIAQNDRLDKSKKKIQSELE----------------DATIELEAQRTKVLELEKKQKNFDKilaeekaiSEQIA 1511
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQRLHQafsrfigshlavafeaDPEAELRQLNRRRVELERALADHES--------QEQQQ 863
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1512 QERDTAEREAREKETKVLSVSRELDEAF--DKIEDLENKRKTLQNELDDLANTQGTADKnvheLEKAKRALES---QLAE 1586
Cdd:PRK04863 864 RSQLEQAKEGLSALNRLLPRLNLLADETlaDRVEEIREQLDEAEEAKRFVQQHGNALAQ----LEPIVSVLQSdpeQFEQ 939
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1587 LKAQNEELEDDLQLTeDAKLRLEVNMQALRSQF----ERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASK 1662
Cdd:PRK04863 940 LKQDYQQAQQTQRDA-KQQAFALTEVVQRRAHFsyedAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY 1018
|
730 740
....*....|....*....|....
gi 62471805 1663 KKLEGDLK-EIETTMEMHNKVKED 1685
Cdd:PRK04863 1019 NQVLASLKsSYDAKRQMLQELKQE 1042
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
935-1170 |
2.08e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 935 LAEQLQAEIELCAEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQL 1014
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1015 EKVQLDAKIKKYEEDLAltddqnqkLLKEKKLLEERANDLSQTLAEEEekAKHLAKLKAKHEATISELEERLHKDQQQRQ 1094
Cdd:COG4942 91 EIAELRAELEAQKEELA--------ELLRALYRLGRQPPLALLLSPED--FLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1095 ESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDL 1170
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
697-724 |
2.15e-05 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 46.95 E-value: 2.15e-05
10 20
....*....|....*....|....*...
gi 62471805 697 SHLYKEQLAKLMDTLRNTNPNFVRCIIP 724
Cdd:cd01363 143 FEIINESLNTLMNVLRATRPHFVRCISP 170
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1075-1261 |
2.51e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1075 HEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELtqtllrideeSATKATAQK 1154
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQL----------ATERSARRE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1155 AQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELrskrEQELATLKKSLEEETVNHE 1234
Cdd:pfam09787 112 AEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKSQSSSSQSEL----ENRLHQLTETLIQKQTMLE 187
|
170 180
....*....|....*....|....*..
gi 62471805 1235 GVladmrhkhSQELNSINDQLENLRKA 1261
Cdd:pfam09787 188 AL--------STEKNSLVLQLERMEQQ 206
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1054-1428 |
2.51e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.41 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1054 LSQTLAEE----EEKAKHLAKLKA--KHEATISELEE---RLHK---------------DQQQRQESDRSKRK---IETE 1106
Cdd:PRK10246 459 RNAALNEMrqryKEKTQQLADVKTicEQEARIKDLEAqraQLQAgqpcplcgstshpavEAYQALEPGVNQSRldaLEKE 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1107 VADLKEQLNERRVQVDEMQAQLaKREEELTQTLLRidEESATKATAQKAQRELESQLAeIQEDLEAEKAARAKAEKVRRD 1186
Cdd:PRK10246 539 VKKLGEEGAALRGQLDALTKQL-QRDESEAQSLRQ--EEQALTQQWQAVCASLNITLQ-PQDDIQPWLDAQEEHERQLRL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1187 LSEELEaLKNELldsldttAAQQELRSKREQELATLKKSLEEE------TVNHEGVLADMRHKHSQELNSI---NDQLEN 1257
Cdd:PRK10246 615 LSQRHE-LQGQI-------AAHNQQIIQYQQQIEQRQQQLLTAlagyalTLPQEDEEASWLATRQQEAQSWqqrQNELTA 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1258 LRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLA-EIERARSELQEKCTKLQQEAENIT 1336
Cdd:PRK10246 687 LQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVlEAQRLQKAQAQFDTALQASVFDDQ 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1337 NQLEEAELKASAAvksasnmeSQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQM 1416
Cdd:PRK10246 767 QAFLAALLDEETL--------TQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQELAQLAQQL 838
|
410
....*....|....*....
gi 62471805 1417 Q-------EIKKKAEEDAD 1428
Cdd:PRK10246 839 RenttrqgEIRQQLKQDAD 857
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1314-1461 |
2.57e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.44 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1314 IERARSELQEKCTKLqqeaENITNQLEEAELKAsaavksasnmESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQE 1393
Cdd:PRK00409 504 IEEAKKLIGEDKEKL----NELIASLEELEREL----------EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLE 569
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1394 QLEED-----DEAKRNYERKLAEVTTQMQEikkkaEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRL 1461
Cdd:PRK00409 570 EAEKEaqqaiKEAKKEADEIIKELRQLQKG-----GYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1714-1960 |
2.95e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1714 LQALSKEAERKVKALEAEVLQLTEDLASSERARRAaeterdELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQS 1793
Cdd:pfam17380 293 FEKMEQERLRQEKEEKAREVERRRKLEEAEKARQA------EMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1794 NSEVLLDRSRKAQLQIEQLTTELANEKSNsQKNENGRA--LLE----RQNKELKAKLAEIETAQRTKVKATIATLEAKIA 1867
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVR-QELEAARKvkILEeerqRKIQQQKVEMEQIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1868 N------LEEQLENEGKERLLQQKANRKMDK----KIKELTMNIEDERRHV-----DQHKEQMDKLNSRIKLLKRNLDE- 1931
Cdd:pfam17380 446 RemervrLEEQERQQQVERLRQQEEERKRKKleleKEKRDRKRAEEQRRKIlekelEERKQAMIEEERKRKLLEKEMEEr 525
|
250 260 270
....*....|....*....|....*....|...
gi 62471805 1932 ----TEEELQKEKTQKRKYQRECEDMIESQEAM 1960
Cdd:pfam17380 526 qkaiYEEERRREAEEERRKQQEMEERRRIQEQM 558
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1152-1604 |
2.95e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 49.08 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1152 AQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKnELLDSLdttaaQQELRSKREQeLATLKKSLEEETV 1231
Cdd:pfam06160 84 AKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELK-DKYREL-----RKTLLANRFS-YGPAIDELEKQLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1232 NHEGVLADMrhkhsQELNSINDQLEnlrkAKTVLEKAKGTLEAENADLAtelrsvnssrqendrrrkqaesQIAELQVKL 1311
Cdd:pfam06160 157 EIEEEFSQF-----EELTESGDYLE----AREVLEKLEEETDALEELME----------------------DIPPLYEEL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1312 -AEIERARSELQEKCTKLQQEAENITNQLEEAELKAsaavksasnMESQLTEAQQLLEEETRQKLglSSKLRQIESEKEA 1390
Cdd:pfam06160 206 kTELPDQLEELKEGYREMEEEGYALEHLNVDKEIQQ---------LEEQLEENLALLENLELDEA--EEALEEIEERIDQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1391 LQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadLAKELEEGKKR--LNKD----IEALERQVKELIAQNDRLDK- 1463
Cdd:pfam06160 275 LYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKE---LKEELERVQQSytLNENelerVRGLEKQLEELEKRYDEIVEr 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1464 --SKKKIQSELEDatieleaqrtkvlELEKKQKNFDKILAEEKAISEQIAQERDtAEREAREketKVLSVSRELDEAFDK 1541
Cdd:pfam06160 352 leEKEVAYSELQE-------------ELEEILEQLEEIEEEQEEFKESLQSLRK-DELEARE---KLDEFKLELREIKRL 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1542 IE---------DLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDA 1604
Cdd:pfam06160 415 VEksnlpglpeSYLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEKTEELIDNATLAEQL 486
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1534-1770 |
3.32e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1534 ELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDL-QLTEDAKLRLEVNM 1612
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIeERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1613 QALRSQFERDLLAKEEGAEE--KRRGLVKQLRDLETELDEERKQRTAAVASKKKlegdlkeiettmemhnkvkedalkha 1690
Cdd:COG3883 97 RSGGSVSYLDVLLGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKA-------------------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1691 kKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLM 1770
Cdd:COG3883 151 -ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1722-1949 |
3.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1722 ERKVKALEAEVLQLTEDLassERARRAAETERDELA--EEIANNANKGSLMIDEKRRLEARIATLeeeleeeqsnsevll 1799
Cdd:COG4913 220 EPDTFEAADALVEHFDDL---ERAHEALEDAREQIEllEPIRELAERYAAARERLAELEYLRAAL--------------- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1800 dRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENegke 1879
Cdd:COG4913 282 -RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEE---- 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1880 rlLQQKANRkMDKKIKELTMNIEDER----RHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRE 1949
Cdd:COG4913 357 --RERRRAR-LEALLAALGLPLPASAeefaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1287-1480 |
3.50e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.26 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1287 NSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEnitnQLEEAELKASAAVKSASNMESQLTEAQQL 1366
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKK----QAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1367 LEEETRQKLGLSSKlrQIESEKEAlQEQLEEDDEAKRNYERKLAEVTTQ--MQEIKKKAEEDADLAKELEEGKKRLNKDI 1444
Cdd:PRK09510 148 KAEAEAKRAAAAAK--KAAAEAKK-KAEAEAAKKAAAEAKKKAEAEAAAkaAAEAKKKAEAEAKKKAAAEAKKKAAAEAK 224
|
170 180 190
....*....|....*....|....*....|....*.
gi 62471805 1445 EALERQVKELIAQNDRLDKSKKKIQSELEDATIELE 1480
Cdd:PRK09510 225 AAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1346-1683 |
3.51e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1346 ASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE 1425
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1426 DADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKA 1505
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1506 ISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLA 1585
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1586 ELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKL 1665
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
330
....*....|....*...
gi 62471805 1666 EGDLKEIETTMEMHNKVK 1683
Cdd:COG4372 353 NDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1807-1945 |
4.11e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1807 LQIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAKIANLEEQLENEGKERLLQ--- 1883
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-KEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalq 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1884 ------QKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRK 1945
Cdd:COG1579 96 keieslKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1053-1433 |
4.42e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 48.29 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1053 DLSQTLAEEEEKAKHLAKLKAKHEatISELEERLHKDQQQRQEsdrskrkIETEVADLKEQLNERRVQVDemqaQLAKRE 1132
Cdd:PRK04778 83 DIEEQLFEAEELNDKFRFRKAKHE--INEIESLLDLIEEDIEQ-------ILEELQELLESEEKNREEVE----QLKDLY 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1133 EELTQTLLrideesATKATAQKAQRELESQLAEIQEDLEAEKAAR-----AKAEKVRRDLSEELEALKN------ELLDS 1201
Cdd:PRK04778 150 RELRKSLL------ANRFSFGPALDELEKQLENLEEEFSQFVELTesgdyVEAREILDQLEEELAALEQimeeipELLKE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1202 LDTTAAQQ--ELRS---------------KREQELATLKKSLEE-----ETVNHEGVLADMRHKHSqELNSINDQLENLR 1259
Cdd:PRK04778 224 LQTELPDQlqELKAgyrelveegyhldhlDIEKEIQDLKEQIDEnlallEELDLDEAEEKNEEIQE-RIDQLYDILEREV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1260 KAKTVLEKAKGTL-------EAENADLATELRSVNSS----------RQENDRRRKQAESQIAELQVKLAEIERARSELQ 1322
Cdd:PRK04778 303 KARKYVEKNSDTLpdflehaKEQNKELKEEIDRVKQSytlneselesVRQLEKQLESLEKQYDEITERIAEQEIAYSELQ 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1323 EK----------CTKLQQEAENITNQLEEAELKASaavKSASNMESQLTEAQQLLEeetrqKLGL-------SSKLRQIE 1385
Cdd:PRK04778 383 EEleeilkqleeIEKEQEKLSEMLQGLRKDELEAR---EKLERYRNKLHEIKRYLE-----KSNLpglpedyLEMFFEVS 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1386 SEKEALQEQLEEddeAKRNYE---RKLAEVTTQMQEIKKKAEE---DADLAKEL 1433
Cdd:PRK04778 455 DEIEALAEELEE---KPINMEavnRLLEEATEDVETLEEETEElveNATLTEQL 505
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
887-1118 |
5.33e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 887 LLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKY----------QQALVEKTTLAEQLQAEI--------ELCAE 948
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEkallkqlaalERRIAALARRIRALEQELaaleaelaELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 949 AEESRSRLMARKQELEDMMQELETRIEEEEERVLalggekkkleLNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEE 1028
Cdd:COG4942 92 IAELRAELEAQKEELAELLRALYRLGRQPPLALL----------LSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1029 DLALTDDQNQkllkekklleeRANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVA 1108
Cdd:COG4942 162 LAALRAELEA-----------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
250
....*....|
gi 62471805 1109 DLKEQLNERR 1118
Cdd:COG4942 231 RLEAEAAAAA 240
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
883-1474 |
5.35e-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: 48.48 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 883 KVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQE 962
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNK 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 963 LEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEkvqldaKIKKYEEDLALTDDQNQkllk 1042
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK------NQEKKLEEIQNQISQNN---- 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1043 ekklleERANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVD 1122
Cdd:TIGR04523 335 ------KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1123 EMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSl 1202
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1203 dttaaQQELRSKrEQELatlkKSLEEETVNHEGVLADMRHKHSQELNSINDqlenlrkaktvLEKAKGTLEAENADLATE 1282
Cdd:TIGR04523 488 -----QKELKSK-EKEL----KKLNEEKKELEEKVKDLTKKISSLKEKIEK-----------LESEKKEKESKISDLEDE 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1283 LRSVNSSRQENDRRRKQAESQ--IAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKAsaavksasnmeSQL 1360
Cdd:TIGR04523 547 LNKDDFELKKENLEKEIDEKNkeIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI-----------SSL 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1361 TEAQQLLEEETRQklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKE-LEEGKKR 1439
Cdd:TIGR04523 616 EKELEKAKKENEK---LSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDwLKELSLH 692
|
570 580 590
....*....|....*....|....*....|....*
gi 62471805 1440 LNKDIEALERqvkelIAQNDRLDKSKKKIQSELED 1474
Cdd:TIGR04523 693 YKKYITRMIR-----IKDLPKLEEKYKEIEKELKK 722
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1119-1430 |
5.66e-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: 48.68 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1119 VQVDEMQAQLAKREEELTQTL----LRIDEESAtKATAQKAQRELESQLAEI---QEDLEAEKAARAKAE-KVRRD-LSE 1189
Cdd:NF012221 1535 VATSESSQQADAVSKHAKQDDaaqnALADKERA-EADRQRLEQEKQQQLAAIsgsQSQLESTDQNALETNgQAQRDaILE 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1190 ELEALKNEL------LDSLDTTAAQQELRSKREQE------LATLKKSLEEeTVNHEGV-LADMRHKHSQELNSINDQLe 1256
Cdd:NF012221 1614 ESRAVTKELttlaqgLDALDSQATYAGESGDQWRNpfagglLDRVQEQLDD-AKKISGKqLADAKQRHVDNQQKVKDAV- 1691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1257 nlrkAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAeIERARSELQEKctklQQEAENIT 1336
Cdd:NF012221 1692 ----AKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAA-ANDAQSRGEQD----ASAAENKA 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1337 NQleeaelkASAAVKSASNMESqlteaqqllEEETRQKL---GLSSKLRQIESEKEALQeQLEEDDEAKRNyERKLAEVT 1413
Cdd:NF012221 1763 NQ-------AQADAKGAKQDES---------DKPNRQGAagsGLSGKAYSVEGVAEPGS-HINPDSPAAAD-GRFSEGLT 1824
|
330
....*....|....*..
gi 62471805 1414 TQMQEikkkAEEDADLA 1430
Cdd:NF012221 1825 EQEQE----ALEGATNA 1837
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1310-1517 |
6.20e-05 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 46.56 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1310 KLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKL-------------- 1375
Cdd:pfam00261 2 KMQQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEeaekaadesergrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1376 GLSSKLRQIESEKEALQEQLEE----DDEAKRNYE---RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALE 1448
Cdd:pfam00261 82 VLENRALKDEEKMEILEAQLKEakeiAEEADRKYEevaRKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSLE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1449 RQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTA 1517
Cdd:pfam00261 162 ASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKEKYKAISEELDQT 230
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1256-1560 |
6.62e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 6.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1256 ENLRKAKTVLEKAKGTLEAENADLA---TELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEA 1332
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1333 ENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKrnYERKLAEV 1412
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1413 TTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKK 1492
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1493 QKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLA 1560
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
889-1324 |
6.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 889 EVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERK-----YQQALVEKTTLAEQLQAEI-ELCAEAEESRSRLMARKQE 962
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREElekleKLLQLLPLYQELEALEAELaELPERLEELEERLEELREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 963 LEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLK 1042
Cdd:COG4717 162 EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1043 EKKLLEER--ANDLSQTLAEEEEKAKHLAKLKAKHEATISELEERLHkdqqQRQESDRSKRKIETEVADLKEQLNERRVQ 1120
Cdd:COG4717 242 EERLKEARllLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLAL----LFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1121 VDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDleaekaarakaeKVRRDLSEELEALKNELLD 1200
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE------------ELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1201 SLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADM-RHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADL 1279
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEELEELREELAELEAELEQL 465
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 62471805 1280 AT--ELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEK 1324
Cdd:COG4717 466 EEdgELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1307-1696 |
7.44e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1307 LQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKASAAVKsasNMESQLTEAQQLLEEETRQKLGLSSKLRQIES 1386
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRR---ELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1387 EKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEdadlaKELEegkkrlnkdIEALERQVKELIAQNDRLDKSKK 1466
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLE-----RETE---------LERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1467 KIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKEtkvlSVSRELDEAFDKIEDLE 1546
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENE----ALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1547 NKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQlTEDAKLRLEVNMQALRSQ-FERDLLA 1625
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWA-QERETLQQSAEADKDRIEkLSAELQR 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1626 KEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQ 1696
Cdd:pfam07888 330 LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQR 400
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1075-1432 |
7.67e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.83 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1075 HEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQvDEMQAQLAKREEELTQTllriDEESATKATAQK 1154
Cdd:pfam09731 47 VLYALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIP-RQSGVSSEVAEEEKEAT----KDAAEAKAQLPK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1155 AQRELESQLAEIQEDLEAE-----KAARAKAEKVRRDLSEELEALKNELLDSLD------TTAAQQELRSKRE--QELAT 1221
Cdd:pfam09731 122 SEQEKEKALEEVLKEAISKaesatAVAKEAKDDAIQAVKAHTDSLKEASDTAEIsrekatDSALQKAEALAEKlkEVINL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1222 LKKSLEEETVNHEGVLADMRHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSV---------NSSRQE 1292
Cdd:pfam09731 202 AKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIfpdiipvlkEDNLLS 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1293 NDR---------------RRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAEN-ITNQLEEAELKASAAV-KSASN 1355
Cdd:pfam09731 282 NDDlnsliahahreidqlSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEvRAADEAQLRLEFEREReEIRES 361
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1356 MESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKE 1432
Cdd:pfam09731 362 YEEKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELLANLKGLEKATSSHSEVEDE 438
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1841-1959 |
8.76e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1841 KAKLAEIETAQRTKVKAtiATLEAKiaNLEEQLENEGKERLLQQKanRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNS 1920
Cdd:PRK12704 30 EAKIKEAEEEAKRILEE--AKKEAE--AIKKEALLEAKEEIHKLR--NEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110
....*....|....*....|....*....|....*....
gi 62471805 1921 RIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEA 1959
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1087-1942 |
1.14e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1087 HKDQQQRQESDRSKRKIETEVADLKEQLnerrVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEI 1166
Cdd:TIGR01612 561 HEIKKELEEENEDSIHLEKEIKDLFDKY----LEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIDLKKIIENNNAYI 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1167 QEDLEAE--------KAARAKAEKVRRDLSE----ELEALKNEL--------LDSLDTTAAQQELRSKREQELATLKkSL 1226
Cdd:TIGR01612 637 DELAKISpyqvpehlKNKDKIYSTIKSELSKiyedDIDALYNELssivkenaIDNTEDKAKLDDLKSKIDKEYDKIQ-NM 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1227 EEETV--------NHEGVLADM-----RHKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADL------ATELRSV- 1286
Cdd:TIGR01612 716 ETATVelhlsnieNKKNELLDIiveikKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELnkykskISEIKNHy 795
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1287 -------NSSRQENDRRRKQAESQIAELQVK-------LAEIERARSELQEKCTKL----QQEAENITNQLEE-AEL--- 1344
Cdd:TIGR01612 796 ndqinidNIKDEDAKQNYDKSKEYIKTISIKedeifkiINEMKFMKDDFLNKVDKFinfeNNCKEKIDSEHEQfAELtnk 875
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1345 -KASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQ--EQLEEDDEAKRNYERKLAEVTTQmqEIKK 1421
Cdd:TIGR01612 876 iKAEISDDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKicENTKESIEKFHNKQNILKEILNK--NIDT 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1422 KAEEDADLAKELEEGKKRLNKDIEALERQVKELI-----AQNDRLDKSKKKIQSEL---EDATI--ELEAQRTKVLELEK 1491
Cdd:TIGR01612 954 IKESNLIEKSYKDKFDNTLIDKINELDKAFKDASlndyeAKNNELIKYFNDLKANLgknKENMLyhQFDEKEKATNDIEQ 1033
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1492 KQKNFDKILAE-EKAISEQIAQERDTAEREA------------REKETKVLSVSrELDEA-----FDKIEDLENKRKTlq 1553
Cdd:TIGR01612 1034 KIEDANKNIPNiEIAIHTSIYNIIDEIEKEIgkniellnkeilEEAEINITNFN-EIKEKlkhynFDDFGKEENIKYA-- 1110
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1554 NEL----DDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDdlqltedaklrlevnmqalrsqferdlLAKEEG 1629
Cdd:TIGR01612 1111 DEInkikDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLED---------------------------VADKAI 1163
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1630 AEEKRRGLVKQLRDLETELDEERKqrtaAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEeaka 1709
Cdd:TIGR01612 1164 SNDDPEEIEKKIENIVTKIDKKKN----IYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEK---- 1235
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1710 akeelqalsKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAE----EIANNANKGSLMIDEK--------RRL 1777
Cdd:TIGR01612 1236 ---------KKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEmetfNISHDDDKDHHIISKKhdenisdiREK 1306
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1778 EARIATLEEELEEEQSNSEVL---LDRSRKAQLQIEQLTTELAN----EKSNSQKN-----ENGRALLERQNKELKAKLA 1845
Cdd:TIGR01612 1307 SLKIIEDFSEESDINDIKKELqknLLDAQKHNSDINLYLNEIANiyniLKLNKIKKiidevKEYTKEIEENNKNIKDELD 1386
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1846 EIETAQRT-KVKATIATLEAKIanleeqlenegkERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKL 1924
Cdd:TIGR01612 1387 KSEKLIKKiKDDINLEECKSKI------------ESTLDDKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLL 1454
|
970
....*....|....*...
gi 62471805 1925 LKRNLdeteeELQKEKTQ 1942
Cdd:TIGR01612 1455 LFKNI-----EMADNKSQ 1467
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1629-1906 |
1.21e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1629 GAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMemhnkvkedalkhakklqaqvkdalrdaeeak 1708
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1709 aakeelqalsKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIAnnankgslmidekRRLEARIATLEEEL 1788
Cdd:COG4942 65 ----------AALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA-------------ELLRALYRLGRQPP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1789 EEEQSNSEVLLDRSRKAQL---QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIEtAQRTKVKATIATLEAK 1865
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYlkyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELE-EERAALEALKAERQKL 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 62471805 1866 IANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERR 1906
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1505-1722 |
1.30e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1505 AISEQIAQERDTAEREAREKETKVLSvsRELDEAFDKIEDLENKRKTL--QNELDDLANTQGTADKNVHELEKAKRALES 1582
Cdd:COG3206 156 ALAEAYLEQNLELRREEARKALEFLE--EQLPELRKELEEAEAALEEFrqKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1583 QLAELKAQNEELEDDLQLTEDAKLRLEVN--MQALRSQfERDLLAKEEGAEEK-------RRGLVKQLRDLETELDEERK 1653
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQ-LAELEAELAELSARytpnhpdVIALRAQIAALRAQLQQEAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1654 QRTAAVASKKK-LEGDLKEIETTMEMHnkvkEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAE 1722
Cdd:COG3206 313 RILASLEAELEaLQAREASLQAQLAQL----EARLAELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1354-1612 |
1.37e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1354 SNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKEL 1433
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1434 EEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILA--EEKAISEQIA 1511
Cdd:COG4372 107 QEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1512 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQN 1591
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260
....*....|....*....|.
gi 62471805 1592 EELEDDLQLTEDAKLRLEVNM 1612
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEA 287
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1368-1812 |
1.38e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1368 EEETRQKLGLSSKLRQiesEKEALQEQLEEDDEAKRNYERKLAEVTtqmqeikkkaEEDADLAKELEEGKKRLNKDIEAL 1447
Cdd:PRK04863 278 ANERRVHLEEALELRR---ELYTSRRQLAAEQYRLVEMARELAELN----------EAESDLEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1448 ERQVKEliaqndrldkskKKIQSELEDATIELEAQrtkvlelekkqknfdkilaeeKAISEQIAQERDTAEREAREKETK 1527
Cdd:PRK04863 345 RQQEKI------------ERYQADLEELEERLEEQ---------------------NEVVEEADEQQEENEARAEAAEEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1528 VLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEE---LEDDLQLTEDA 1604
Cdd:PRK04863 392 VDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEEllsLEQKLSVAQAA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1605 KLRLEVNMQALRSqferdlLAKEEGAEEKRRGLVKQLRDLeteldeeRKQRTAAvASKKKLEGDLKEIETTMEMHNKVKE 1684
Cdd:PRK04863 472 HSQFEQAYQLVRK------IAGEVSRSEAWDVARELLRRL-------REQRHLA-EQLQQLRMRLSELEQRLRQQQRAER 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1685 DALKHAKKLQAQVKDAlrdaeeakaakEELQALSKEAERKVKALEAEVlqltedlaSSERARRAA-ETERDELAEEIANN 1763
Cdd:PRK04863 538 LLAEFCKRLGKNLDDE-----------DELEQLQEELEARLESLSESV--------SEARERRMAlRQQLEQLQARIQRL 598
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1764 ANK------------------GSLMIDEKRRLEARIATLEEELEEEQSNSEVlldRSRKAQL--QIEQL 1812
Cdd:PRK04863 599 AARapawlaaqdalarlreqsGEEFEDSQDVTEYMQQLLERERELTVERDEL---AARKQALdeEIERL 664
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
854-1144 |
1.49e-04 |
|
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: 46.97 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 854 QQLNAIRIIQRNCAAYLKLRNWQWWRLYTKV----KPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQAL 929
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQIsalrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 930 VEKTTLAEQLQAEIElcaEAEESRSRLMARKQELEDMMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAAR 1009
Cdd:TIGR02168 778 AEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1010 QKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKhlaklkakheatisELEERLHKD 1089
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS--------------ELRRELEEL 920
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1090 QQQRQESDRSKRKIETEVADLKEQLNER-RVQVDEMQAQLAKREEELTQTLLRIDE 1144
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1332-1598 |
1.60e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1332 AENITNQLEEAELKAS-AAVKSASNMESQLTEAQQLLEeetrQKLGLSSKLRQIESEKEALQEQLEEDDEakrnyerKLA 1410
Cdd:PRK11281 29 AASNGDLPTEADVQAQlDALNKQKLLEAEDKLVQQDLE----QTLALLDKIDRQKEETEQLKQQLAQAPA-------KLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1411 EVTTQMQEIKKKAEEDA--DLAK-ELEEGKKRLNKDIEALERQVKELIAQNDRLDKSkkkiQSELEDATIELEAQRTKVL 1487
Cdd:PRK11281 98 QAQAELEALKDDNDEETreTLSTlSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL----QTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1488 ELEKKQKNF------------DKILAEEKAISEQIAQERdtAEREAREKETKVLSVSRELDEAfdKIEDLENKRKTLQNE 1555
Cdd:PRK11281 174 QIRNLLKGGkvggkalrpsqrVLLQAEQALLNAQNDLQR--KSLEGNTQLQDLLQKQRDYLTA--RIQRLEHQLQLLQEA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 62471805 1556 LDD--LANTQGTAdKNVHELEKAKRALESQL--AELkAQNEELEDDL 1598
Cdd:PRK11281 250 INSkrLTLSEKTV-QEAQSQDEAARIQANPLvaQEL-EINLQLSQRL 294
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1656-1964 |
1.61e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1656 TAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQL 1735
Cdd:PRK10929 19 AATAPDEKQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1736 TEDLASSErarraaeterdelaeeiannankgslmidekrrLEARIatleeeleeEQSNSEvLLDRSRkaQLQIEQlttE 1815
Cdd:PRK10929 99 PPNMSTDA---------------------------------LEQEI---------LQVSSQ-LLEKSR--QAQQEQ---D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1816 LANEKSNS------QKNENGRAL--LERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEeqlenegkerLLQQKAN 1887
Cdd:PRK10929 131 RAREISDSlsqlpqQQTEARRQLneIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELE----------LAQLSAN 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1888 RKmdkkiKELTmniedeRRHVDQHKEQMDKLNSRIKLLKRNLD---ETEEELQKEKTQKRKYQreCEDM---IESQEAMN 1961
Cdd:PRK10929 201 NR-----QELA------RLRSELAKKRSQQLDAYLQALRNQLNsqrQREAERALESTELLAEQ--SGDLpksIVAQFKIN 267
|
...
gi 62471805 1962 REI 1964
Cdd:PRK10929 268 REL 270
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1449-1886 |
1.66e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 46.21 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1449 RQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKvleLEKKQKNFDKILAEEKAISEQIA---QERDTAEREAREKE 1525
Cdd:pfam19220 20 EDLRSLKADFSQLIEPIEAILRELPQAKSRLLELEAL---LAQERAAYGKLRRELAGLTRRLSaaeGELEELVARLAKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1526 TKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLA-NTQGTADKNVHELEKAKrALESQLAELKAQNEELEDDLQLTEDA 1604
Cdd:pfam19220 97 AALREAEAAKEELRIELRDKTAQAEALERQLAAETeQNRALEEENKALREEAQ-AAEKALQRAEGELATARERLALLEQE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1605 KLRLEVNMQALRSQFERdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKE 1684
Cdd:pfam19220 176 NRRLQALSEEQAAELAE-LTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLRMKLEALT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1685 DALKHAKKLQAQVKDALRDAEEA----KAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAeei 1760
Cdd:pfam19220 255 ARAAATEQLLAEARNQLRDRDEAiraaERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLT--- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1761 annankgslmidekRRLEARIATLeeeleeeqsnsEVLLDRSRKAQLQIEQLTTELANEKsnsqknengrallerqnkel 1840
Cdd:pfam19220 332 --------------KALAAKDAAL-----------ERAEERIASLSDRIAELTKRFEVER-------------------- 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 62471805 1841 kaklaeietaqrtkvkatiATLEAKIANLEEQLENEGKERLLQQKA 1886
Cdd:pfam19220 367 -------------------AALEQANRRLKEELQRERAERALAQGA 393
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
841-1345 |
2.01e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 841 RGFLARRNYQKRLQQ--LNAIRIIQRNCAAYLKLRNWQWWRLYTKVKPLLEVTKQEEKLVQKEDELKQVREKldtlaknt 918
Cdd:TIGR00618 423 QGQLAHAKKQQELQQryAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA-------- 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 919 QEYERKYQQALVEKTTLaeQLQAEIELCAEAEESRSRLMARKQeledmmqeletrieeeeeRVLALGGEKKKLELNIQDL 998
Cdd:TIGR00618 495 RLLELQEEPCPLCGSCI--HPNPARQDIDNPGPLTRRMQRGEQ------------------TYAQLETSEEDVYHQLTSE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 999 EEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTddqnqkllkekKLLEERANDLSQTLAEEEEK---AKHLAKLKAKH 1075
Cdd:TIGR00618 555 RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-----------QNITVRLQDLTEKLSEAEDMlacEQHALLRKLQP 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1076 EATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQaQLAKREEELTQTLLRIDEESATKATaqka 1155
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE-LLASRQLALQKMQSEKEQLTYWKEM---- 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1156 qrelesqLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDttAAQQELRSKREQELATLKKSLEEETVNHEG 1235
Cdd:TIGR00618 699 -------LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARED--ALNQSLKELMHQARTVLKARTEAHFNNNEE 769
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1236 VLADMrhKHSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATE-LRSVNSSRQENDRRRKQAESQIAELQVKLAEI 1314
Cdd:TIGR00618 770 VTAAL--QTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
490 500 510
....*....|....*....|....*....|....
gi 62471805 1315 ERARSELQEKCTKLQQ---EAENITNQLEEAELK 1345
Cdd:TIGR00618 848 THQLLKYEECSKQLAQltqEQAKIIQLSDKLNGI 881
|
|
| CagA_N |
pfam18971 |
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial ... |
1357-1766 |
2.05e-04 |
|
CagA protein; The Helicobacter pylori type IV secretion effector CagA is a major bacterial virulence determinant and critical for gastric carcinogenesis. X-ray crystallographic analysis of the N-terminal CagA fragment (residues 1-876) revealed that the region has a structure comprised of three discrete domains. Domain I constitutes a mobile CagA N terminus, while Domain II tethers CagA to the plasma membrane by interacting with membrane phosphatidylserine. Domain III interacts intramolecularly with the intrinsically disordered C-terminal region, and this interaction potentiates the pathogenic scaffold/hub function of CagA.
Pssm-ID: 408741 [Multi-domain] Cd Length: 876 Bit Score: 46.69 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEAQQLL-EEETRQKLGLSSKLRQ--------IESEKEALQEQLEEDDEAKRNYERKLAevTTQMQEIKKKAEEDA 1427
Cdd:pfam18971 383 EDQLTGSQRALsQEEIRNKVDFMEFLAQnntkldnlSEKEKEKFQNEIEDFQKDSKAYLDALG--NDRIAFVSKKDTKHS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1428 DLAKELEEGKkrlnkdieaLERQVKELIAQNDR-LDKSKK-KIQSELE-DATIELEAQRTKvleLEKKQKNFDKILAEEK 1504
Cdd:pfam18971 461 ALITEFNNGD---------LSYTLKDYGKKADKaLDREKNvTLQGSLKhDGVMFVDYSNFK---YTNASKNPNKGVGATN 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1505 AISEQIAQERDTA-------------EREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDL--ANTQGTADKN 1569
Cdd:pfam18971 529 GVSHLEAGFNKVAvfnlpdlnnlaitSFVRRNLENKLTAKGLSLQEANKLIKDFLSSNKELAGKALNFnkAVAEAKSTGN 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1570 VHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKR--------------- 1634
Cdd:pfam18971 609 YDEVKKAQKDLEKSLRKREHLEKEVEKKLESKSGNKNKMEAKAQANSQKDEIFALINKEANRDARaiaytqnlkgikrel 688
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1635 ----RGLVKQLRDLETELDE----ERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKE-----DALKHAKK--------- 1692
Cdd:pfam18971 689 sdklEKISKDLKDFSKSFDEfkngKNKDFSKAEETLKALKGSVKDLGINPEWISKVENlnaalNEFKNGKNkdfskvtqa 768
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1693 ---LQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETE------RDELAEEIANN 1763
Cdd:pfam18971 769 ksdLENSVKDVIINQKVTDKVDNLNQAVSVAKAMGDFSRVEQVLADLKNFSKEQLAQQAQKNEdfntgkNSELYQSVKNS 848
|
...
gi 62471805 1764 ANK 1766
Cdd:pfam18971 849 VNK 851
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1364-1635 |
2.09e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 46.27 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1364 QQLLEEETRQKLGLSSKLRQIESEKEAL----QEQL----EEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEE 1435
Cdd:pfam17380 307 EKAREVERRRKLEEAEKARQAEMDRQAAiyaeQERMamerERELERIRQEERKRELERIRQEEIAMEISRMRELERLQME 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1436 GKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLEL-EKKQKNFDKILAEEKAISEQIAQER 1514
Cdd:pfam17380 387 RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLeEERAREMERVRLEEQERQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1515 DTAEREAREK--------------ETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTqgtadknVHELEKAKRAL 1580
Cdd:pfam17380 467 QQEEERKRKKlelekekrdrkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA-------IYEEERRREAE 539
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 1581 ESQLAElkaqnEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRR 1635
Cdd:pfam17380 540 EERRKQ-----QEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1581-1976 |
3.00e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 45.89 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1581 ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLlakEEGAEEKRRGL--VKQLRDLETELDEERKQRTAA 1658
Cdd:pfam05557 1 RAELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQL---DRESDRNQELQkrIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1659 VASKKKLEgdlkeieTTMEMHNKVKEDALKHAKKLQAQVKDALRD-AEEAKAAKEELQALSKEAERKVKALE------AE 1731
Cdd:pfam05557 78 NRLKKKYL-------EALNKKLNEKESQLADAREVISCLKNELSElRRQIQRAELELQSTNSELEELQERLDllkakaSE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1732 VLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLeARIATLEEELEEEQSNSEVLldrsRKAQLQIEQ 1811
Cdd:pfam05557 151 AEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSEL-ARIPELEKELERLREHNKHL----NENIENKLL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1812 LTTELANEKSNSQKNENGR---ALLERQNKELKAKLAEIE-TAQRTK--------VKATIATLEAKIANLEEQLENEGKE 1879
Cdd:pfam05557 226 LKEEVEDLKRKLEREEKYReeaATLELEKEKLEQELQSWVkLAQDTGlnlrspedLSRRIEQLQQREIVLKEENSSLTSS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1880 RLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSR-------IKLLKRNLDETEEELQKEKT--QKRKYQREC 1950
Cdd:pfam05557 306 ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRvllltkeRDGYRAILESYDKELTMSNYspQLLERIEEA 385
|
410 420
....*....|....*....|....*.
gi 62471805 1951 EDMIESQEAMNREINSLKTKLRRTGG 1976
Cdd:pfam05557 386 EDMTQKMQAHNEEMEAQLSVAEEELG 411
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1535-1968 |
3.10e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1535 LDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQA 1614
Cdd:PRK01156 164 LERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1615 LRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQR---TAAVASKKKLEG---DLKEIETTMEMHNKVK----- 1683
Cdd:PRK01156 244 LSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKiinDPVYKNRNYINDyfkYKNDIENKKQILSNIDaeink 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1684 -EDALKHAKKLQAQVKDALRDAEEAKAAKEEL----------QALSKEAERKVKALEAEVLQLTEDLASSERARRAAETE 1752
Cdd:PRK01156 324 yHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQIlelegyemdyNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEID 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1753 RDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSR-----------KAQLQIEQLTTELANEKS 1821
Cdd:PRK01156 404 PDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVcpvcgttlgeeKSNHIINHYNEKKSRLEE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1822 NSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANrKMDKKIKELTMNI 1901
Cdd:PRK01156 484 KIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYE-EIKNRYKSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1902 EDERRH-------------VDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLK 1968
Cdd:PRK01156 563 LDSKRTswlnalavislidIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENK 642
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1483-1696 |
3.38e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1483 RTKVLELEKKqknFDKILAEEKAISEQIAQErdtAEREAREKETKVLS-VSRELDEAFDKIEDLENKrktLQNELDDLAN 1561
Cdd:PRK12704 30 EAKIKEAEEE---AKRILEEAKKEAEAIKKE---ALLEAKEEIHKLRNeFEKELRERRNELQKLEKR---LLQKEENLDR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1562 TQGTADKNVHELEKAKRALESQLAELKAQNEELEddlQLTEDAKLRLEVNMQalrsqferdlLAKEEGAEEkrrglvkQL 1641
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELE---ELIEEQLQELERISG----------LTAEEAKEI-------LL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 1642 RDLETELDEERKQRtaavaskkklegdLKEIEttmemhNKVKEDALKHAKKLQAQ 1696
Cdd:PRK12704 161 EKVEEEARHEAAVL-------------IKEIE------EEAKEEADKKAKEILAQ 196
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1542-1703 |
3.71e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.62 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1542 IEDLENKRKTLQNELDDLANTqgTADKNVHELEKAKRALESQLAELKAQNEELEDDLqltEDAKLRLEvnmqalRSQFER 1621
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKE--HEERELTEEEEEIRRLEEQVERLEAEVEELEAEL---EEKDERIE------RLEREL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1622 DLLAKEEGAEEKRRGLVKQLR----DLETELDEERKQRtaavaskKKLEGDLKEIEttmEMHNKVKEDALKHAKKLQAQV 1697
Cdd:COG2433 451 SEARSEERREIRKDREISRLDreieRLERELEEERERI-------EELKRKLERLK---ELWKLEHSGELVPVKVVEKFT 520
|
....*.
gi 62471805 1698 KDALRD 1703
Cdd:COG2433 521 KEAIRR 526
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
919-1661 |
4.08e-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: 45.71 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 919 QEYERKYQQALVEkttLAEQLQAEIELCAEAEESRSRLMARKQELE-----------------DMMQELETRIEEEeerV 981
Cdd:COG3096 346 QEKIERYQEDLEE---LTERLEEQEEVVEEAAEQLAEAEARLEAAEeevdslksqladyqqalDVQQTRAIQYQQA---V 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 982 LALGGEKKKLELNIQDLEEQLEEEEAARQKLQlekvQLDAKIKKYEEDLALTDDQNQK--------LLKEKKLLEERAND 1053
Cdd:COG3096 420 QALEKARALCGLPDLTPENAEDYLAAFRAKEQ----QATEEVLELEQKLSVADAARRQfekayelvCKIAGEVERSQAWQ 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1054 LSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEVADlkeqlnerRVQVDEMQAQLAKREE 1133
Cdd:COG3096 496 TARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDA--------AEELEELLAELEAQLE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1134 ELTQTLlrideesatkATAQKAQRELESQLaeiqEDLEAEKAARAKAEKVRRDLSEELEALKNE----LLDSLDTTAA-Q 1208
Cdd:COG3096 568 ELEEQA----------AEAVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQsgeaLADSQEVTAAmQ 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1209 QELRSKRE-----QELATLKKSLEE--ETVNHEGVLADMR----------------------------------HKHS-- 1245
Cdd:COG3096 634 QLLEREREatverDELAARKQALESqiERLSQPGGAEDPRllalaerlggvllseiyddvtledapyfsalygpARHAiv 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1246 -QELNSINDQLENL-----------RKAKTVLEKAKGTLEAENADLAtelrsVNSSRQENDRR--------RKQAESQIA 1305
Cdd:COG3096 714 vPDLSAVKEQLAGLedcpedlylieGDPDSFDDSVFDAEELEDAVVV-----KLSDRQWRYSRfpevplfgRAAREKRLE 788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1306 ELQVKLAEIERARSEL---QEKCTKLQQEAEN-ITNQLE-------EAELKASAAvksasnmesQLTEAQQLLEEETRQK 1374
Cdd:COG3096 789 ELRAERDELAEQYAKAsfdVQKLQRLHQAFSQfVGGHLAvafapdpEAELAALRQ---------RRSELERELAQHRAQE 859
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1375 LGLSSKLRQIESEKEALQ------EQLEEDDEAKRNYErklaevttqmqeikkkAEEDADLAKELEEGKKRLNKDIEALE 1448
Cdd:COG3096 860 QQLRQQLDQLKEQLQLLNkllpqaNLLADETLADRLEE----------------LREELDAAQEAQAFIQQHGKALAQLE 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1449 RQVKELiaQNDRLdkSKKKIQSELEDATIELEAQRTKVLELEKKQKNFD--------KILAEEKAISEQIAQERDTAERE 1520
Cdd:COG3096 924 PLVAVL--QSDPE--QFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhfsyedavGLLGENSDLNEKLRARLEQAEEA 999
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1521 AREKETKVLSVSRELDEAFDKIEDL----ENKRKTLQNELDDLANTQGTADKNVHELEKAKRA-LESQLAELKAQNEELE 1595
Cdd:COG3096 1000 RREAREQLRQAQAQYSQYNQVLASLkssrDAKQQTLQELEQELEELGVQADAEAEERARIRRDeLHEELSQNRSRRSQLE 1079
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1596 DDLQLTEdaklrlevnmqalrsqferdllakeegAEekRRGLVKQLRDLETELDEERKQRTAAVAS 1661
Cdd:COG3096 1080 KQLTRCE---------------------------AE--MDSLQKRLRKAERDYKQEREQVVQAKAG 1116
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1050-1228 |
4.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1050 RANDLSQTLAEEEEKakhLAKLKAKH------------EATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNER 1117
Cdd:COG3206 183 QLPELRKELEEAEAA---LEEFRQKNglvdlseeakllLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1118 R--VQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQL-AEIQEDLEAEKAARAKAEKVRRDLSEELEAL 1194
Cdd:COG3206 260 LqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQL 339
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 62471805 1195 KNELldsLDTTAAQQELRS-KREQELA-----TLKKSLEE 1228
Cdd:COG3206 340 EARL---AELPELEAELRRlEREVEVArelyeSLLQRLEE 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1216-1632 |
5.34e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1216 EQELATLKKSLEEETvNHEGVLADMRHKHSQELNSINDQLE----------NLRKAKTVLEKAKGTLEA-ENADLATELR 1284
Cdd:PRK10246 215 PEQVQSLTASLQVLT-DEEKQLLTAQQQQQQSLNWLTRLDElqqeasrrqqALQQALAAEEKAQPQLAAlSLAQPARQLR 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1285 SVNSSRQENDRRRKQAESQIAELQVKLAEIERARSEL----QEKCTKLQQEAENITNQLEE--------AELKASAAVKS 1352
Cdd:PRK10246 294 PHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIrhhaAKQSAELQAQQQSLNTWLAEhdrfrqwnNELAGWRAQFS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1353 A-SNMESQLTEAQQLLEEETRQKLGL-----------SSKLRQIESEKEALQEQ---LEEDDEAKRNYERKLAEVTTQMQ 1417
Cdd:PRK10246 374 QqTSDREQLRQWQQQLTHAEQKLNALpaitltltadeVAAALAQHAEQRPLRQRlvaLHGQIVPQQKRLAQLQVAIQNVT 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1418 EIKKKAEEDADLAKELEEGKKRLNKDIEAL---ERQVKELIAQNDRLDKSKKkiqSELEDAT----------IELEAQRT 1484
Cdd:PRK10246 454 QEQTQRNAALNEMRQRYKEKTQQLADVKTIceqEARIKDLEAQRAQLQAGQP---CPLCGSTshpaveayqaLEPGVNQS 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1485 KVLELEKKQKNfdkiLAEE--------KAISEQIAQERDTAEREAREKETkvlsvsreLDEAFDKIEDLENKRKTLQNEL 1556
Cdd:PRK10246 531 RLDALEKEVKK----LGEEgaalrgqlDALTKQLQRDESEAQSLRQEEQA--------LTQQWQAVCASLNITLQPQDDI 598
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1557 DDLANTQGTADKNVHELEKaKRALESQLAELKAQNEELEDDLQLTEdaklrlevnmQALRSQFER-DLLAKEEGAEE 1632
Cdd:PRK10246 599 QPWLDAQEEHERQLRLLSQ-RHELQGQIAAHNQQIIQYQQQIEQRQ----------QQLLTALAGyALTLPQEDEEA 664
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1547-1898 |
5.86e-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: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1547 NKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTEDaklRLEVNMQALRSQ-----FER 1621
Cdd:COG3096 278 NERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASD---HLNLVQTALRQQekierYQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1622 DLLAKEEGAEEKrrglVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMhnkvkedalKHAKKLQ-AQVKDA 1700
Cdd:COG3096 355 DLEELTERLEEQ----EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDV---------QQTRAIQyQQAVQA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1701 LRDAeeakaakeelQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETeRDELAEEIANNankgslmIDEKRRLEAR 1780
Cdd:COG3096 422 LEKA----------RALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQ-KLSVADAARRQ-------FEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1781 IATLEEELEEEQSNSEVLLD-RSRKAQL-QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETaqrtkVKAT 1858
Cdd:COG3096 484 IAGEVERSQAWQTARELLRRyRSQQALAqRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEE-----LEEL 558
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 62471805 1859 IATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELT 1898
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELA 598
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1714-1874 |
6.40e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1714 LQALSKEAERKVKALEAEVLQLTEDLASSERARRA---------AETERDELAEEIANNANKGSLMIDEKRRLEARIATL 1784
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAAL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1785 EEELEEEQSNSEVLLDRSRKAQL--QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKVKATIATL 1862
Cdd:COG3206 246 RAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEAL 325
|
170
....*....|..
gi 62471805 1863 EAKIANLEEQLE 1874
Cdd:COG3206 326 QAREASLQAQLA 337
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1248-1608 |
6.61e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1248 LNSINDQLENLRKAKTV------LEKAKGTLEAENADLATELRSVNSSrqendrrrkqaeSQIAELQvklAEIERARSEL 1321
Cdd:PRK10929 54 LNWLEERKGSLERAKQYqqvidnFPKLSAELRQQLNNERDEPRSVPPN------------MSTDALE---QEILQVSSQL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1322 QEKCTKLQQEAEnitnqleeaelKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSS--------KLRQIESEKEALQE 1393
Cdd:PRK10929 119 LEKSRQAQQEQD-----------RAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTpntplaqaQLTALQAESAALKA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1394 QLEEDDEAK--RNYERKLAEVTTqmqEIKKKAEEDADLakELEEGKKRLN----KDIE-ALERqvKELIA-QNDRLDKSK 1465
Cdd:PRK10929 188 LVDELELAQlsANNRQELARLRS---ELAKKRSQQLDA--YLQALRNQLNsqrqREAErALES--TELLAeQSGDLPKSI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1466 KKiqseledatiELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQERDT--AEREarekETKVLSVSRELDEAF-DKI 1542
Cdd:PRK10929 261 VA----------QFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQAlnTLRE----QSQWLGVSNALGEALrAQV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1543 EDLENKRKTLQneLD--------------DLANTQGTADKNVHE----LEKA-KRALESQlaeLKAQNEELED-----DL 1598
Cdd:PRK10929 327 ARLPEMPKPQQ--LDtemaqlrvqrlryeDLLNKQPQLRQIRQAdgqpLTAEqNRILDAQ---LRTQRELLNSllsggDT 401
|
410
....*....|
gi 62471805 1599 QLTEDAKLRL 1608
Cdd:PRK10929 402 LILELTKLKV 411
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1360-1523 |
6.99e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1360 LTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERklaevttqmqEIKKKAEEDADLAKELEEGKKR 1439
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEK----------ELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1440 LNKDIEALERQVKELIAQNDRLDKSKKkiqseledatieleaqrtkvlELEKKQKNFDKILAEEKAISEQIAQErdTAEr 1519
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQQ---------------------ELEKKEEELEELIEEQLQELERISGL--TAE- 153
|
....
gi 62471805 1520 EARE 1523
Cdd:PRK12704 154 EAKE 157
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1297-1644 |
7.19e-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: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1297 RKQAESQIAELQVKLAEIERARSE-LQEKCTKLQQEAENITNQLEEAELKASAAVKSASNM---ESQLTEAQQLLEEETR 1372
Cdd:pfam09731 105 EKEATKDAAEAKAQLPKSEQEKEKaLEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSlkeASDTAEISREKATDSA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1373 QKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVK 1452
Cdd:pfam09731 185 LQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELV 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1453 ELI------------AQNDRLDKSKKKIQSELEDATIELEAQRTKV-----LELEKKQKNFDKILAE-----EKAISEQI 1510
Cdd:pfam09731 265 SIFpdiipvlkednlLSNDDLNSLIAHAHREIDQLSKKLAELKKREekhieRALEKQKEELDKLAEElsarlEEVRAADE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1511 AQERDTAEREaREKETKVL--SVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKnvheLEKAKRALESQLAELK 1588
Cdd:pfam09731 345 AQLRLEFERE-REEIRESYeeKLRTELERQAEAHEEHLKDVLVEQEIELQREFLQDIKEK----VEEERAGRLLKLNELL 419
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1589 AQNEELE---DDLQLTEDAKLR---LEVNMQALRSQFERdllakeEGAEEKRRGLVKQLRDL 1644
Cdd:pfam09731 420 ANLKGLEkatSSHSEVEDENRKaqqLWLAVEALRSTLED------GSADSRPRPLVRELKAL 475
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1358-1496 |
7.62e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1358 SQLTEAQQLLEEETRQKLGLSSKLRQIE---SEKEALQEQLEEDDEAKrnyERKLAEVTTQMQEIKKKAEEDADLAKELE 1434
Cdd:PRK09039 60 SQIAELADLLSLERQGNQDLQDSVANLRaslSAAEAERSRLQALLAEL---AGAGAAAEGRAGELAQELDSEKQVSARAL 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1435 EGKKRLNKDIEALERQvkeLIAQNDRLDKSKKKIQSelEDATIELEAQR------TKVLELEKKQKNF 1496
Cdd:PRK09039 137 AQVELLNQQIAALRRQ---LAALEAALDASEKRDRE--SQAKIADLGRRlnvalaQRVQELNRYRSEF 199
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1246-1677 |
7.80e-04 |
|
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: 44.29 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1246 QELNSINDQL----ENLRKAKTVLEKAKGTLEAENADL---ATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERAR 1318
Cdd:pfam05622 3 SEAQEEKDELaqrcHELDQQVSLLQEEKNSLQQENKKLqerLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1319 SELQEKC-------TKLQQEAENITNQLEEAE-LKASAAVKSASNMESQLTEAQQlleEETRQKLG-LSSKLRQI----E 1385
Cdd:pfam05622 83 DDYRIKCeelekevLELQHRNEELTSLAEEAQaLKDEMDILRESSDKVKKLEATV---ETYKKKLEdLGDLRRQVklleE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1386 SEKEALQEQLEEDDEAKR--NYERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRL-- 1461
Cdd:pfam05622 160 RNAEYMQRTLQLEEELKKanALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLre 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1462 -----------DKSKKKIQSELEDATIELEAQRTKVLELEKKQKnFDKILAEEKAISEQiaQERDTAEREAreketkvlS 1530
Cdd:pfam05622 240 tneelrcaqlqQAELSQADALLSPSSDPGDNLAAEIMPAEIREK-LIRLQHENKMLRLG--QEGSYRERLT--------E 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1531 VSRELDEAFDKIEDLENKRKT-------LQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQNEELEDDLQLTED 1603
Cdd:pfam05622 309 LQQLLEDANRRKNELETQNRLanqrileLQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEE 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 62471805 1604 AKLRLEVNMQALRSQFERDLLAKEE---GAEEKRRGLVKQLRDLETELDEerKQRTAAVASKKKLEGDLKEIETTME 1677
Cdd:pfam05622 389 LEPKQDSNLAQKIDELQEALRKKDEdmkAMEERYKKYVEKAKSVIKTLDP--KQNPASPPEIQALKNQLLEKDKKIE 463
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1185-1529 |
8.06e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1185 RDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETvnhegvladmrhkhsQELNSINDQLENLRKAKTV 1264
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---------------EQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1265 LEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAEL 1344
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1345 KASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAE 1424
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1425 EDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEK 1504
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
330 340
....*....|....*....|....*
gi 62471805 1505 AISEQIAQERDTAEREAREKETKVL 1529
Cdd:COG4372 346 LLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1433-1973 |
8.13e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1433 LEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIEL-----EAQRTKVLELEKKQKNFD--KILAEEKA 1505
Cdd:PRK01156 188 LEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYnnlksALNELSSLEDMKNRYESEikTAESDLSM 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1506 ISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNeLDDLANTQGTADKNVHELE----------K 1575
Cdd:PRK01156 268 ELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSN-IDAEINKYHAIIKKLSVLQkdyndyikkkS 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1576 AKRALESQLAELKAQNEELEDDLQLTEDAKLRLE---VNMQALRSQFERDLLAKEEGAEEkrrgLVKQLRDLETELDEER 1652
Cdd:PRK01156 347 RYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEeysKNIERMSAFISEILKIQEIDPDA----IKKELNEINVKLQDIS 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1653 KQRTAAVASKKKLEGDLKEIETTMEM---HNK-------VKEDALKHAKKLQAQVKDALRDAEeakaakeelqalsKEAE 1722
Cdd:PRK01156 423 SKVSSLNQRIRALRENLDELSRNMEMlngQSVcpvcgttLGEEKSNHIINHYNEKKSRLEEKI-------------REIE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1723 RKVKALEAEVLQLT---EDLASSERARRAAETERDELAEeiannANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLl 1799
Cdd:PRK01156 490 IEVKDIDEKIVDLKkrkEYLESEEINKSINEYNKIESAR-----ADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDL- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1800 DRSRKAQLQIEQLTTELANEKSNSQKNEngralLERQNKELKAKLAEIETaQRTKVKATIATLEAKIANLEEQLENEGKE 1879
Cdd:PRK01156 564 DSKRTSWLNALAVISLIDIETNRSRSNE-----IKKQLNDLESRLQEIEI-GFPDDKSYIDKSIREIENEANNLNNKYNE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1880 RLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEqmdkLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQEA 1959
Cdd:PRK01156 638 IQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE----ITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINE 713
|
570
....*....|....
gi 62471805 1960 MNREINSLKTKLRR 1973
Cdd:PRK01156 714 LSDRINDINETLES 727
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1298-1543 |
8.41e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1298 KQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITN--QLEEAEL-KASAAVKSASnmeSQLTEAQQLLEEETRQK 1374
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRriQLLEEELeRTEERLAEAL---EKLEEAEKAADESERGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1375 LGLSSKLRQIESEKEALQEQLEE----DDEAKRNYE---RKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEAL 1447
Cdd:pfam00261 81 KVLENRALKDEEKMEILEAQLKEakeiAEEADRKYEevaRKLVVVEGDLERAEERAELAESKIVELEEELKVVGNNLKSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1448 ERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKkqknfdkilaeekaiseqiaqERDTAEREAREKETK 1527
Cdd:pfam00261 161 EASEEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEK---------------------EVDRLEDELEAEKEK 219
|
250
....*....|....*.
gi 62471805 1528 VLSVSRELDEAFDKIE 1543
Cdd:pfam00261 220 YKAISEELDQTLAELN 235
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1352-1540 |
9.40e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.74 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1352 SASNMESQLTEAQQLLEEEtrqklglsskLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE-----D 1426
Cdd:pfam04012 12 NIHEGLDKAEDPEKMLEQA----------IRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAaltkgN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1427 ADLAKELEEGKKRLNKDIEALERQVKEliaQNDRLDKSKKKIQsELEDATIELEAQRTKVLELEKKQKNFDKI------L 1500
Cdd:pfam04012 82 EELAREALAEKKSLEKQAEALETQLAQ---QRSAVEQLRKQLA-ALETKIQQLKAKKNLLKARLKAAKAQEAVqtslgsL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 62471805 1501 AEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFD 1540
Cdd:pfam04012 158 STSSATDSFERIEEKIEEREARADAAAELASAVDLDAKLE 197
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1699-1973 |
9.62e-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: 44.44 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1699 DALRDAEEAKAAKEELQALSKEaerkVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKR-RL 1777
Cdd:pfam12128 231 QAIAGIMKIRPEFTKLQQEFNT----LESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRdEL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1778 EARIATLEEELEEEQSNSEVLLDRSRK-AQLQIEQLTTELANEKSNSQKNENgralLERQNKELKAKLAEIETAQRTKVK 1856
Cdd:pfam12128 307 NGELSAADAAVAKDRSELEALEDQHGAfLDADIETAAADQEQLPSWQSELEN----LEERLKALTGKHQDVTAKYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1857 ATIATLEAKIANLEEQLENEGKERLLQQKANRK-MDKKIKELTMNIEDERRHVdqhKEQMDKLNSRIKLLKRNLDETEEE 1935
Cdd:pfam12128 383 KIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDdLQALESELREQLEAGKLEF---NEEEYRLKSRLGELKLRLNQATAT 459
|
250 260 270
....*....|....*....|....*....|....*...
gi 62471805 1936 lQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKLRR 1973
Cdd:pfam12128 460 -PELLLQLENFDERIERAREEQEAANAEVERLQSELRQ 496
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
1297-1494 |
1.19e-03 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 43.67 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1297 RKQaESQIAELQVKLAEIERARSELQEKCTKlQQEAENITNQLEE-----------AELKASAAVKSASNMESQLTEAQQ 1365
Cdd:pfam15066 328 RKQ-QMQIQDLQCSNLYLEKKVKELQMKITK-QQVFVDIINKLKEnveeliedkynVILEKNDINKTLQNLQEILANTQK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1366 LLEEetrqklglsSKLrqiesEKEALQEQLEeddEAKRNYERKLAEVTTQMQEIKKKA----EEDADLAKElEEGKKRLN 1441
Cdd:pfam15066 406 HLQE---------SRK-----EKETLQLELK---KIKVNYVHLQERYITEMQQKNKSVsqclEMDKTLSKK-EEEVERLQ 467
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 1442 KDIEALERqvkeliAQNDRLD--KSKKKIQsELEDATIELEAQRTKVLELEKKQK 1494
Cdd:pfam15066 468 QLKGELEK------ATTSALDllKREKETR-EQEFLSLQEEFQKHEKENLEERQK 515
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1287-1457 |
1.20e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1287 NSSRQENDRRRKQAESQIaELQVKL--AEIERARSELqekctkLQQEAENitnqleeAELKASAAVKSASNMESqltEAQ 1364
Cdd:PTZ00491 666 AAARHQAELLEQEARGRL-ERQKMHdkAKAEEQRTKL------LELQAES-------AAVESSGQSRAEALAEA---EAR 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1365 QLLEEETRQKLGLSSKLRQIEseKEALQEQLEEDDEAKRNYERKLAEVttqmqEIKKkaeedadlAKELEEGK-KRLNKD 1443
Cdd:PTZ00491 729 LIEAEAEVEQAELRAKALRIE--AEAELEKLRKRQELELEYEQAQNEL-----EIAK--------AKELADIEaTKFERI 793
|
170
....*....|....
gi 62471805 1444 IEALERQVKELIAQ 1457
Cdd:PTZ00491 794 VEALGRETLIAIAR 807
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1432-1797 |
1.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1432 ELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILaeekaisEQIA 1511
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL-------EELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1512 QERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKAQN 1591
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1592 EELEDDLQLTEDAKLRLEVNMqalrsqferdLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVASKKKLEGDLKE 1671
Cdd:COG4372 167 AALEQELQALSEAEAEQALDE----------LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1672 IETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAET 1751
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDA 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 62471805 1752 ERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEV 1797
Cdd:COG4372 317 LLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKG 362
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1094-1275 |
1.34e-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: 42.60 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1094 QESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEdleae 1173
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1174 kaarakaekvrrdlSEELEALKNElldsLDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSIND 1253
Cdd:COG1579 88 --------------NKEYEALQKE----IESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|..
gi 62471805 1254 QLENLRKAKTVLEKAKGTLEAE 1275
Cdd:COG1579 150 ELAELEAELEELEAEREELAAK 171
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1357-1601 |
1.40e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.32 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1436
Cdd:pfam00261 7 KEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESERGRKVLENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1437 KKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAqrtkvlelekkqknfdkilAEEKAiseqiaqerDT 1516
Cdd:pfam00261 87 ALKDEEKMEILEAQLKEAKEIAEEADRKYEEVARKLVVVEGDLER-------------------AEERA---------EL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1517 AEREAREKETKVLSVSREL-------DEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAKRALESQLAELKA 1589
Cdd:pfam00261 139 AESKIVELEEELKVVGNNLksleaseEKASEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRLEDELEAEKE 218
|
250
....*....|..
gi 62471805 1590 QNEELEDDLQLT 1601
Cdd:pfam00261 219 KYKAISEELDQT 230
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1279-1524 |
1.60e-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: 42.88 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1279 LATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENIT--NQLEEAELKASAAVKSASNM 1356
Cdd:pfam15905 78 LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTrvNELLKAKFSEDGTQKKMSSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1357 ESQLTEAQQLLEEETRQklgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEEG 1436
Cdd:pfam15905 158 SMELMKLRNKLEAKMKE---VMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCV 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1437 KKRLNKDIEALeRQVKELIAQNDRLDKSkkkIQSELEDATIELEAQ------RTKVLELEKKQK-NFDKILAEEKAISEQ 1509
Cdd:pfam15905 235 SEQVEKYKLDI-AQLEELLKEKNDEIES---LKQSLEEKEQELSKQikdlneKCKLLESEKEELlREYEEKEQTLNAELE 310
|
250
....*....|....*
gi 62471805 1510 IAQERDTAEREAREK 1524
Cdd:pfam15905 311 ELKEKLTLEEQEHQK 325
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1488-1880 |
1.75e-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: 43.35 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1488 ELEKKQKNFDKILAEEKaisEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDdlantqgtad 1567
Cdd:pfam07888 45 ELLQAQEAANRQREKEK---ERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE---------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1568 knvhELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKrrglvkqlRDLETE 1647
Cdd:pfam07888 112 ----ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAER--------KQLQAK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1648 LDEERKQRTAAVASKKKLEGDLKEIET-TMEMHNKVKEDALKHAkklQAQVKDAlrDAEEAKAAKEELQALSKEAERKVK 1726
Cdd:pfam07888 180 LQQTEEELRSLSKEFQELRNSLAQRDTqVLQLQDTITTLTQKLT---TAHRKEA--ENEALLEELRSLQERLNASERKVE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1727 ALEAEVLQLtedlaSSERARRAAETERDEL-AEEIANNANKGSLMIDEKRrleariATLEEELEEEQSNSEVLLDRSRKA 1805
Cdd:pfam07888 255 GLGEELSSM-----AAQRDRTQAELHQARLqAAQLTLQLADASLALREGR------ARWAQERETLQQSAEADKDRIEKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1806 QLQIEQLTTELANEKSNSQKNE--------NGRALLERQNKELKAKLAEIETAQRTK--VKATIATLEAKIANLEEQLEN 1875
Cdd:pfam07888 324 SAELQRLEERLQEERMEREKLEvelgrekdCNRVQLSESRRELQELKASLRVAQKEKeqLQAEKQELLEYIRQLEQRLET 403
|
....*
gi 62471805 1876 EGKER 1880
Cdd:pfam07888 404 VADAK 408
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1190-1575 |
1.81e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1190 ELEALKNELLDSLDTTAAQ-QELRSKREQELATLKKSLEEETVNHEgvladmrhKHSQELNSINDQLENLRKAKTVLEKA 1268
Cdd:PTZ00440 1081 LLEEKVEALLKKIDENKNKlIEIKNKSHEHVVNADKEKNKQTEHYN--------KKKKSLEKIYKQMEKTLKELENMNLE 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1269 KGTL-EAENADLATELRSVNSSRQendrrrkQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAELKAS 1347
Cdd:PTZ00440 1153 DITLnEVNEIEIEYERILIDHIVE-------QINNEAKKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAYYDK 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1348 AAVKSAsNMESQLTEAQQLLEEETRqklglSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTT-----QMQEIKKK 1422
Cdd:PTZ00440 1226 ATASYE-NIEELTTEAKGLKGEANR-----STNVDELKEIKLQVFSYLQQVIKENNKMENALHEIKNmyeflISIDSEKI 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1423 AEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQRTKVL--ELEKKQKNFDKIL 1500
Cdd:PTZ00440 1300 LKEILNSTKKAEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLEDKQIDDEIKKIEQIkeEISNKRKEINKYL 1379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1501 AEEKAISEQIAQERDTAEREARE----KETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEK 1575
Cdd:PTZ00440 1380 SNIKSNKEKCDLHVRNASRGKDKidflNKHEAIEPSNSKEVNIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEK 1458
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1411-1753 |
2.00e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1411 EVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLdkskKKIQSELEDATIELEAQRTKVLELE 1490
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL----EELNEQLQAAQAELAQAQEELESLQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1491 KKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNV 1570
Cdd:COG4372 108 EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1571 HELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDE 1650
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1651 ERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEA 1730
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLL 347
|
330 340
....*....|....*....|...
gi 62471805 1731 EVLQLTEDLASSERARRAAETER 1753
Cdd:COG4372 348 VGLLDNDVLELLSKGAEAGVADG 370
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
883-1275 |
2.13e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 883 KVKPLLEVTKQEEKLVQKEDELKQVREKLDTLAKNTQEYERKYQQALVEKTTLAEQLQAEIELCAEAEESRSRLMARKQE 962
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV 1635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 963 LEDMMQELEtrieeeeervlalggEKKKLElniqdleeqleeeeaarqklQLEKVQLDAKIKKYEEDLALTDDQNQKLLK 1042
Cdd:PTZ00121 1636 EQLKKKEAE---------------EKKKAE--------------------ELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1043 EKKLLEERANdlSQTLAEEEEKAKHLAKLKAKHEATISELEERLHKDQQQRQESDRSKRKIETEvadlKEQLNERRVQVD 1122
Cdd:PTZ00121 1681 KKAEEDEKKA--AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED----KKKAEEAKKDEE 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1123 EMQ--AQLAKREEELTQTLLRIDE---ESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNE 1197
Cdd:PTZ00121 1755 EKKkiAHLKKEEEKKAEEIRKEKEaviEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKE 1834
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62471805 1198 LLDSLDTtaaqQELRSKREQELATLKKSLEEETVNHEGvladmrhKHSQELNSINDQLENLRKAKTVLEKAKGTLEAE 1275
Cdd:PTZ00121 1835 VADSKNM----QLEEADAFEKHKFNKNNENGEDGNKEA-------DFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1266-1418 |
2.14e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.02 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1266 EKAKGTLEAENADLATELRsVNSSRQENDRRRKQAESQIAELQVKLAEiERARSELQEKCTKLQQEAENitNQLEEAElK 1345
Cdd:pfam15709 372 EKMREELELEQQRRFEEIR-LRKQRLEEERQRQEEEERKQRLQLQAAQ-ERARQQQEEFRRKLQELQRK--KQQEEAE-R 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62471805 1346 ASAAVKSASNMESQLTEAQQLLEEETRQKLgLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQE 1418
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLMEMAEEER-LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQE 518
|
|
| rad2 |
TIGR00600 |
DNA excision repair protein (rad2); All proteins in this family for which functions are known ... |
1467-1597 |
2.52e-03 |
|
DNA excision repair protein (rad2); All proteins in this family for which functions are known are flap endonucleases that generate the 3' incision next to DNA damage as part of nucleotide excision repair. This family is related to many other flap endonuclease families including the fen1 family. 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: 273166 [Multi-domain] Cd Length: 1034 Bit Score: 42.96 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1467 KIQSELEDATIELEAqrtkVLELEKKQknfdkilAEEKAISEQIAQERDTAEREAREKETKVLSVSRELDEafDKIEDLE 1546
Cdd:TIGR00600 651 KEESESDGSFIEVDS----VSSTLELQ-------VPSKSQPTDESEENAENKVASIEGEHRKEIEDLLFDE--SEEDNIV 717
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1547 NKRKTlQNELDDLANTqgTADKNVHELEKAKRALESQLAELKAQNEELEDD 1597
Cdd:TIGR00600 718 GMIEE-EKDADDFKNE--WQDISLEELEALEANLLAEQNSLKAQKQQQKRI 765
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
937-1485 |
2.55e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.81 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 937 EQLQAEIELCAEAEESRSRLMARKQELE---DMMQELETRIEEEEER-VLALGGEKKKLELNIQDLEEQLEEEEAARQKL 1012
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDresDRNQELQKRIRLLEKReAEAEEALREQAELNRLKKKYLEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1013 QL-------------EKVQLDAKIKKYEEDLALTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKAKHLaklkAKHEATI 1079
Cdd:pfam05557 97 SQladarevisclknELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSL----AEAEQRI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1080 SELEERLHKDQQQRQESDRSKRKIET--EVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQR 1157
Cdd:pfam05557 173 KELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLEL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1158 ELESQLAEIQEdLEAEKAARAKAEKVRRDLSEELEALKN-ELLDSLDTTAAQQELRSKR------EQELATLKKSLEEET 1230
Cdd:pfam05557 253 EKEKLEQELQS-WVKLAQDTGLNLRSPEDLSRRIEQLQQrEIVLKEENSSLTSSARQLEkarrelEQELAQYLKKIEDLN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1231 VNHEgvladmRHKhsqelnsinDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENdRRRKQAESQIAELQVK 1310
Cdd:pfam05557 332 KKLK------RHK---------ALVRRLQRRVLLLTKERDGYRAILESYDKELTMSNYSPQLL-ERIEEAEDMTQKMQAH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1311 LAEIERARSELQEKCTKLQQEAEniTNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEa 1390
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQ--TLERELQALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELE- 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1391 lQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQS 1470
Cdd:pfam05557 473 -RRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEK-LQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRK 550
|
570
....*....|....*
gi 62471805 1471 ELEDAtiELEAQRTK 1485
Cdd:pfam05557 551 ELESA--ELKNQRLK 563
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1303-1527 |
2.89e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1303 QIAELQVKLAeierarSELQEKCTKLQQEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKL-----GL 1377
Cdd:PRK05771 32 HIEDLKEELS------NERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIekeikEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1378 SSKLRQIESEKEALQEQLEE---------DDEAKRNYERKLAEVTTQMQEIKKKAEEDADLAKELEE------------G 1436
Cdd:PRK05771 106 EEEISELENEIKELEQEIERlepwgnfdlDLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvvvV 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1437 KKRLNKDIEAL-------------ERQVKELIAQndrLDKSKKKIQSELEDATIELEaqrtkvlelEKKQKNFDKILAEE 1503
Cdd:PRK05771 186 LKELSDEVEEElkklgferleleeEGTPSELIRE---IKEELEEIEKERESLLEELK---------ELAKKYLEELLALY 253
|
250 260
....*....|....*....|....
gi 62471805 1504 kaisEQIAQERDTAEREAREKETK 1527
Cdd:PRK05771 254 ----EYLEIELERAEALSKFLKTD 273
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1273-1525 |
2.93e-03 |
|
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: 42.71 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1273 EAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIE----RARSELQEKCTKLQQEAENITNQLEEAELKASA 1348
Cdd:pfam05667 225 EWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATsgasRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1349 AV---KSASNMESQLTEAQQllEEETRQKlglssklrQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEE 1425
Cdd:pfam05667 305 KLqftNEAPAATSSPPTKVE--TEEELQQ--------QREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1426 DADLAKELEEGKKRLNKDIEAL---ERQVKELIAQNDRLDKSKKKIQSELEDATIEL--------EAQRTKVLELEKKqk 1494
Cdd:pfam05667 375 LKEQNEELEKQYKVKKKTLDLLpdaEENIAKLQALVDASAQRLVELAGQWEKHRVPLieeyralkEAKSNKEDESQRK-- 452
|
250 260 270
....*....|....*....|....*....|.
gi 62471805 1495 nfdkiLAEEKAISEQIaqeRDTAErEAREKE 1525
Cdd:pfam05667 453 -----LEEIKELREKI---KEVAE-EAKQKE 474
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1081-1475 |
2.93e-03 |
|
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: 42.37 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1081 ELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQA------QLAKREEELTQTLLRIdeESATKATAQK 1154
Cdd:pfam05622 11 ELAQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPggkkylLLQKQLEQLQEENFRL--ETARDDYRIK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1155 AQrELESQLAEIQ---EDLEAekaarakaekvrrdLSEELEALKNELlDSLDTTAaqqELRSKREQELATLKKSLEEetv 1231
Cdd:pfam05622 89 CE-ELEKEVLELQhrnEELTS--------------LAEEAQALKDEM-DILRESS---DKVKKLEATVETYKKKLED--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1232 nhegvladmrhkhsqelnsindqLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQaesqIAELQVKL 1311
Cdd:pfam05622 147 -----------------------LGDLRRQVKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQ----VQELHGKL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1312 AEiERARSE--------LQEKCTKLQQEAENI---------TN------QLEEAELKASAAV--KSASNMESQLTEAQQL 1366
Cdd:pfam05622 200 SE-ESKKADklefeykkLEEKLEALQKEKERLiierdtlreTNeelrcaQLQQAELSQADALlsPSSDPGDNLAAEIMPA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1367 LEEETRQKLGLSSK---LRQIESEKE---ALQEQLEEDDEAKRNYE--------------RKLAEVTTQMQEIKKKAEED 1426
Cdd:pfam05622 279 EIREKLIRLQHENKmlrLGQEGSYRErltELQQLLEDANRRKNELEtqnrlanqrilelqQQVEELQKALQEQGSKAEDS 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 62471805 1427 ADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDA 1475
Cdd:pfam05622 359 SLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEA 407
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1088-1404 |
3.05e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 42.53 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1088 KDQQQRQESDRSK-RKIETEVADLKEQLNERRvqvdemQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEI 1166
Cdd:PLN03229 418 KVNMKKREAVKTPvRELEGEVEKLKEQILKAK------ESSSKPSELALNEMIEKLKKEIDLEYTEAVIAMGLQERLENL 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1167 QEDLEAEKAARAKaekVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQ-ELATLKKSLEEETVNHEGVLADMRHK-- 1243
Cdd:PLN03229 492 REEFSKANSQDQL---MHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDMlNEFSRAKALSEKKSKAEKLKAEINKKfk 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1244 -------------------HSQELNSINDQLENLRKAktvLEKAKGTLEAEnadLATELRSVNSSRQENDRRRKQAESQI 1304
Cdd:PLN03229 569 evmdrpeikekmealkaevASSGASSGDELDDDLKEK---VEKMKKEIELE---LAGVLKSMGLEVIGVTKKNKDTAEQT 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1305 AELQVKlAEIERARSELQEKCTKLQQEAEnITNQLEEAELKASAAVKSASNMESQLTEAqqlLEEETRQKL-------GL 1377
Cdd:PLN03229 643 PPPNLQ-EKIESLNEEINKKIERVIRSSD-LKSKIELLKLEVAKASKTPDVTEKEKIEA---LEQQIKQKIaealnssEL 717
|
330 340
....*....|....*....|....*..
gi 62471805 1378 SSKLRQIESEKEALQEQLEEDDEAKRN 1404
Cdd:PLN03229 718 KEKFEELEAELAAARETAAESNGSLKN 744
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1245-1467 |
3.08e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1245 SQELNSINDQLEnlrkaktVLEKAKGTLEAENADLATELRSVNSSRQENDrrrKQAESQIAELQVKLAEIERARSELQEK 1324
Cdd:PHA02562 187 DMKIDHIQQQIK-------TYNKNIEEQRKKNGENIARKQNKYDELVEEA---KTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1325 CTKLQQEAENITNQLE----EAELKASAAVKSASNmeSQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDE 1400
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqfqkVIKMYEKGGVCPTCT--QQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNE 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1401 AKRNY---ERKLAEVTTQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIaqNDRLDKSKKK 1467
Cdd:PHA02562 335 QSKKLlelKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV--KTKSELVKEK 402
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1272-1620 |
3.08e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1272 LEAENADLATELRSvnsSRQENDRRRKQA----ESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLE-EAELKA 1346
Cdd:pfam00038 23 LEQQNKLLETKISE---LRQKKGAEPSRLyslyEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEdELNLRT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1347 SAavksasnmESQLTEAQQLLEEETRQKLGLSSKLrqiesekEALQEQLEEddeAKRNYERKLAEVTTQMQEIKKKAEED 1426
Cdd:pfam00038 100 SA--------ENDLVGLRKDLDEATLARVDLEAKI-------ESLKEELAF---LKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1427 A----DLAKELEEgkkrlnkdieaLERQVKELIAQNdrLDKSKKKIQSELEDATIELEaqrtkvlelekkqKNFDKIlae 1502
Cdd:pfam00038 162 AarklDLTSALAE-----------IRAQYEEIAAKN--REEAEEWYQSKLEELQQAAA-------------RNGDAL--- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1503 eKAISEQIAQERDTAEREAREketkvlsvsreldeafdkIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAkraLES 1582
Cdd:pfam00038 213 -RSAKEEITELRRTIQSLEIE------------------LQSLKKQKASLERQLAETEERYELQLADYQELISE---LEA 270
|
330 340 350
....*....|....*....|....*....|....*...
gi 62471805 1583 QLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFE 1620
Cdd:pfam00038 271 ELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLE 308
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1431-1560 |
3.23e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 42.36 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1431 KELEEGKKRLNKdiealeRQVKELIAQNDRLDKSKKKIQSELEdatiELEAQRtkvlelekkqknfdkilaeeKAISEQI 1510
Cdd:PRK05431 9 ENPEAVKEALAK------RGFPLDVDELLELDEERRELQTELE----ELQAER--------------------NALSKEI 58
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1511 AQERDTAER-EAREKETKVLSvsreldeafDKIEDLENKRKTLQNELDDLA 1560
Cdd:PRK05431 59 GQAKRKGEDaEALIAEVKELK---------EEIKALEAELDELEAELEELL 100
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1572-1698 |
3.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1572 ELEKAKRALESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQLRDLETELDEE 1651
Cdd:PRK00409 517 KLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 62471805 1652 RKQRTAAVASKkklegDLKEIETTMEMHNKVKEDALKHAKKLQAQVK 1698
Cdd:PRK00409 597 QKGGYASVKAH-----ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1581-1831 |
3.44e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1581 ESQLAELKAQNEELEDDLQLTEDAKLRLEVNMQALRSQFErDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVA 1660
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN-ELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1661 SKKKLEGDLKEIETTMEMHNKvkEDALKHA---KKLQAQVKDALRDaeeakaakeeLQALSKEAERKVKALEAEVLQLTE 1737
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESF--SDFLDRLsalSKIADADADLLEE----------LKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1738 DLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVLLDRSRKAQLQIEQLTTELA 1817
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250
....*....|....
gi 62471805 1818 NEKSNSQKNENGRA 1831
Cdd:COG3883 242 AAASAAGAGAAGAA 255
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1543-1694 |
3.75e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1543 EDLENKRKTLQNELDDLANT----QGTADKNVHELEKAKRALESQLAELKAQNEELEDdlQLTEDAKLRLEVNMQALRSQ 1618
Cdd:cd22656 110 EELEEAKKTIKALLDDLLKEakkyQDKAAKVVDKLTDFENQTEKDQTALETLEKALKD--LLTDEGGAIARKEIKDLQKE 187
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62471805 1619 FERDLlaKEEGAEEKRRglVKQLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEmhnkvkeDALKHAKKLQ 1694
Cdd:cd22656 188 LEKLN--EEYAAKLKAK--IDELKALIADDEAKLAAALRLIADLTAADTDLDNLLALIG-------PAIPALEKLQ 252
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
879-1203 |
3.80e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 879 RLYTKVKPLLEVTKQEEKLVQKEDELK----------QVREKLDTLAKNTQEYERKYQQalVEKTTLAEQLQAEIELCAE 948
Cdd:PTZ00121 1593 RIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelkkaeEEKKKVEQLKKKEAEEKKKAEE--LKKAEEENKIKAAEEAKKA 1670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 949 AEESRSRLMARKQELEDMMQELETRIEEEeervlalggEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEE 1028
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALKKEAE---------EAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEE 1741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1029 DlaltddqnQKLLKEKKLLEERANDLSQTLAEEEEKAKHLAKLKakhEATISelEERLHKDQQQRQESDRSKRKIETEVA 1108
Cdd:PTZ00121 1742 D--------KKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIE--EELDEEDEKRRMEVDKKIKDIFDNFA 1808
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1109 DLKEQLNERRVQVDEmqaqlaKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLS 1188
Cdd:PTZ00121 1809 NIIEGGKEGNLVIND------SKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
330
....*....|....*
gi 62471805 1189 EELEALKNELLDSLD 1203
Cdd:PTZ00121 1883 EIEEADEIEKIDKDD 1897
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1533-1604 |
4.04e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 41.98 E-value: 4.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 1533 RELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELEKAK---RALESQLAELKAQNEELEDDLQLTEDA 1604
Cdd:PRK05431 21 RGFPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGedaEALIAEVKELKEEIKALEAELDELEAE 95
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1331-1533 |
4.13e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.67 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1331 EAENITNQLEEAELKASAAVKSASNMESQLTEAQQllEEETRQKLGLSSKLRQIESEKEALQEQLEeddeakrNYERKLA 1410
Cdd:pfam09787 1 NLESAKQELADYKQKAARILQSKEKLIASLKEGSG--VEGLDSSTALTLELEELRQERDLLREEIQ-------KLRGQIQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1411 EVTTQMQEIKKKAEEDAD-------LAKELEEGKKRLNKDIEA-LERQVKELIAQNDRLDKSKKKIQSELEDATIELEAQ 1482
Cdd:pfam09787 72 QLRTELQELEAQQQEEAEssreqlqELEEQLATERSARREAEAeLERLQEELRYLEEELRRSKATLQSRIKDREAEIEKL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1483 RTKVLELEKKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSVSR 1533
Cdd:pfam09787 152 RNQLTSKSQSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLER 202
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1189-1599 |
4.42e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1189 EELEALKNELLDsLDTTAAQQELRSKR-----EQELATLKKSLEEETVNHegvLADMrhkhSQELNSINDQLE--NLRKA 1261
Cdd:pfam06160 13 DELEERKNELMN-LPVQEELSKVKKLNltgetQEKFEEWRKKWDDIVTKS---LPDI----EELLFEAEELNDkyRFKKA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1262 KTVLEKAkgtleaeNADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEE 1341
Cdd:pfam06160 85 KKALDEI-------EELLDDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRKTLLANRFSYGPAIDELEKQLAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1342 AELKASAAVksasnmesQLTEAQQLLEEETrqklglssKLRQIESEKEALQEQLEE----DDEAKRNYERKLAEVTTQMQ 1417
Cdd:pfam06160 158 IEEEFSQFE--------ELTESGDYLEARE--------VLEKLEEETDALEELMEDipplYEELKTELPDQLEELKEGYR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1418 EIKKK--AEEDADLAKELEEGKKRLNKDIEALER-QVKELIAQNDRLDKSKKKIQSELEDatiELEAQRtkvlELEKKQK 1494
Cdd:pfam06160 222 EMEEEgyALEHLNVDKEIQQLEEQLEENLALLENlELDEAEEALEEIEERIDQLYDLLEK---EVDAKK----YVEKNLP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1495 NFdkilaeEKAISEQIAQERDTAEREAREKETKVLSvsrelDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELE 1574
Cdd:pfam06160 295 EI------EDYLEHAEEQNKELKEELERVQQSYTLN-----ENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQ 363
|
410 420
....*....|....*....|....*
gi 62471805 1575 KAKRALESQLAELKAQNEELEDDLQ 1599
Cdd:pfam06160 364 EELEEILEQLEEIEEEQEEFKESLQ 388
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1340-1528 |
4.53e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 41.78 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1340 EEAELKASAAVKSASNMESQLT-EAQQLLEEETRQklglSSKLRqieseKEALqeqLEEDDEAKRNYERKLAEVTTQMQE 1418
Cdd:PRK00106 31 EAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRE----SKALK-----KELL---LEAKEEARKYREEIEQEFKSERQE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1419 IKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELEaqrtKVLELEKKQKNfDK 1498
Cdd:PRK00106 99 LKQIESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELE----RVAALSQAEAR-EI 173
|
170 180 190
....*....|....*....|....*....|.
gi 62471805 1499 ILAE-EKAISEQIAQERDTAEREAREKETKV 1528
Cdd:PRK00106 174 ILAEtENKLTHEIATRIREAEREVKDRSDKM 204
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1202-1504 |
4.61e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 41.78 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1202 LDTTAAQQELRSKREQELATLKKSLEEETVNHEGVLADMRHKHSQELNSI---NDQLENLRKAKTVLEKAKGTLEAENAD 1278
Cdd:pfam02029 65 LDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSwekEEKRDSRLGRYKEEETEIREKEYQENK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1279 LATELRSVNSSRQENDRRRKQAESQ----IAELQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE-----LKASAA 1349
Cdd:pfam02029 145 WSTEVRQAEEEGEEEEDKSEEAEEVptenFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEeevtkLKVTTK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1350 VKSASNMESQLTEAQQLLEEETRQKLGlssKLRQIESEKEalqeqlEEDDEAKRnyeRKLAEVTTQMQEIKKKAEEDADL 1429
Cdd:pfam02029 225 RRQGGLSQSQEREEEAEVFLEAEQKLE---ELRRRRQEKE------SEEFEKLR---QKQQEAELELEELKKKREERRKL 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62471805 1430 AKELEEGKKRlnkdiEALERQVKEliaqndrlDKSKKKIQSELEdatieleaqRTKVLELEKKQKNFDKILAEEK 1504
Cdd:pfam02029 293 LEEEEQRRKQ-----EEAERKLRE--------EEEKRRMKEEIE---------RRRAEAAEKRQKLPEDSSSEGK 345
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1579-1760 |
4.92e-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: 40.68 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1579 ALESQLAELKAQNEELEDDLQltedaklRLEVNMQALRSQFERdllakeegAEEKRRGLVKQLRDLETELDEERKQRtaa 1658
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELA-------ELEDELAALEARLEA--------AKTELEDLEKEIKRLELEIEEVEARI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1659 vaskKKLEGDLKEIETTMEMHNKVKEdaLKHAKKLQAQVKDALRDAEEAK-AAKEELQALSKEAERKVKALEAEVLQLTE 1737
Cdd:COG1579 76 ----KKYEEQLGNVRNNKEYEALQKE--IESLKRRISDLEDEILELMERIeELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|...
gi 62471805 1738 DLASSERARRAAETERDELAEEI 1760
Cdd:COG1579 150 ELAELEAELEELEAEREELAAKI 172
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
892-1251 |
5.08e-03 |
|
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: 42.05 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 892 KQEEKLVQKEDELKQVREKLDT--LAKNTQEYERKYQQALVEKTTLAEQLQAeieLCAEAEESRSRLMA--RKQELE--D 965
Cdd:pfam07111 255 QEDRADLQATVELLQVRVQSLThmLALQEEELTRKIQPSDSLEPEFPKKCRS---LLNRWREKVFALMVqlKAQDLEhrD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 966 MMQELETRIEEEEERVLALGGEKKKLELNIQDLEEQLEEEEAARQKLQLEKVQLDAKIKKYEEDLALTDDQNQKLLKEKK 1045
Cdd:pfam07111 332 SVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMS 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1046 LLEERandLSQTLAEEEEKAKHLAKLK------AKHEATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRV 1119
Cdd:pfam07111 412 STQIW---LETTMTRVEQAVARIPSLSnrlsyaVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1120 QVDEMQAQLAKREEELTQTLLRIDEE-SATKATAQKAQRELESQLAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNEL 1198
Cdd:pfam07111 489 ERNRLDAELQLSAHLIQQEVGRAREQgEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL 568
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 62471805 1199 ldsldttAAQQELRSKREQE-LATLKKSLEEETVNHEGVLADMRHKHSQELNSI 1251
Cdd:pfam07111 569 -------TQQQEIYGQALQEkVAEVETRLREQLSDTKRRLNEARREQAKAVVSL 615
|
|
| ATG14 |
pfam10186 |
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are ... |
1010-1165 |
5.11e-03 |
|
Vacuolar sorting 38 and autophagy-related subunit 14; The Atg14 or Apg14 proteins are hydrophilic proteins with a predicted molecular mass of 40.5 kDa, and have a coiled-coil motif at the N terminus region. Yeast cells with mutant Atg14 are defective not only in autophagy but also in sorting of carboxypeptidase Y (CPY), a vacuolar-soluble hydrolase, to the vacuole. Subcellular fractionation indicate that Apg14p and Apg6p are peripherally associated with a membrane structure(s). Apg14p was co-immunoprecipitated with Apg6p, suggesting that they form a stable protein complex. These results imply that Apg6/Vps30p has two distinct functions: in the autophagic process and in the vacuolar protein sorting pathway. Apg14p may be a component specifically required for the function of Apg6/Vps30p through the autophagic pathway. There are 17 auto-phagosomal component proteins which are categorized into six functional units, one of which is the AS-PI3K complex (Vps30/Atg6 and Atg14). The AS-PI3K complex and the Atg2-Atg18 complex are essential for nucleation, and the specific function of the AS-PI3K apparently is to produce phosphatidylinositol 3-phosphate (PtdIns(3)P) at the pre-autophagosomal structure (PAS). The localization of this complex at the PAS is controlled by Atg14. Autophagy mediates the cellular response to nutrient deprivation, protein aggregation, and pathogen invasion in humans, and malfunction of autophagy has been implicated in multiple human diseases including cancer. This effect seems to be mediated through direct interaction of the human Atg14 with Beclin 1 in the human phosphatidylinositol 3-kinase class III complex.
Pssm-ID: 462986 [Multi-domain] Cd Length: 347 Bit Score: 41.28 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1010 QKLQLEKVQLDAKIKKYEEdlalTDDQNQKLLKEKKLLEERANDLSQTLAEEEEKakhlaklkakheatISELEERLHkd 1089
Cdd:pfam10186 29 ARLLSEKDSLKKKVEEALE----GKEEGEQLEDNIGNKKLKLRLLKSEVAISNER--------------LNEIKDKLD-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1090 qQQRQESDRSKRKIETevadLKEQLNERRVQVDEMQAQLAKRE----EELTQTLLRIDEE-SATKATAQKAQRELESQLA 1164
Cdd:pfam10186 89 -QLRREIAEKKKKIEK----LRSSLKQRRSDLESASYQLEERRasqlAKLQNSIKRIKQKwTALHSKTAESRSFLCRELA 163
|
.
gi 62471805 1165 E 1165
Cdd:pfam10186 164 K 164
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1572-1956 |
5.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1572 ELEKAKRALESQLAELKAQNE---ELEDDLQlteDAKLRLEVNMQALRSQ-----FERDLLAKEEGAEEKrrglvKQLRD 1643
Cdd:PRK04863 301 QLAAEQYRLVEMARELAELNEaesDLEQDYQ---AASDHLNLVQTALRQQekierYQADLEELEERLEEQ-----NEVVE 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1644 LETE-LDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKvKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQAlskEAE 1722
Cdd:PRK04863 373 EADEqQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQLCGLPDLTADNAEDWLE---EFQ 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1723 RKVKALEAEVLQLTEDLASSERARRAAEtERDELAEEIAnnankgslmiDEKRRLEAriatleeeleeEQSNSEVLLD-R 1801
Cdd:PRK04863 449 AKEQEATEELLSLEQKLSVAQAAHSQFE-QAYQLVRKIA----------GEVSRSEA-----------WDVARELLRRlR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1802 SRKAQL-QIEQLTTELANEKSNSQKNENGRALLERQNKELKAKLAEIETAQRTKvkatiATLEAKIANLEEQLENEGKER 1880
Cdd:PRK04863 507 EQRHLAeQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQ-----EELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1881 LLQQKANRKMDKKIKELT------MNIEDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMI 1954
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAarapawLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI 661
|
..
gi 62471805 1955 ES 1956
Cdd:PRK04863 662 ER 663
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1640-1782 |
5.69e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1640 QLRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNKVKEDALKHAKKLQAQVKDA------LRDAEEAKAAKEE 1713
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkYEEQLGNVRNNKE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1714 LQALSKE---AERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIAnnankgslmiDEKRRLEARIA 1782
Cdd:COG1579 91 YEALQKEiesLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELE----------EKKAELDEELA 152
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1362-1496 |
5.83e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1362 EAQQLLEEETrQKL-----GLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQMQEIKKKAEEDAdlAKELEEG 1436
Cdd:PRK00409 506 EAKKLIGEDK-EKLneliaSLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEA--QQAIKEA 582
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1437 KKRLNKDIEALERQVKELIAQNDRldKSKKKIQSELEDAtieLEAQRTKVLELEKKQKNF 1496
Cdd:PRK00409 583 KKEADEIIKELRQLQKGGYASVKA--HELIEARKRLNKA---NEKKEKKKKKQKEKQEEL 637
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1076-1305 |
6.20e-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: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1076 EATISELEERLHKDQQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDE-ESATKATAQK 1154
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1155 AQRE----------LESQ----LAEIQEDLEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQelrskreQELA 1220
Cdd:COG3883 95 LYRSggsvsyldvlLGSEsfsdFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALK-------AELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1221 TLKKSLEEETVNHEGVLADMrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQA 1300
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
....*
gi 62471805 1301 ESQIA 1305
Cdd:COG3883 244 ASAAG 248
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1137-1322 |
6.24e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.87 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1137 QTLLRIDeesatKATAQKAQRELESQLAEIQEDLEAEkaarakaekvrRDLSEELEALKNELLDS-LDTTAAQQELRSKR 1215
Cdd:pfam00529 46 DVLFQLD-----PTDYQAALDSAEAQLAKAQAQVARL-----------QAELDRLQALESELAISrQDYDGATAQLRAAQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1216 EQeLATLKKSLEEETVNHEG--VLADMRHKHSQELNSINDQLENlrkAKTVLEKAKGTLEAENADLAtelRSVNSSRQEN 1293
Cdd:pfam00529 110 AA-VKAAQAQLAQAQIDLARrrVLAPIGGISRESLVTAGALVAQ---AQANLLATVAQLDQIYVQIT---QSAAENQAEV 182
|
170 180
....*....|....*....|....*....
gi 62471805 1294 DRRRKQAESQIAELQvklAEIERARSELQ 1322
Cdd:pfam00529 183 RSELSGAQLQIAEAE---AELKLAKLDLE 208
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1493-1974 |
6.33e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.57 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1493 QKNFDKILAEEKAIS--EQIAQERDTAEREAREKETKVLSVSRELDEAF---DKIEDLENKR-------KTLQNELDDLA 1560
Cdd:TIGR00606 172 KQKFDEIFSATRYIKalETLRQVRQTQGQKVQEHQMELKYLKQYKEKACeirDQITSKEAQLessreivKSYENELDPLK 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1561 NTQGTADKNVHELEKakraLESQLAELKAQNEELEDDlqltedaKLRLEVNMQALRSQFERDLLAKEEGAEEKRRGLVKQ 1640
Cdd:TIGR00606 252 NRLKEIEHNLSKIMK----LDNEIKALKSRKKQMEKD-------NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1641 LRDLETELDEERKQRTAAVASKKKLEGDLKEIETTMEMHNK--VKEDALKHAKKLQAQVKDALRDAEEAKAAKEELQALS 1718
Cdd:TIGR00606 321 LVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEhiRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1719 KEAERKVKALEAEVLQLTEDLASSERARRAAETERDELAEEIANNANKGSLMIDEKRRLEARIATLEEELEEEQSNSEVL 1798
Cdd:TIGR00606 401 ERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1799 LDRSRKAQLQIEQLTTELANEKSNSQKNEngRALLERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGK 1878
Cdd:TIGR00606 481 RKAERELSKAEKNSLTETLKKEVKSLQNE--KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1879 ERLLQQKANRKMDKKIKELTMNieDERRHVDQHKEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRKYQRECEDMIESQe 1958
Cdd:TIGR00606 559 SDELTSLLGYFPNKKQLEDWLH--SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQ- 635
|
490
....*....|....*.
gi 62471805 1959 AMNREINSLKTKLRRT 1974
Cdd:TIGR00606 636 DEESDLERLKEEIEKS 651
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1255-1531 |
6.95e-03 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 41.52 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1255 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKlAEIERARSELQEKCTKLQQEAEN 1334
Cdd:TIGR00927 627 LGDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESE-GEIPAERKGEQEGEGEIEAKEAD 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1335 ITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKlglssklrqiESEKEALQEQLEEDDEAKRNYE-RKLAEVT 1413
Cdd:TIGR00927 706 HKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEG----------EGEAEGKHEVETEGDRKETEHEgETEAEGK 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1414 TQMQEIKKKAEEDADLAKELEEGKKRLNKDIEALERQVKELIAQNDRLDKSKKKIQSELEDATIELE---AQRTKVLELE 1490
Cdd:TIGR00927 776 EDEDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGEQELNAENQgeaKQDEKGVDGG 855
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 62471805 1491 KKQKNFDKILAEEKAISEQIAQERDTAEREAREKETKVLSV 1531
Cdd:TIGR00927 856 GGSDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEEPLSL 896
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1060-1343 |
7.07e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1060 EEEEKAKHLAKLKAKHEAT----ISELEeRLHKDQQQRQESDRSkrkiETEVAdlkeqlneRRVQVDEMQAQLAKREEEL 1135
Cdd:pfam17380 354 RQEERKRELERIRQEEIAMeisrMRELE-RLQMERQQKNERVRQ----ELEAA--------RKVKILEEERQRKIQQQKV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1136 TQTLLRIDEESATKATAQKAQRELESQLAEIQEdleaekaarakaekvrrdlsEELEalknelldsldttaAQQELRSKR 1215
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRL--------------------EEQE--------------RQQQVERLR 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1216 EQELATLKKSLEEETVNHEGVLADmrhkhSQELNSINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDR 1295
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAE-----EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEE 541
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 62471805 1296 RRKQAE----SQIAElQVKLAEIERARSELQEKCTKLQQEAENITNQLEEAE 1343
Cdd:pfam17380 542 RRKQQEmeerRRIQE-QMRKATEERSRLEAMEREREMMRQIVESEKARAEYE 592
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1062-1666 |
7.13e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 41.74 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1062 EEKAKHLAKLKAKHEATISELE-------ERLHKDQQQRQESDRskRKIETEVADLKEQLNERRVQVDEmQAQLAKREEE 1134
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRstataesERVRTEAIERATTLR--RQAEETLERTRAEAERLRAEAEE-QAEEVRAAAE 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1135 LTQTLLRIDEESATKATAQKAQRELESQLAEIQEDLEAEKAA----RAKAEKVRRDLSEELEALKNELLDSLDTTAAQQE 1210
Cdd:NF041483 553 RAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEAladaRAEAERIRREAAEETERLRTEAAERIRTLQAQAE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1211 LRSKREQELATLKKSleEETVNHEGVLADMRHKHSQELNSINDQLENlrKAKTVLEKAKGTLEAENADLATELrsvNSSR 1290
Cdd:NF041483 633 QEAERLRTEAAADAS--AARAEGENVAVRLRSEAAAEAERLKSEAQE--SADRVRAEAAAAAERVGTEAAEAL---AAAQ 705
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1291 QENDRRRKQAESQIAELQVKlAEIERARS-----ELQEKCTKLQQEAENITNQL-EEAELKASAAVKSASNMESQLTEAQ 1364
Cdd:NF041483 706 EEAARRRREAEETLGSARAE-ADQERERAreqseELLASARKRVEEAQAEAQRLvEEADRRATELVSAAEQTAQQVRDSV 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1365 QLLEEETRQKL-GLSSKlrqieSEKEALQEQLEEDDEAKRNYERKLAE---VTTQMQEIKKKAEEDADLAKELEegkkrl 1440
Cdd:NF041483 785 AGLQEQAEEEIaGLRSA-----AEHAAERTRTEAQEEADRVRSDAYAErerASEDANRLRREAQEETEAAKALA------ 853
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1441 nkdiealERQVKELIAQNDRL----DKSKKKIQSELED--ATIELEAQRTKVLELEKKQK-------NFDKILAEEKAIS 1507
Cdd:NF041483 854 -------ERTVSEAIAEAERLrsdaSEYAQRVRTEASDtlASAEQDAARTRADAREDANRirsdaaaQADRLIGEATSEA 926
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1508 EQI-AQERDTAEREAREKETKVLSVSRELDEAFDK-IEDLENKRKTLQNEL-DDLANTQGTADKNVHELEKAKRALESQL 1584
Cdd:NF041483 927 ERLtAEARAEAERLRDEARAEAERVRADAAAQAEQlIAEATGEAERLRAEAaETVGSAQQHAERIRTEAERVKAEAAAEA 1006
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1585 AELKAQNEELED---DLQLTEDAKLRLEVNMQAlrsqferDLLAKEEGAEEKRRGLVKQLRDLETELDEERKQRTAAVAS 1661
Cdd:NF041483 1007 ERLRTEAREEADrtlDEARKDANKRRSEAAEQA-------DTLITEAAAEADQLTAKAQEEALRTTTEAEAQADTMVGAA 1079
|
....*
gi 62471805 1662 KKKLE 1666
Cdd:NF041483 1080 RKEAE 1084
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1183-1346 |
7.52e-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: 7.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1183 VRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEetvnhegvLADMRHKHSQELNSI--NDQLENLRK 1260
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE--------VEARIKKYEEQLGNVrnNKEYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1261 AKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQvklAEIERARSELQEKCTKLQQEAENITNQLE 1340
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK---AELDEELAELEAELEELEAEREELAAKIP 173
|
....*.
gi 62471805 1341 EAELKA 1346
Cdd:COG1579 174 PELLAL 179
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1833-1944 |
7.75e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1833 LERQNKELKAKLAEIETAQRTKVKATIATLEAKIANLEEQLEnegkERLLQQKANRKMDKKIKELtmniederrhvdqhK 1912
Cdd:COG0542 416 LERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELE----ALKARWEAEKELIEEIQEL--------------K 477
|
90 100 110
....*....|....*....|....*....|..
gi 62471805 1913 EQMDKLNSRIKLLKRNLDETEEELQKEKTQKR 1944
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1434-1574 |
8.11e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1434 EEGKKRLNKDIEALErqvkELIAqndRLDKSKKKIQSELEDATIELEAQRTKVLELEKKQKNFDKILAEEKAISEQIAQE 1513
Cdd:PRK00409 505 EEAKKLIGEDKEKLN----ELIA---SLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1514 RDTAEREAREKETKVLSVSRELDEAFDKIEDLENKRKTLQNELDDLANTQGTADKNVHELE 1574
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
1337-1425 |
8.12e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 40.29 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1337 NQLEEAELKASAAVKSASnmesqltEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKLAEVTTQM 1416
Cdd:pfam11932 13 ATLDQALDLAEKAVAAAA-------QSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
....*....
gi 62471805 1417 QEIKKKAEE 1425
Cdd:pfam11932 86 EEIERTERE 94
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1090-1433 |
8.19e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1090 QQQRQESDRSKRKIETEVADLKEQLNERRVQVDEMQAQLAKREEELTQTLLRIDEESATKATAQKAQRELESQLAEIQED 1169
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1170 LEAEKAARAKAEKVRRDLSEELEALKNELLDSLDTTAAQQELRSKREQELATLKKSLEEETVNHEgvlADMRHKHSQELN 1249
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ---ALSEAEAEQALD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1250 SINDQLENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRRRKQAESQIAELQVKLAEIERARSELQEKCTKLQ 1329
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1330 QEAENITNQLEEAELKASAAVKSASNMESQLTEAQQLLEEETRQKLGLSSKLRQIESEKEALQEQLEEDDEAKRNYERKL 1409
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|....
gi 62471805 1410 AEVTTQMQEIKKKAEEDADLAKEL 1433
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1684-1971 |
8.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1684 EDALKHAKKLQAQVKDALRDAEEAKAAKEELQALSKEAERKVKALEAEVLQLTEDLASSERARRAAETER---DELAEEI 1760
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1761 ANNANKGSLMIDEKRRLEARIATleeeleeeqsnsevLLDRSRKAQLQIEQLTTELANEKSNSQKNENGRALLERQNKEL 1840
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRE--------------LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1841 KAKlaeietaqrTKVKATIATLEAKIANLEEQLE--NEGKERLlqqkanRKMDKKIKELTMNIED-ERRH-----VDQHK 1912
Cdd:PRK03918 307 DEL---------REIEKRLSRLEEEINGIEERIKelEEKEERL------EELKKKLKELEKRLEElEERHelyeeAKAKK 371
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 62471805 1913 EQMDKLNSRIKllKRNLDETEEELQKEKTQKRKYQRECEDMIESQEAMNREINSLKTKL 1971
Cdd:PRK03918 372 EELERLKKRLT--GLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1152-1390 |
8.31e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1152 AQKAQRELESQLAEIQEDLEAEKAARAkaekvrrdlSEELEALKNELLDSLDttaAQQELRSKREQELATLKKSL---EE 1228
Cdd:cd22656 82 AQNAGGTIDSYYAEILELIDDLADATD---------DEELEEAKKTIKALLD---DLLKEAKKYQDKAAKVVDKLtdfEN 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1229 ETVNHEGVLADMRHKHSQELNSINDQLENLRkaktvLEKAKGTLEAENADLATELRsvnssrqendRRRKQAESQIAELQ 1308
Cdd:cd22656 150 QTEKDQTALETLEKALKDLLTDEGGAIARKE-----IKDLQKELEKLNEEYAAKLK----------AKIDELKALIADDE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1309 VKLAEIERARSELqekcTKLQQEAENITNQLEEAeLKASAAVKSA-SNMESQLTEAQQLLEEETRQKLGLSSKLRQIESE 1387
Cdd:cd22656 215 AKLAAALRLIADL----TAADTDLDNLLALIGPA-IPALEKLQGAwQAIATDLDSLKDLLEDDISKIPAAILAKLELEKA 289
|
...
gi 62471805 1388 KEA 1390
Cdd:cd22656 290 IEK 292
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1849-1938 |
8.67e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1849 TAQRTKVKATIATLEAKIANLEEQLENEGKERLLQQKANRKMDKKIKELTMNIEDERRHVDQHKEQMDKLNSRIKLLKRN 1928
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90
....*....|
gi 62471805 1929 LDETEEELQK 1938
Cdd:COG4942 99 LEAQKEELAE 108
|
|
| AIP3 |
smart00806 |
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in ... |
1816-1961 |
9.08e-03 |
|
Actin interacting protein 3; Aip3p/Bud6p is a regulator of cell and cytoskeletal polarity in Saccharomyces cerevisiae that was previously identified as an actin-interacting protein. Actin-interacting protein 3 (Aip3p) localizes at the cell cortex where cytoskeleton assembly must be achieved to execute polarized cell growth, and deletion of AIP3 causes gross defects in cell and cytoskeletal polarity. Aip3p localization is mediated by the secretory pathway, mutations in early- or late-acting components of the secretory apparatus lead to Aip3p mislocalization.
Pssm-ID: 214826 [Multi-domain] Cd Length: 426 Bit Score: 40.81 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1816 LANEKSNSQKNENGRALLERQNKELK------AKLAEIETAQRTKVKATIATLEAKIANLEEQLENEGKE--RLLQQKAN 1887
Cdd:smart00806 133 LASSSSAISLANNPDKLNKEQRAELKslqrelAVLRQTHNSFFTEIKESIKDILEKIDKFKSSSLSASGSsnRAYVESSK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1888 RKMD-------KKIKELTMNIEDERRHVDQH-----KEQMDKLNSRIKLLKRNLDETEEELQKEKTQKRK-YQRECEDMI 1954
Cdd:smart00806 213 KKLSedsdsllTKVDDLQDIIEALRKDVAQRgvrpsKKQLETVQKELETARKELKKMEEYIDIEKPIWKKiWEAELDKVC 292
|
....*..
gi 62471805 1955 ESQEAMN 1961
Cdd:smart00806 293 EEQQFLT 299
|
|
| DUF4618 |
pfam15397 |
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins ... |
1255-1457 |
9.60e-03 |
|
Domain of unknown function (DUF4618); This family of proteins is found in eukaryotes. Proteins in this family are typically between 238 and 363 amino acids in length. There are two conserved sequence motifs: EYP and KCTPD.
Pssm-ID: 464704 [Multi-domain] Cd Length: 258 Bit Score: 39.94 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1255 LENLRKAKTVLEKAKGTLEAENADLATELRSVNSSRQENDRR--RKQA--ESQIAELQVKLA-EIERARSELQEKCTKLQ 1329
Cdd:pfam15397 1 IRNRRTSLEELKKHEDFLTKLNLELIKAIQDTEDSTALKVRKllQQYEkfGTIISILEYSNKkQLQQAKAELQEWEEKEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62471805 1330 QEAENITNQLEEAELKASAA----------------VKSA--SNMESQLteaQQLLEEETRQKLGLSsklRQIESEKEAL 1391
Cdd:pfam15397 81 SKLNKLEQQLEQLNAKIQKTqeelnflstykdkeypVKAVqiANLVRQL---QQLKDSQQDELDELE---EMRRMVLESL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62471805 1392 QEQLEEDdeaKRNYERKLAEVT-TQMQE-IKKKAEEDADLAKELEEGKK---RLNKDIEALERQVKELIAQ 1457
Cdd:pfam15397 155 SRKIQKK---KEKILSSLAEKTlSPYQEsLLQKTRDNQVMLKEIEQFREfidELEEEIPKLKAEVQQLQAQ 222
|
|
| |
